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Conserved domains on  [gi|1907086396|ref|XP_036013140|]
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protein numb homolog isoform X8 [Mus musculus]

Protein Classification

numb family protein; PH domain-containing RhoGEF family protein( domain architecture ID 10352266)

numb family protein similar to protein numb that is required in determination of cell fate during sensory organ formation in embryos, and numb-like protein that plays a role in the process of neurogenesis| PH domain-containing RhoGEF family protein may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 4B and Danio rerio quattro

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 6-98 5.31e-68

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd01268:

Pssm-ID: 473070  Cd Length: 135  Bit Score: 216.40  E-value: 5.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396   6 LTKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLS 85
Cdd:cd01268    43 LKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLS 122

                          90
                  ....*....|...
gi 1907086396  86 HAVGCAFAACLER 98
Cdd:cd01268   123 HAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 188-268 9.51e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


:

Pssm-ID: 461874  Cd Length: 95  Bit Score: 134.52  E-value: 9.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396 188 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNTVPEVEG---E 253
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 1907086396 254 AESISSLCSQITSAF 268
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 6-98 5.31e-68

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 241298  Cd Length: 135  Bit Score: 216.40  E-value: 5.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396   6 LTKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLS 85
Cdd:cd01268    43 LKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLS 122

                          90
                  ....*....|...
gi 1907086396  86 HAVGCAFAACLER 98
Cdd:cd01268   123 HAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 188-268 9.51e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 134.52  E-value: 9.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396 188 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNTVPEVEG---E 253
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 1907086396 254 AESISSLCSQITSAF 268
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
14-95 3.08e-26

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 103.98  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396  14 VKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAF 92
Cdd:pfam00640  52 TKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAF 130


                  ...
gi 1907086396  93 AAC 95
Cdd:pfam00640 131 ALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 6-105 3.95e-23

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 95.07  E-value: 3.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396    6 LTKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGErLS 85
Cdd:smart00462  36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAED-IA 114

                           90       100
                   ....*....|....*....|
gi 1907086396   86 HAVGCAFAACLERKQKREKE 105
Cdd:smart00462 115 LAIGQAFQLAYELKLKARSE 134
 
Name Accession Description Interval E-value
PTB_Numb cd01268
Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which ...
 6-98 5.31e-68

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 241298  Cd Length: 135  Bit Score: 216.40  E-value: 5.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396   6 LTKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLS 85
Cdd:cd01268    43 LKASRKKPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRNHERAFSYICRDGTTRRWMCHCFLAVKDSGERLS 122

                          90
                  ....*....|...
gi 1907086396  86 HAVGCAFAACLER 98
Cdd:cd01268   123 HAVGCAFAACLER 135
NumbF pfam06311
NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB ...
 188-268 9.51e-38

NUMB domain; This presumed domain is found in the Numb family of proteins adjacent to the PTB domain..


Pssm-ID: 461874  Cd Length: 95  Bit Score: 134.52  E-value: 9.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396 188 PHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDF-----------PIKNTVPEVEG---E 253
Cdd:pfam06311   1 PFAIERPHAPLSMLQRQGSFRGFPQLSQKNSPFKRQLSLRLNELPSNLQRKRSFslepsdpplktPVSNPIPEISPsseQ 80

                          90
                  ....*....|....*
gi 1907086396 254 AESISSLCSQITSAF 268
Cdd:pfam06311  81 ADSISAMCQQISSGL 95
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
14-95 3.08e-26

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 103.98  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396  14 VKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAP-DRNFDRAFSYICRDGTTRRWICHCFMAVKDtGERLSHAVGCAF 92
Cdd:pfam00640  52 TKVDLFISTDGLKLLNPDTQELIHDHPLVSISFCADgDPDLMRYFAYIARDKATNKFACHVFESEDG-AQDIAQSIGQAF 130


                  ...
gi 1907086396  93 AAC 95
Cdd:pfam00640 131 ALA 133
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 6-105 3.95e-23

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 95.07  E-value: 3.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396    6 LTKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGErLS 85
Cdd:smart00462  36 QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDDLDVFGYIARDPGSSRFACHVFRCEKAAED-IA 114

