nebulin isoform X2 [Rattus norvegicus]
Protein Classification
SH3 domain-containing protein; high osmolarity signaling Sho1 family protein( domain architecture ID 12373231)
Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others| high osmolarity signaling Sho1 family protein, similar to yeast Sho1 which is a plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity; contains a Src homology 3 domain
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SH3_Nebulin_C | cd11933 | C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ... |
7462-7519 | 5.78e-35 | ||
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. : Pssm-ID: 212866 [Multi-domain] Cd Length: 58 Bit Score: 129.36 E-value: 5.78e-35
|
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| Nebulin | pfam00880 | Nebulin repeat; |
5129-5156 | 6.69e-05 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 43.15 E-value: 6.69e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4152-4182 | 7.29e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 43.22 E-value: 7.29e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2451-2481 | 9.05e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.84 E-value: 9.05e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
248-278 | 1.11e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.45 E-value: 1.11e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2078-2105 | 1.16e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.16e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
611-638 | 1.23e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.23e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1102-1129 | 1.30e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.30e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4638-4668 | 1.71e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.07 E-value: 1.71e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
858-885 | 2.01e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.61 E-value: 2.01e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1232-1262 | 2.06e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.06e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1267-1297 | 2.30e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.30e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3945-3974 | 2.34e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.34e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1834-1861 | 2.86e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 2.86e-04
|
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| Nebulin | pfam00880 | Nebulin repeat; |
2565-2592 | 3.44e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2808-2835 | 3.44e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3051-3078 | 3.44e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3294-3321 | 3.44e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1756-1785 | 4.85e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.91 E-value: 4.85e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
784-811 | 5.05e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.05e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4266-4293 | 5.91e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.91e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
6789-6815 | 6.08e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 6.08e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3909-3938 | 7.84e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 7.84e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
820-847 | 8.49e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
573-600 | 8.49e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2244-2273 | 8.82e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 8.82e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3780-3807 | 9.65e-04 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 9.65e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1511-1541 | 1.05e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.05e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2491-2518 | 1.11e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.11e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2000-2029 | 1.21e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.21e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6855-6881 | 1.22e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.22e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
888-918 | 1.36e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.36e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1964-1993 | 1.44e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.44e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2322-2349 | 1.46e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.30 E-value: 1.46e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4674-4703 | 1.77e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.77e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
919-948 | 1.86e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.86e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1163-1192 | 1.90e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.90e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2734-2761 | 1.92e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 1.92e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6712-6740 | 1.94e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.94e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
7267-7294 | 2.16e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 2.16e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6602-6632 | 2.26e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 2.26e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1346-1373 | 2.57e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.57e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5584-5611 | 2.63e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.63e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5971-5998 | 2.68e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.68e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3985-4012 | 2.81e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.81e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3423-3453 | 3.19e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 3.19e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
532-562 | 3.52e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.52e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4400-4427 | 3.53e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 3.53e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1476-1506 | 3.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.74e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3603-3630 | 4.08e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4228-4254 | 4.08e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3463-3490 | 4.97e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 4.97e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7134-7159 | 5.27e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.27e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4471-4498 | 5.82e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.82e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1590-1617 | 5.87e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.87e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3180-3210 | 6.29e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.29e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7165-7194 | 6.42e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.42e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4332-4359 | 6.68e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 6.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4188-4217 | 7.30e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.30e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
178-207 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3702-3731 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3220-3247 | 8.05e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 8.05e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7041-7070 | 8.79e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 8.79e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1308-1335 | 8.88e-03 | ||
Nebulin repeat; : Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 8.88e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6176-6206 | 9.89e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. : Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 9.89e-03
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| SH3_Nebulin_C | cd11933 | C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ... |
7462-7519 | 5.78e-35 | ||
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212866 [Multi-domain] Cd Length: 58 Bit Score: 129.36 E-value: 5.78e-35
|
||||||
| SH3 | smart00326 | Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
7462-7517 | 9.16e-14 | ||
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations. Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 69.10 E-value: 9.16e-14
|
||||||
| SH3_9 | pfam14604 | Variant SH3 domain; |
7467-7517 | 2.82e-11 | ||
Variant SH3 domain; Pssm-ID: 434066 [Multi-domain] Cd Length: 49 Bit Score: 61.86 E-value: 2.82e-11
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5129-5156 | 6.69e-05 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 43.15 E-value: 6.69e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4152-4182 | 7.29e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 43.22 E-value: 7.29e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2451-2481 | 9.05e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.84 E-value: 9.05e-05
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
5124-5154 | 1.10e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.45 E-value: 1.10e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
248-278 | 1.11e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.45 E-value: 1.11e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2078-2105 | 1.16e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.16e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
611-638 | 1.23e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.23e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1102-1129 | 1.30e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.30e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2456-2483 | 1.63e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.99 E-value: 1.63e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4638-4668 | 1.71e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.07 E-value: 1.71e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4157-4184 | 1.97e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.61 E-value: 1.97e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
858-885 | 2.01e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.61 E-value: 2.01e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1232-1262 | 2.06e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.06e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1267-1297 | 2.30e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.30e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3945-3974 | 2.34e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.34e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1834-1861 | 2.86e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 2.86e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2565-2592 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2808-2835 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3051-3078 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3294-3321 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1756-1785 | 4.85e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.91 E-value: 4.85e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
784-811 | 5.05e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.05e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4266-4293 | 5.91e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.91e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
6789-6815 | 6.08e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 6.08e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6784-6814 | 7.32e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 7.32e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3909-3938 | 7.84e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 7.84e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3949-3976 | 8.16e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.16e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
820-847 | 8.49e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
573-600 | 8.49e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2244-2273 | 8.82e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 8.82e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3780-3807 | 9.65e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 9.65e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1511-1541 | 1.05e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.05e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4643-4670 | 1.07e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.07e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2491-2518 | 1.11e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.11e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2000-2029 | 1.21e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.21e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6855-6881 | 1.22e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.22e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1760-1787 | 1.27e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
888-918 | 1.36e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.36e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1964-1993 | 1.44e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.44e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2322-2349 | 1.46e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.30 E-value: 1.46e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4674-4703 | 1.77e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.77e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
919-948 | 1.86e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.86e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1163-1192 | 1.90e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.90e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2734-2761 | 1.92e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 1.92e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6712-6740 | 1.94e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.94e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
7267-7294 | 2.16e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 2.16e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6602-6632 | 2.26e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 2.26e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
855-883 | 2.47e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 2.47e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1346-1373 | 2.57e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.57e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5584-5611 | 2.63e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.63e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5971-5998 | 2.68e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2073-2103 | 2.73e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 2.73e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3914-3941 | 2.78e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.78e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3985-4012 | 2.81e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.81e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
779-809 | 3.04e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 3.04e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3423-3453 | 3.19e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 3.19e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
532-562 | 3.52e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.52e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4400-4427 | 3.53e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 3.53e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1476-1506 | 3.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.74e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3603-3630 | 4.08e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4228-4254 | 4.08e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4395-4425 | 4.38e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 4.38e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
537-564 | 4.46e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.46e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
568-598 | 4.69e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 4.69e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
815-845 | 4.69e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 4.69e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2004-2031 | 4.73e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 4.73e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3463-3490 | 4.97e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 4.97e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1097-1127 | 5.07e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.07e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2730-2759 | 5.27e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7134-7159 | 5.27e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1829-1859 | 5.38e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.38e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4471-4498 | 5.82e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.82e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1590-1617 | 5.87e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.87e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2317-2347 | 5.99e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.99e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3180-3210 | 6.29e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.29e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7165-7194 | 6.42e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.42e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4332-4359 | 6.68e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 6.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
608-636 | 6.68e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4188-4217 | 7.30e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.30e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
178-207 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3702-3731 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3220-3247 | 8.05e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 8.05e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
6859-6881 | 8.79e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 8.79e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7041-7070 | 8.79e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 8.79e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1308-1335 | 8.88e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 8.88e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1237-1264 | 9.41e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 9.41e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4678-4705 | 9.70e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 9.70e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6176-6206 | 9.89e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 9.89e-03