                           90       100
                   ....*....|....*....|
gi 1907086396   86 HAVGCAFAACLERKQKREKE 105
Cdd:smart00462 115 LAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 10-92 8.85e-17

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 76.78  E-value: 8.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396  10 GKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAV-KDTGERLSHAV 88
Cdd:cd00934    37 KRKPGPVLLEVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPDNPNVFAFIAGEEGGSGFRCHVFQCEdEEEAEEILQAI 116


                  ....
gi 1907086396  89 GCAF 92
Cdd:cd00934   117 GQAF 120
PTB_TK_HMTK cd13161
Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK ...
 9-97 3.45e-13

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269983  Cd Length: 120  Bit Score: 66.50  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396   9 TGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMaVKDTGERLSHAV 88
Cdd:cd13161    33 LKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPKDKKLFAFISHDPRLGRITCHVFR-CKRGAQEICDTI 111


                  ....*....
gi 1907086396  89 GCAFAACLE 97
Cdd:cd13161   112 AEAFKAAAE 120
PTB_LDLRAP-mammal-like cd13159
Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins ...
 7-78 1.16e-11

Low Density Lipoprotein Receptor Adaptor Protein 1 (LDLRAP1) in mammals and similar proteins Phosphotyrosine-binding (PTB) PH-like fold; The null mutations in the LDL receptor adaptor protein 1 (LDLRAP1) gene, which serves as an adaptor for LDLR endocytosis in the liver, causes autosomal recessive hypercholesterolemia (ARH). LDLRAP1 contains a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd contains mammals, insects, and sponges.


Pssm-ID: 269981  Cd Length: 123  Bit Score: 61.96  E-value: 1.16e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907086396   7 TKTGKKAVKAV-LWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVK 78
Cdd:cd13159    35 AKASGKKLQKVtLTVSPKGIKVTDSATNETILEVSIYRISYCTADANHDKVFAFIATNQDNEKLECHAFLCAK 107
PTB_CED-6 cd01273
Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also ...
 8-92 8.12e-11

Cell death protein 6 homolog (CED-6/GULP1) Phosphotyrosine-binding (PTB) domain; CED6 (also known as GULP1: engulfment adaptor PTB domain containing 1) is an adaptor protein involved in the specific recognition and engulfment of apoptotic cells. CED6 has been shown to interact with the cytoplasmic tail of another protein involved in the engulfment of apoptotic cells, CED1. CED6 has a C-terminal PTB domain, which can bind to NPXY motifs. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269971  Cd Length: 144  Bit Score: 60.37  E-value: 8.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086396   8 KTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKdTGERLSHA 87
Cdd:cd01273    49 SEGAKLPKVELQISIDGVKIQDPKTKVIMHQFPLHRISFCADDKTDKRIFSFIAKDSESEKHLCFVFDSEK-LAEEITLT 127


                  ....*
gi 1907086396  88 VGCAF 92
Cdd:cd01273   128 IGQAF 132
PTB_Dab cd01215
Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which ...
 9-61 2.11e-07

Disabled (Dab) Phosphotyrosine-binding domain; Dab is a cystosolic adaptor protein, which binds to the cytoplasmic tails of lipoprotein receptors, such as ApoER2 and VLDLR, via its PTB domain. The dab PTB domain has a preference for unphosphorylated tyrosine within an NPxY motif. Additionally, the Dab PTB domain, which is structurally similar to PH domains, binds to phosphatidlyinositol phosphate 4,5 bisphosphate in a manner characteristic of phosphoinositide binding PH domains. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269926  Cd Length: 147  Bit Score: 50.33  E-value: 2.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907086396   9 TGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYIC 61
Cdd:cd01215    51 AGEHKQRIWLNISLEGIKILDEKTGALLHHHPVHKISFIARDTTDNRAFGYVC 103
PTB_Anks cd01274
Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family ...
 17-78 5.53e-07

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269972  Cd Length: 146  Bit Score: 49.20  E-value: 5.53e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907086396  17 VLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVK 78
Cdd:cd01274    57 ILSISYKGVKFIDATTKNLICEHEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLT 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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