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| SH3_Nebulin_C | cd11933 | C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ... |
7462-7519 | 5.78e-35 | ||
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212866 [Multi-domain] Cd Length: 58 Bit Score: 129.36 E-value: 5.78e-35
|
||||||
| SH3_Nebulin_family_C | cd11789 | C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ... |
7465-7518 | 3.56e-32 | ||
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212723 [Multi-domain] Cd Length: 55 Bit Score: 121.27 E-value: 3.56e-32
|
||||||
| SH3_Lasp1_C | cd11934 | C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ... |
7461-7519 | 5.76e-31 | ||
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212867 [Multi-domain] Cd Length: 59 Bit Score: 118.18 E-value: 5.76e-31
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| SH3_Nebulette_C | cd11935 | C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ... |
7463-7519 | 4.23e-28 | ||
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212868 [Multi-domain] Cd Length: 58 Bit Score: 110.09 E-value: 4.23e-28
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| SH3_Abp1_eu | cd11960 | Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ... |
7466-7517 | 3.63e-14 | ||
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212893 [Multi-domain] Cd Length: 54 Bit Score: 70.12 E-value: 3.63e-14
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| SH3 | smart00326 | Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
7462-7517 | 9.16e-14 | ||
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations. Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 69.10 E-value: 9.16e-14
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| SH3_Cortactin_like | cd11819 | Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ... |
7466-7517 | 5.37e-13 | ||
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212753 [Multi-domain] Cd Length: 54 Bit Score: 66.95 E-value: 5.37e-13
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| SH3_Cortactin | cd11959 | Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src ... |
7467-7518 | 2.94e-12 | ||
Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src kinase. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion. It is expressed ubiquitously except in hematopoietic cells, where the homolog hematopoietic lineage cell-specific 1 (HS1) is expressed instead. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212892 [Multi-domain] Cd Length: 53 Bit Score: 64.75 E-value: 2.94e-12
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| SH3 | cd00174 | Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
7464-7515 | 1.13e-11 | ||
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction. Pssm-ID: 212690 [Multi-domain] Cd Length: 51 Bit Score: 62.87 E-value: 1.13e-11
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| SH3_9 | pfam14604 | Variant SH3 domain; |
7467-7517 | 2.82e-11 | ||
Variant SH3 domain; Pssm-ID: 434066 [Multi-domain] Cd Length: 49 Bit Score: 61.86 E-value: 2.82e-11
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| SH3_PACSIN | cd11843 | Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ... |
7465-7517 | 5.50e-11 | ||
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212777 [Multi-domain] Cd Length: 53 Bit Score: 60.90 E-value: 5.50e-11
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| SH3_GRAF-like | cd11882 | Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ... |
7466-7517 | 1.88e-10 | ||
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212815 [Multi-domain] Cd Length: 54 Bit Score: 59.61 E-value: 1.88e-10
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| SH3_Abp1_fungi_C2 | cd11961 | Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ... |
7466-7517 | 1.99e-10 | ||
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212894 [Multi-domain] Cd Length: 53 Bit Score: 59.46 E-value: 1.99e-10
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| SH3_Sorbs_3 | cd11780 | Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) ... |
7464-7518 | 2.65e-10 | ||
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212714 [Multi-domain] Cd Length: 55 Bit Score: 59.24 E-value: 2.65e-10
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| SH3_HS1 | cd12073 | Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 ... |
7467-7517 | 4.91e-10 | ||
Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 (hematopoietic cell-specific Lyn substrate 1), is a cortactin homolog expressed specifically in hematopoietic cells. It is an actin regulatory protein that binds the Arp2/3 complex and stabilizes branched actin filaments. It is required for cell spreading and signaling in lymphocytes. It regulates cytoskeletal remodeling that controls lymphocyte trafficking, and it also affects tissue invasion and infiltration of leukemic B cells. Like cortactin, HS1 contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region binds the Arp2/3 complex and F-actin, while the C-terminal region acts as an adaptor or scaffold that can connect varied proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 213006 [Multi-domain] Cd Length: 55 Bit Score: 58.30 E-value: 4.91e-10
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| SH3_PIX | cd11877 | Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ... |
7466-7517 | 7.59e-10 | ||
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212810 [Multi-domain] Cd Length: 53 Bit Score: 57.71 E-value: 7.59e-10
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| SH3_PACSIN_like | cd11999 | Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ... |
7462-7517 | 9.46e-10 | ||
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212932 [Multi-domain] Cd Length: 56 Bit Score: 57.64 E-value: 9.46e-10
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| SH3_PACSIN3 | cd11997 | Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ... |
7466-7517 | 1.06e-09 | ||
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212930 [Multi-domain] Cd Length: 56 Bit Score: 57.66 E-value: 1.06e-09
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| SH3_UBASH3 | cd11791 | Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ... |
7466-7517 | 1.34e-09 | ||
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins; UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212725 [Multi-domain] Cd Length: 59 Bit Score: 57.31 E-value: 1.34e-09
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| SH3_OSTF1 | cd11772 | Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ... |
7464-7518 | 2.04e-09 | ||
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212706 [Multi-domain] Cd Length: 53 Bit Score: 56.54 E-value: 2.04e-09
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| SH3_Amphiphysin | cd11790 | Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ... |
7466-7519 | 3.93e-09 | ||
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212724 [Multi-domain] Cd Length: 64 Bit Score: 56.18 E-value: 3.93e-09
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| SH3_CD2AP-like_1 | cd11873 | First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ... |
7465-7517 | 6.06e-09 | ||
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212806 [Multi-domain] Cd Length: 53 Bit Score: 55.35 E-value: 6.06e-09
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| SH3_Endophilin_A | cd11803 | Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ... |
7466-7519 | 7.01e-09 | ||
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212737 [Multi-domain] Cd Length: 55 Bit Score: 54.96 E-value: 7.01e-09
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| SH3_PACSIN1-2 | cd11998 | Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ... |
7466-7518 | 8.91e-09 | ||
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212931 [Multi-domain] Cd Length: 56 Bit Score: 54.96 E-value: 8.91e-09
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| SH3_Nostrin | cd11823 | Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ... |
7466-7517 | 1.06e-08 | ||
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212757 [Multi-domain] Cd Length: 53 Bit Score: 54.66 E-value: 1.06e-08
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| SH3_Sorbs2_3 | cd11917 | Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), ... |
7460-7517 | 1.11e-08 | ||
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212850 [Multi-domain] Cd Length: 61 Bit Score: 55.00 E-value: 1.11e-08
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| SH3_Intersectin_1 | cd11836 | First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ... |
7465-7518 | 1.12e-08 | ||
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212770 [Multi-domain] Cd Length: 55 Bit Score: 54.67 E-value: 1.12e-08
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| SH3_Sorbs1_3 | cd11916 | Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), ... |
7465-7519 | 2.31e-08 | ||
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212849 [Multi-domain] Cd Length: 59 Bit Score: 53.84 E-value: 2.31e-08
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| SH3_SH3RF_1 | cd11786 | First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ... |
7466-7517 | 2.72e-08 | ||
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212720 [Multi-domain] Cd Length: 53 Bit Score: 53.52 E-value: 2.72e-08
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| SH3_Eve1_5 | cd11818 | Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ... |
7466-7515 | 3.81e-08 | ||
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212752 [Multi-domain] Cd Length: 50 Bit Score: 52.87 E-value: 3.81e-08
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| SH3_1 | pfam00018 | SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ... |
7466-7513 | 4.25e-08 | ||
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel. Pssm-ID: 394975 [Multi-domain] Cd Length: 47 Bit Score: 52.59 E-value: 4.25e-08
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| SH3_Vinexin_3 | cd11918 | Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain ... |
7465-7519 | 4.43e-08 | ||
Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212851 [Multi-domain] Cd Length: 58 Bit Score: 53.04 E-value: 4.43e-08
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| SH3_MyoIe_If_like | cd11827 | Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ... |
7466-7517 | 5.62e-08 | ||
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212761 [Multi-domain] Cd Length: 53 Bit Score: 52.42 E-value: 5.62e-08
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| SH3_CD2AP-like_3 | cd11875 | Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ... |
7466-7517 | 8.89e-08 | ||
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212808 [Multi-domain] Cd Length: 55 Bit Score: 51.97 E-value: 8.89e-08
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| SH3_Sorbs_1 | cd11781 | First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ... |
7466-7517 | 1.83e-07 | ||
First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the first SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212715 [Multi-domain] Cd Length: 53 Bit Score: 51.19 E-value: 1.83e-07
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| SH3_Abi | cd11826 | Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ... |
7466-7517 | 2.44e-07 | ||
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212760 [Multi-domain] Cd Length: 52 Bit Score: 50.78 E-value: 2.44e-07
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| SH3_SH3RF_C | cd11785 | C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ... |
7465-7517 | 2.58e-07 | ||
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the fourth SH3 domain, located at the C-terminus of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212719 Cd Length: 55 Bit Score: 50.93 E-value: 2.58e-07
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| SH3_GRB2_like_C | cd11805 | C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ... |
7466-7517 | 8.25e-07 | ||
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212739 [Multi-domain] Cd Length: 53 Bit Score: 49.16 E-value: 8.25e-07
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| SH3_RasGAP | cd11788 | Src Homology 3 domain of Ras GTPase-Activating Protein 1; RasGAP, also called Ras p21 protein ... |
7466-7519 | 1.22e-06 | ||
Src Homology 3 domain of Ras GTPase-Activating Protein 1; RasGAP, also called Ras p21 protein activator, RASA1, or p120RasGAP, is part of the GAP1 family of GTPase-activating proteins. It is a 120kD cytosolic protein containing an SH3 domain flanked by two SH2 domains at the N-terminal end, a pleckstrin homology (PH) domain, a calcium dependent phospholipid binding domain (CaLB/C2), and a C-terminal catalytic GAP domain. It stimulates the GTPase activity of normal RAS p21. It acts as a positive effector of Ras in tumor cells. It also functions as a regulator downstream of tyrosine receptors such as those of PDGF, EGF, ephrin, and insulin, among others. The SH3 domain of RasGAP is unable to bind proline-rich sequences but have been shown to interact with protein partners such as the G3BP protein, Aurora kinases, and the Calpain small subunit 1. The RasGAP SH3 domain is necessary for the downstream signaling of Ras and it also influences Rho-mediated cytoskeletal reorganization. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212722 Cd Length: 59 Bit Score: 48.91 E-value: 1.22e-06
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| SH3_UBASH3A | cd11937 | Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ... |
7463-7517 | 1.23e-06 | ||
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212870 [Multi-domain] Cd Length: 60 Bit Score: 48.86 E-value: 1.23e-06
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| SH3_MYO15 | cd11884 | Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ... |
7466-7518 | 1.23e-06 | ||
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212817 [Multi-domain] Cd Length: 56 Bit Score: 48.86 E-value: 1.23e-06
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| SH3_Sorbs2_1 | cd11920 | First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called ... |
7466-7519 | 1.53e-06 | ||
First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212853 [Multi-domain] Cd Length: 55 Bit Score: 48.47 E-value: 1.53e-06
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| SH3_UBASH3B | cd11936 | Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, ... |
7465-7516 | 1.72e-06 | ||
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, also called Suppressor of T cell receptor Signaling (STS)-1 or T cell Ubiquitin LigAnd (TULA)-2 is an active phosphatase that is expressed ubiquitously. The phosphatase activity of UBASH3B is essential for its roles in the suppression of TCR signaling and the regulation of EGFR. It also interacts with Syk and functions as a negative regulator of platelet glycoprotein VI signaling. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212869 Cd Length: 62 Bit Score: 48.50 E-value: 1.72e-06
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| SH3_PSTPIP1 | cd11824 | Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ... |
7465-7517 | 2.24e-06 | ||
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212758 [Multi-domain] Cd Length: 53 Bit Score: 48.14 E-value: 2.24e-06
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| SH3_ASAP | cd11821 | Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing ... |
7466-7515 | 2.38e-06 | ||
Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing proteins; ASAPs are Arf GTPase activating proteins (GAPs) and they function in regulating cell growth, migration, and invasion. They contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3, but some ASAP3 proteins do not seem to harbor a C-terminal SH3 domain. ASAP1 and ASAP2 show GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but are able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212755 [Multi-domain] Cd Length: 53 Bit Score: 48.08 E-value: 2.38e-06
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| SH3_MLK4 | cd12058 | Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), ... |
7464-7516 | 2.52e-06 | ||
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. MLK4 contains an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212991 [Multi-domain] Cd Length: 58 Bit Score: 48.01 E-value: 2.52e-06
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| SH3_betaPIX | cd12061 | Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho ... |
7464-7519 | 3.10e-06 | ||
Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7) or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212994 [Multi-domain] Cd Length: 54 Bit Score: 47.76 E-value: 3.10e-06
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| SH3_Sla1p_3 | cd11775 | Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ... |
7463-7517 | 3.11e-06 | ||
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212709 [Multi-domain] Cd Length: 57 Bit Score: 47.70 E-value: 3.11e-06
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| SH3_SH3RF2_3 | cd11784 | Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ... |
7464-7516 | 3.60e-06 | ||
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212718 Cd Length: 55 Bit Score: 47.46 E-value: 3.60e-06
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| SH3_Intersectin2_1 | cd11988 | First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ... |
7465-7517 | 4.86e-06 | ||
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212921 [Multi-domain] Cd Length: 57 Bit Score: 47.17 E-value: 4.86e-06
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| SH3_SNX9_like | cd11763 | Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ... |
7466-7517 | 6.95e-06 | ||
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212697 [Multi-domain] Cd Length: 55 Bit Score: 46.55 E-value: 6.95e-06
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| SH3_Abi1 | cd11971 | Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ... |
7467-7519 | 7.19e-06 | ||
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of actin cytoskeletal reorganization through interactions with many protein complexes. It is part of WAVE, a nucleation-promoting factor complex, that links Rac 1 activation to actin polymerization causing lamellipodia protrusion at the plasma membrane. Abi1 interact with formins to promote protrusions at the leading edge of motile cells. It also is a target of alpha4 integrin, regulating membrane protrusions at sites of integrin engagement. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212904 [Multi-domain] Cd Length: 59 Bit Score: 46.94 E-value: 7.19e-06
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| SH3_PEX13_eumet | cd11864 | Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and ... |
7466-7517 | 7.66e-06 | ||
Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and is required for protein import into the peroxisomal matrix and membrane. It is an integral membrane protein that is essential for the localization of PEX14 and the import of proteins containing the peroxisome matrix targeting signals, PTS1 and PTS2. Mutations of the PEX13 gene in humans lead to a wide range of peroxisome biogenesis disorders (PBDs), the most severe of which is known as Zellweger syndrome (ZS), a severe multisystem disorder characterized by hypotonia, psychomotor retardation, and neuronal migration defects. PEX13 contains two transmembrane regions and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212798 Cd Length: 58 Bit Score: 46.47 E-value: 7.66e-06
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| SH3_Abi2 | cd11972 | Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ... |
7467-7519 | 9.03e-06 | ||
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It regulates actin cytoskeletal reorganization at adherens junctions and dendritic spines, which is important in cell morphogenesis, migration, and cognitive function. Mice deficient with Abi2 show defects in orientation and migration of lens fibers, neuronal migration, dendritic spine morphology, as well as deficits in learning and memory. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212905 [Multi-domain] Cd Length: 61 Bit Score: 46.54 E-value: 9.03e-06
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| SH3_Irsp53_BAIAP2L | cd11779 | Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ... |
7466-7518 | 1.08e-05 | ||
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212713 [Multi-domain] Cd Length: 57 Bit Score: 46.16 E-value: 1.08e-05
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| SH3_STAM | cd11820 | Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ... |
7466-7518 | 1.74e-05 | ||
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212754 [Multi-domain] Cd Length: 54 Bit Score: 45.53 E-value: 1.74e-05
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| SH3_Bzz1_2 | cd11778 | Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ... |
7467-7515 | 1.77e-05 | ||
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212712 [Multi-domain] Cd Length: 51 Bit Score: 45.57 E-value: 1.77e-05
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| SH3_Abp1_fungi_C1 | cd11962 | First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ... |
7468-7517 | 2.01e-05 | ||
First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212895 [Multi-domain] Cd Length: 54 Bit Score: 45.56 E-value: 2.01e-05
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| SH3_Intersectin1_1 | cd11987 | First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ... |
7465-7517 | 2.07e-05 | ||
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212920 [Multi-domain] Cd Length: 55 Bit Score: 45.38 E-value: 2.07e-05
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| SH3_CSK | cd11769 | Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr ... |
7467-7517 | 2.30e-05 | ||
Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, CSK is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. CSK catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. It is expressed in a wide variety of tissues and plays a role, as a regulator of Src, in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. In addition, CSK also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212703 [Multi-domain] Cd Length: 57 Bit Score: 45.37 E-value: 2.30e-05
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| SH3_Pex13p_fungal | cd11771 | Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ... |
7466-7517 | 2.62e-05 | ||
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212705 [Multi-domain] Cd Length: 60 Bit Score: 45.34 E-value: 2.62e-05
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| SH3_VAV1_2 | cd11976 | C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ... |
7466-7517 | 3.43e-05 | ||
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212909 [Multi-domain] Cd Length: 54 Bit Score: 44.55 E-value: 3.43e-05
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| SH3_alphaPIX | cd12060 | Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho ... |
7464-7519 | 3.55e-05 | ||
Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6) or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212993 Cd Length: 58 Bit Score: 44.99 E-value: 3.55e-05
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| SH3_Eve1_4 | cd11817 | Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ... |
7467-7515 | 3.66e-05 | ||
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212751 [Multi-domain] Cd Length: 50 Bit Score: 44.39 E-value: 3.66e-05
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| SH3_CD2AP_2 | cd12054 | Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ... |
7466-7519 | 3.74e-05 | ||
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212987 [Multi-domain] Cd Length: 55 Bit Score: 44.57 E-value: 3.74e-05
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| SH3_SNX18 | cd11897 | Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal ... |
7466-7517 | 3.90e-05 | ||
Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. It binds FIP5 and is required for apical lumen formation. It may also play a role in axonal elongation. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX18 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212830 [Multi-domain] Cd Length: 55 Bit Score: 44.60 E-value: 3.90e-05
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| SH3_STAM1 | cd11964 | Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ... |
7466-7518 | 4.06e-05 | ||
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212897 [Multi-domain] Cd Length: 55 Bit Score: 44.55 E-value: 4.06e-05
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| SH3_SH3RF1_3 | cd11926 | Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ... |
7464-7516 | 4.73e-05 | ||
Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212859 [Multi-domain] Cd Length: 55 Bit Score: 44.19 E-value: 4.73e-05
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| SH3_D21-like | cd12142 | Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ... |
7466-7517 | 4.82e-05 | ||
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 213018 [Multi-domain] Cd Length: 55 Bit Score: 44.38 E-value: 4.82e-05
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| SH3_GRB2_C | cd11949 | C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ... |
7466-7518 | 4.91e-05 | ||
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212882 [Multi-domain] Cd Length: 53 Bit Score: 44.06 E-value: 4.91e-05
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| SH3_Yes | cd12007 | Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src ... |
7464-7516 | 5.40e-05 | ||
Src homology 3 domain of Yes Protein Tyrosine Kinase; Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212940 [Multi-domain] Cd Length: 58 Bit Score: 44.25 E-value: 5.40e-05
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| SH3_Intersectin2_5 | cd11996 | Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ... |
7467-7517 | 6.38e-05 | ||
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212929 [Multi-domain] Cd Length: 54 Bit Score: 43.82 E-value: 6.38e-05
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| Nebulin | pfam00880 | Nebulin repeat; |
5129-5156 | 6.69e-05 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 43.15 E-value: 6.69e-05
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4152-4182 | 7.29e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 43.22 E-value: 7.29e-05
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| SH3_Sorbs1_2 | cd11922 | Second Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ... |
7467-7519 | 8.32e-05 | ||
Second Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212855 [Multi-domain] Cd Length: 58 Bit Score: 43.83 E-value: 8.32e-05
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2451-2481 | 9.05e-05 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.84 E-value: 9.05e-05
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| SH3_MLK | cd11876 | Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ... |
7467-7516 | 9.37e-05 | ||
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212809 [Multi-domain] Cd Length: 58 Bit Score: 43.66 E-value: 9.37e-05
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| SH3_CD2AP-like_2 | cd11874 | Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ... |
7466-7517 | 9.68e-05 | ||
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212807 [Multi-domain] Cd Length: 53 Bit Score: 43.48 E-value: 9.68e-05
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| SH3_CIN85_3 | cd12057 | Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ... |
7466-7517 | 9.85e-05 | ||
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212990 [Multi-domain] Cd Length: 56 Bit Score: 43.35 E-value: 9.85e-05
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| SH3_SH3RF3_3 | cd11925 | Third Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ... |
7464-7519 | 1.01e-04 | ||
Third Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212858 Cd Length: 57 Bit Score: 43.45 E-value: 1.01e-04
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| SH3_Eve1_3 | cd11816 | Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ... |
7466-7516 | 1.05e-04 | ||
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212750 [Multi-domain] Cd Length: 51 Bit Score: 43.16 E-value: 1.05e-04
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| SH3_p47phox_like | cd11856 | Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ... |
7464-7517 | 1.06e-04 | ||
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212790 [Multi-domain] Cd Length: 53 Bit Score: 43.39 E-value: 1.06e-04
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| SH3_FCHSD_2 | cd11762 | Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ... |
7466-7517 | 1.08e-04 | ||
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212696 [Multi-domain] Cd Length: 57 Bit Score: 43.54 E-value: 1.08e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
5124-5154 | 1.10e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.45 E-value: 1.10e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
248-278 | 1.11e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.45 E-value: 1.11e-04
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| SH3_SPIN90 | cd11849 | Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ... |
7465-7517 | 1.14e-04 | ||
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212783 [Multi-domain] Cd Length: 53 Bit Score: 43.07 E-value: 1.14e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
2078-2105 | 1.16e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.16e-04
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| SH3_Src_like | cd11845 | Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ... |
7464-7515 | 1.17e-04 | ||
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212779 [Multi-domain] Cd Length: 52 Bit Score: 42.95 E-value: 1.17e-04
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| SH3_GRAP2_C | cd11950 | C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ... |
7466-7517 | 1.22e-04 | ||
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212883 [Multi-domain] Cd Length: 53 Bit Score: 43.28 E-value: 1.22e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
611-638 | 1.23e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.23e-04
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| SH3_PLCgamma | cd11825 | Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of ... |
7466-7517 | 1.23e-04 | ||
Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG) in response to various receptors. Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma catalyzes this reaction in tyrosine kinase-dependent signaling pathways. It is activated and recruited to its substrate at the membrane. Vertebrates contain two forms of PLCgamma, PLCgamma1, which is widely expressed, and PLCgamma2, which is primarily found in haematopoietic cells. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212759 [Multi-domain] Cd Length: 54 Bit Score: 43.09 E-value: 1.23e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
1102-1129 | 1.30e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 42.38 E-value: 1.30e-04
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| SH3_Sorbs_2 | cd11782 | Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ... |
7466-7517 | 1.31e-04 | ||
Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the second SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212716 [Multi-domain] Cd Length: 53 Bit Score: 43.11 E-value: 1.31e-04
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| SH3_CRK_N | cd11758 | N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ... |
7466-7518 | 1.32e-04 | ||
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212692 [Multi-domain] Cd Length: 55 Bit Score: 43.12 E-value: 1.32e-04
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| SH3_GRAP_C | cd11951 | C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ... |
7466-7516 | 1.36e-04 | ||
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212884 Cd Length: 53 Bit Score: 42.87 E-value: 1.36e-04
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| SH3_SH3RF_3 | cd11783 | Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ... |
7464-7518 | 1.43e-04 | ||
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212717 [Multi-domain] Cd Length: 55 Bit Score: 43.15 E-value: 1.43e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
2456-2483 | 1.63e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.99 E-value: 1.63e-04
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| SH3_VAV_2 | cd11830 | C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ... |
7467-7517 | 1.64e-04 | ||
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212764 [Multi-domain] Cd Length: 54 Bit Score: 43.00 E-value: 1.64e-04
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| SH3_ephexin1_like | cd11793 | Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange ... |
7467-7518 | 1.70e-04 | ||
Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors; Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212727 [Multi-domain] Cd Length: 55 Bit Score: 42.71 E-value: 1.70e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4638-4668 | 1.71e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 42.07 E-value: 1.71e-04
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| SH3_Vinexin_2 | cd11924 | Second Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 ... |
7467-7517 | 1.71e-04 | ||
Second Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212857 Cd Length: 56 Bit Score: 42.64 E-value: 1.71e-04
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| SH3_CD2AP_1 | cd12053 | First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ... |
7469-7519 | 1.88e-04 | ||
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212986 Cd Length: 56 Bit Score: 42.52 E-value: 1.88e-04
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| SH3_Sorbs2_2 | cd11923 | Second Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called ... |
7467-7519 | 1.91e-04 | ||
Second Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212856 [Multi-domain] Cd Length: 57 Bit Score: 42.60 E-value: 1.91e-04
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| SH3_Intersectin_5 | cd11840 | Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ... |
7466-7517 | 1.93e-04 | ||
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212774 [Multi-domain] Cd Length: 53 Bit Score: 42.40 E-value: 1.93e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
4157-4184 | 1.97e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.61 E-value: 1.97e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
858-885 | 2.01e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.61 E-value: 2.01e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1232-1262 | 2.06e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.06e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1267-1297 | 2.30e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.30e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3945-3974 | 2.34e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 41.68 E-value: 2.34e-04
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| SH3_CIN85_2 | cd12055 | Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ... |
7466-7517 | 2.48e-04 | ||
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212988 [Multi-domain] Cd Length: 53 Bit Score: 42.29 E-value: 2.48e-04
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| SH3_ARHGEF16_26 | cd11938 | Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ... |
7465-7513 | 2.51e-04 | ||
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ARHGEF16, also called ephexin-4, acts as a GEF for RhoG, activating it by exchanging bound GDP for free GTP. RhoG is a small GTPase that is a crucial regulator of Rac in migrating cells. ARHGEF16 interacts directly with the ephrin receptor EphA2 and mediates cell migration and invasion in breast cancer cells by activating RhoG. ARHGEF26, also called SGEF (SH3 domain-containing guanine exchange factor), also activates RhoG. It is highly expressed in liver and may play a role in regulating membrane dynamics. ARHGEF16 and ARHGEF26 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212871 Cd Length: 55 Bit Score: 42.14 E-value: 2.51e-04
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| SH3_SH3RF3_1 | cd11928 | First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ... |
7466-7517 | 2.66e-04 | ||
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212861 Cd Length: 54 Bit Score: 42.22 E-value: 2.66e-04
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| SH3_STAM2 | cd11963 | Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ... |
7466-7516 | 2.77e-04 | ||
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212896 [Multi-domain] Cd Length: 57 Bit Score: 42.31 E-value: 2.77e-04
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| SH3_PRMT2 | cd11806 | Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, ... |
7464-7516 | 2.85e-04 | ||
Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, belongs to the arginine methyltransferase protein family. It functions as a coactivator to both estrogen receptor alpha (ER-alpha) and androgen receptor (AR), presumably through arginine methylation. The ER-alpha transcription factor is involved in cell proliferation, differentiation, morphogenesis, and apoptosis, and is also implicated in the development and progression of breast cancer. PRMT2 and its variants are upregulated in breast cancer cells and may be involved in modulating the ER-alpha signaling pathway during formation of breast cancer. PRMT2 also plays a role in regulating the function of E2F transcription factors, which are critical cell cycle regulators, by binding to the retinoblastoma gene product (RB). It contains an N-terminal SH3 domain and an AdoMet binding domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212740 [Multi-domain] Cd Length: 53 Bit Score: 41.99 E-value: 2.85e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
1834-1861 | 2.86e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 2.86e-04
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| SH3_Fyn_Yrk | cd12006 | Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) ... |
7464-7516 | 2.88e-04 | ||
Src homology 3 domain of Fyn and Yrk Protein Tyrosine Kinases; Fyn and Yrk (Yes-related kinase) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212939 [Multi-domain] Cd Length: 56 Bit Score: 42.34 E-value: 2.88e-04
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| SH3_CIN85_1 | cd12052 | First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ... |
7469-7516 | 3.00e-04 | ||
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212985 [Multi-domain] Cd Length: 53 Bit Score: 42.19 E-value: 3.00e-04
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| SH3_Bem1p_1 | cd11878 | First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this ... |
7464-7515 | 3.17e-04 | ||
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212811 [Multi-domain] Cd Length: 54 Bit Score: 41.89 E-value: 3.17e-04
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| SH3_GRAF3 | cd12066 | Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 3; GRAF3 is ... |
7466-7517 | 3.39e-04 | ||
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 3; GRAF3 is also called Rho GTPase activating protein 42 (ARHGAP42) or ARHGAP10-like. Though its function has not been characterized, it may be a GAP with activity towards RhoA and Cdc42, based on its similarity to GRAF and GRAF2. It contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212999 Cd Length: 55 Bit Score: 41.97 E-value: 3.39e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
2565-2592 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
2808-2835 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
3051-3078 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
3294-3321 | 3.44e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 41.22 E-value: 3.44e-04
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| SH3_Nck_2 | cd11766 | Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ... |
7464-7517 | 4.06e-04 | ||
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212700 [Multi-domain] Cd Length: 53 Bit Score: 41.48 E-value: 4.06e-04
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| SH3_MLK1-3 | cd12059 | Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ... |
7467-7516 | 4.29e-04 | ||
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212992 [Multi-domain] Cd Length: 58 Bit Score: 41.68 E-value: 4.29e-04
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| SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
7465-7517 | 4.58e-04 | ||
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel. Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 41.43 E-value: 4.58e-04
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| SH3_AHI-1 | cd11812 | Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ... |
7467-7516 | 4.70e-04 | ||
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212746 [Multi-domain] Cd Length: 52 Bit Score: 41.34 E-value: 4.70e-04
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| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1756-1785 | 4.85e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.91 E-value: 4.85e-04
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| Nebulin | pfam00880 | Nebulin repeat; |
784-811 | 5.05e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.05e-04
|
||||||
| SH3_ARHGEF9_like | cd11828 | Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ... |
7467-7516 | 5.55e-04 | ||
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212762 [Multi-domain] Cd Length: 53 Bit Score: 41.21 E-value: 5.55e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4266-4293 | 5.91e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 5.91e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
6789-6815 | 6.08e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.45 E-value: 6.08e-04
|
||||||
| SH3_GRAP_N | cd11948 | N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ... |
7467-7517 | 6.47e-04 | ||
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212881 [Multi-domain] Cd Length: 54 Bit Score: 40.95 E-value: 6.47e-04
|
||||||
| SH3_BOI | cd11886 | Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ... |
7464-7515 | 6.60e-04 | ||
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces cerevisiae proteins BOI1 and BOI2, and similar proteins. They contain an N-terminal SH3 domain, a Sterile alpha motif (SAM), and a Pleckstrin homology (PH) domain at the C-terminus. BOI1 and BOI2 interact with the SH3 domain of Bem1p, a protein involved in bud formation. They promote polarized cell growth and participates in the NoCut signaling pathway, which is involved in the control of cytokinesis. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212819 Cd Length: 55 Bit Score: 41.16 E-value: 6.60e-04
|
||||||
| SH3_Sho1p | cd11855 | Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called ... |
7466-7517 | 6.99e-04 | ||
Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called SSU81 (Suppressor of SUA8-1 mutation), is a yeast membrane protein that regulates adaptation to high salt conditions by activating the HOG (high-osmolarity glycerol) pathway. High salt concentrations lead to the localization to the membrane of the MAPKK Pbs2, which is then activated by the MAPKK Ste11 and in turn, activates the MAPK Hog1. Pbs2 is localized to the membrane though the interaction of its PxxP motif with the SH3 domain of Sho1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212789 [Multi-domain] Cd Length: 55 Bit Score: 40.87 E-value: 6.99e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6784-6814 | 7.32e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 7.32e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3909-3938 | 7.84e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 7.84e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3949-3976 | 8.16e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.16e-04
|
||||||
| SH3_Sorbs1_1 | cd11919 | First Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; ... |
7466-7519 | 8.46e-04 | ||
First Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212852 [Multi-domain] Cd Length: 55 Bit Score: 40.72 E-value: 8.46e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
820-847 | 8.49e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
573-600 | 8.49e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 40.07 E-value: 8.49e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2244-2273 | 8.82e-04 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 40.14 E-value: 8.82e-04
|
||||||
| SH3_SNX33 | cd11896 | Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome ... |
7466-7517 | 8.99e-04 | ||
Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX33 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212829 [Multi-domain] Cd Length: 55 Bit Score: 40.71 E-value: 8.99e-04
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3780-3807 | 9.65e-04 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 9.65e-04
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1511-1541 | 1.05e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.05e-03
|
||||||
| SH3_DNMBP_N3 | cd11796 | Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ... |
7466-7516 | 1.07e-03 | ||
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212730 Cd Length: 51 Bit Score: 40.42 E-value: 1.07e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4643-4670 | 1.07e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.07e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2491-2518 | 1.11e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.11e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2000-2029 | 1.21e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.21e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6855-6881 | 1.22e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.76 E-value: 1.22e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1760-1787 | 1.27e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.68 E-value: 1.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
888-918 | 1.36e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.36e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1964-1993 | 1.44e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 39.37 E-value: 1.44e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2322-2349 | 1.46e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 39.30 E-value: 1.46e-03
|
||||||
| SH3_Bzz1_1 | cd11912 | First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ... |
7466-7517 | 1.76e-03 | ||
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212845 [Multi-domain] Cd Length: 55 Bit Score: 39.90 E-value: 1.76e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4674-4703 | 1.77e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.77e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
919-948 | 1.86e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.86e-03
|
||||||
| SH3_iASPP | cd11952 | Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called ... |
7467-7515 | 1.88e-03 | ||
Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called RelA-associated inhibitor (RAI), is an oncoprotein that inhibits the apoptotic transactivation potential of p53. It is upregulated in human breast cancers expressing wild-type p53, in acute leukemias regardless of the p53 mutation status, as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212885 [Multi-domain] Cd Length: 56 Bit Score: 39.91 E-value: 1.88e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1163-1192 | 1.90e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.90e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2734-2761 | 1.92e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 1.92e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6712-6740 | 1.94e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 1.94e-03
|
||||||
| SH3_GRAF | cd12064 | Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase; GRAF, also ... |
7466-7517 | 1.99e-03 | ||
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase; GRAF, also called Rho GTPase activating protein 26 (ARHGAP26), Oligophrenin-1-like (OPHN1L) or GRAF1, is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. It is essential for the major clathrin-independent endocytic pathway mediated by pleiomorphic membranes. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212997 Cd Length: 56 Bit Score: 39.71 E-value: 1.99e-03
|
||||||
| SH3_p40phox | cd11869 | Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil ... |
7467-7519 | 2.07e-03 | ||
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil cytosol factor 4 (NCF-4), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. It contains an N-terminal PX domain, a central SH3 domain, and a C-terminal PB1 domain that interacts with p67phox. The SH3 domain of p40phox binds to canonical polyproline and noncanonical motifs at the C-terminus of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212802 Cd Length: 54 Bit Score: 39.78 E-value: 2.07e-03
|
||||||
| SH3_Vinexin_1 | cd11921 | First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3) ... |
7466-7519 | 2.11e-03 | ||
First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212854 Cd Length: 55 Bit Score: 39.91 E-value: 2.11e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
7267-7294 | 2.16e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.91 E-value: 2.16e-03
|
||||||
| SH3_SH3TC | cd11885 | Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins ... |
7465-7516 | 2.24e-03 | ||
Src Homology 3 domain of SH3 domain and tetratricopeptide repeat-containing (SH3TC) proteins and similar domains; This subfamily is composed of vertebrate SH3TC proteins and hypothetical fungal proteins containing BAR and SH3 domains. Mammals contain two SH3TC proteins, SH3TC1 and SH3TC2. The function of SH3TC1 is unknown. SH3TC2 is localized in Schwann cells in the peripheral nervous system, where it interacts with Rab11 and plays a role in peripheral nerve myelination. Mutations in SH3TC2 are associated with Charcot-Marie-Tooth disease type 4C, a severe hereditary peripheral neuropathy with symptoms that include progressive scoliosis, delayed age of walking, muscular atrophy, distal weakness, and reduced nerve conduction velocity. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies. Pssm-ID: 212818 Cd Length: 55 Bit Score: 39.61 E-value: 2.24e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6602-6632 | 2.26e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.99 E-value: 2.26e-03
|
||||||
| SH3_PI3K_p85 | cd11776 | Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; ... |
7465-7519 | 2.30e-03 | ||
Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212710 Cd Length: 72 Bit Score: 40.18 E-value: 2.30e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
855-883 | 2.47e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 2.47e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1346-1373 | 2.57e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.57e-03
|
||||||
| SH3_SH3RF1_1 | cd11927 | First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ... |
7466-7517 | 2.58e-03 | ||
First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212860 Cd Length: 54 Bit Score: 39.55 E-value: 2.58e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5584-5611 | 2.63e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.63e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
5971-5998 | 2.68e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2073-2103 | 2.73e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 2.73e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3914-3941 | 2.78e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.78e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3985-4012 | 2.81e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.53 E-value: 2.81e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
779-809 | 3.04e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 3.04e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3423-3453 | 3.19e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.60 E-value: 3.19e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
532-562 | 3.52e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.52e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4400-4427 | 3.53e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 3.53e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1476-1506 | 3.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 3.74e-03
|
||||||
| SH3_SH3RF2_1 | cd11929 | First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ... |
7466-7517 | 3.81e-03 | ||
First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212862 Cd Length: 54 Bit Score: 39.15 E-value: 3.81e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3603-3630 | 4.08e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4228-4254 | 4.08e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.08e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4395-4425 | 4.38e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 38.22 E-value: 4.38e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
537-564 | 4.46e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 38.14 E-value: 4.46e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
568-598 | 4.69e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 4.69e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
815-845 | 4.69e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 4.69e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
2004-2031 | 4.73e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 4.73e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3463-3490 | 4.97e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 4.97e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1097-1127 | 5.07e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.07e-03
|
||||||
| SH3_PLCgamma2 | cd11969 | Src homology 3 domain of Phospholipase C (PLC) gamma 2; PLCgamma2 is primarily expressed in ... |
7466-7519 | 5.16e-03 | ||
Src homology 3 domain of Phospholipase C (PLC) gamma 2; PLCgamma2 is primarily expressed in haematopoietic cells, specifically in B cells. It is activated by tyrosine phosphorylation by B cell receptor (BCR) kinases and is recruited to the plasma membrane where its substrate is located. It is required in pre-BCR signaling and in the maturation of B cells. PLCs catalyze the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG). Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212902 Cd Length: 55 Bit Score: 38.67 E-value: 5.16e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2730-2759 | 5.27e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7134-7159 | 5.27e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.27e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
1829-1859 | 5.38e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.38e-03
|
||||||
| SH3_Ysc84p_like | cd11842 | Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ... |
7466-7518 | 5.40e-03 | ||
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212776 [Multi-domain] Cd Length: 55 Bit Score: 38.56 E-value: 5.40e-03
|
||||||
| SH3_Stac_1 | cd11833 | First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ... |
7465-7516 | 5.52e-03 | ||
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies. Pssm-ID: 212767 [Multi-domain] Cd Length: 53 Bit Score: 38.64 E-value: 5.52e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4471-4498 | 5.82e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.82e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1590-1617 | 5.87e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.76 E-value: 5.87e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
2317-2347 | 5.99e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.83 E-value: 5.99e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3180-3210 | 6.29e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.29e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7165-7194 | 6.42e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.42e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4332-4359 | 6.68e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 6.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
608-636 | 6.68e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 6.68e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
4188-4217 | 7.30e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.30e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
178-207 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
3702-3731 | 7.74e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.45 E-value: 7.74e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
3220-3247 | 8.05e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 37.37 E-value: 8.05e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
6859-6881 | 8.79e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 8.79e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
7041-7070 | 8.79e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 8.79e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1308-1335 | 8.88e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 8.88e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
1237-1264 | 9.41e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 9.41e-03
|
||||||
| Nebulin | pfam00880 | Nebulin repeat; |
4678-4705 | 9.70e-03 | ||
Nebulin repeat; Pssm-ID: 459977 Cd Length: 28 Bit Score: 36.98 E-value: 9.70e-03
|
||||||
| NEBU | smart00227 | The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind ... |
6176-6206 | 9.89e-03 | ||
The Nebulin repeat is present also in Las1; Tandem arrays of these repeats are known to bind actin. Pssm-ID: 128523 Cd Length: 31 Bit Score: 37.06 E-value: 9.89e-03
|
||||||
| Blast search parameters | ||||
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