WD repeat and HMG-box DNA-binding protein 1 Acidic nucleoplasmic DNA-binding protein 1 [Channa argus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Mcl1_mid | pfam12341 | Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of ... |
756-1050 | 3.60e-124 | |||||
Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of minichromosome loss protein 1, is the domain that lies between a 7-bladed beta-propeller at the N-terminus, family WD40 pfam00400 etc, and a Homeobox (HMG) domain, pfam00505, at the C-terminus. The full length proteins with all three domains are referred to as DNA polymerase alpha accessory factor Mcl1, but the exact function of this domain is not known. : Pssm-ID: 463539 Cd Length: 288 Bit Score: 388.08 E-value: 3.60e-124
|
|||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
325-612 | 3.39e-38 | |||||
WD40 repeat [General function prediction only]; : Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.52 E-value: 3.39e-38
|
|||||||||
| SH2 super family | cl15255 | Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ... |
245-307 | 2.26e-31 | |||||
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others. The actual alignment was detected with superfamily member cd10385: Pssm-ID: 472789 Cd Length: 101 Bit Score: 118.65 E-value: 2.26e-31
|
|||||||||
| HMG-box_WDHD1 | cd21993 | high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and ... |
1344-1403 | 1.55e-25 | |||||
high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and similar proteins; WDHD1, also called acidic nucleoplasmic DNA-binding protein 1 (And-1), acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. : Pssm-ID: 438809 [Multi-domain] Cd Length: 62 Bit Score: 100.80 E-value: 1.55e-25
|
|||||||||
| SOCS | pfam12610 | Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and ... |
66-120 | 1.60e-19 | |||||
Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam07525, pfam00017. The suppressors of cytokine signaling (SOCS) family play important roles in regulating a variety of signal transduction pathways that are involved in immunity, growth and development of organizms. : Pssm-ID: 432667 Cd Length: 57 Bit Score: 83.29 E-value: 1.60e-19
|
|||||||||
| NHP6B super family | cl26372 | Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; |
1311-1446 | 6.51e-07 | |||||
Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; The actual alignment was detected with superfamily member COG5648: Pssm-ID: 227935 [Multi-domain] Cd Length: 211 Bit Score: 51.79 E-value: 6.51e-07
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Mcl1_mid | pfam12341 | Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of ... |
756-1050 | 3.60e-124 | |||||
Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of minichromosome loss protein 1, is the domain that lies between a 7-bladed beta-propeller at the N-terminus, family WD40 pfam00400 etc, and a Homeobox (HMG) domain, pfam00505, at the C-terminus. The full length proteins with all three domains are referred to as DNA polymerase alpha accessory factor Mcl1, but the exact function of this domain is not known. Pssm-ID: 463539 Cd Length: 288 Bit Score: 388.08 E-value: 3.60e-124
|
|||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
325-612 | 3.39e-38 | |||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.52 E-value: 3.39e-38
|
|||||||||
| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
324-612 | 1.27e-35 | |||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 137.85 E-value: 1.27e-35
|
|||||||||
| SH2_SOCS4 | cd10385 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
245-307 | 2.26e-31 | |||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198248 Cd Length: 101 Bit Score: 118.65 E-value: 2.26e-31
|
|||||||||
| HMG-box_WDHD1 | cd21993 | high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and ... |
1344-1403 | 1.55e-25 | |||||
high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and similar proteins; WDHD1, also called acidic nucleoplasmic DNA-binding protein 1 (And-1), acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Pssm-ID: 438809 [Multi-domain] Cd Length: 62 Bit Score: 100.80 E-value: 1.55e-25
|
|||||||||
| SOCS | pfam12610 | Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and ... |
66-120 | 1.60e-19 | |||||
Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam07525, pfam00017. The suppressors of cytokine signaling (SOCS) family play important roles in regulating a variety of signal transduction pathways that are involved in immunity, growth and development of organizms. Pssm-ID: 432667 Cd Length: 57 Bit Score: 83.29 E-value: 1.60e-19
|
|||||||||
| SH2 | smart00252 | Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ... |
255-308 | 1.35e-12 | |||||
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae. Pssm-ID: 214585 [Multi-domain] Cd Length: 84 Bit Score: 64.56 E-value: 1.35e-12
|
|||||||||
| HMG | smart00398 | high mobility group; |
1346-1415 | 8.70e-12 | |||||
high mobility group; Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 61.95 E-value: 8.70e-12
|
|||||||||
| SH2 | pfam00017 | SH2 domain; |
257-308 | 3.02e-09 | |||||
SH2 domain; Pssm-ID: 425423 [Multi-domain] Cd Length: 77 Bit Score: 54.91 E-value: 3.02e-09
|
|||||||||
| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
439-478 | 3.96e-08 | |||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 50.39 E-value: 3.96e-08
|
|||||||||
| WD40 | pfam00400 | WD domain, G-beta repeat; |
440-478 | 7.89e-08 | |||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 49.65 E-value: 7.89e-08
|
|||||||||
| HMG_box | pfam00505 | HMG (high mobility group) box; |
1346-1415 | 2.45e-07 | |||||
HMG (high mobility group) box; Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 49.15 E-value: 2.45e-07
|
|||||||||
| NHP6B | COG5648 | Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; |
1311-1446 | 6.51e-07 | |||||
Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; Pssm-ID: 227935 [Multi-domain] Cd Length: 211 Bit Score: 51.79 E-value: 6.51e-07
|
|||||||||
| Name | Accession | Description | Interval | E-value | ||||||
| Mcl1_mid | pfam12341 | Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of ... |
756-1050 | 3.60e-124 | ||||||
Minichromosome loss protein, Mcl1, middle region; Mcl1_mid, or the middle domain of minichromosome loss protein 1, is the domain that lies between a 7-bladed beta-propeller at the N-terminus, family WD40 pfam00400 etc, and a Homeobox (HMG) domain, pfam00505, at the C-terminus. The full length proteins with all three domains are referred to as DNA polymerase alpha accessory factor Mcl1, but the exact function of this domain is not known. Pssm-ID: 463539 Cd Length: 288 Bit Score: 388.08 E-value: 3.60e-124
|
||||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
325-612 | 3.39e-38 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.52 E-value: 3.39e-38
|
||||||||||
| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
324-612 | 1.27e-35 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 137.85 E-value: 1.27e-35
|
||||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
269-612 | 4.23e-35 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 139.28 E-value: 4.23e-35
|
||||||||||
| SH2_SOCS4 | cd10385 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
245-307 | 2.26e-31 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198248 Cd Length: 101 Bit Score: 118.65 E-value: 2.26e-31
|
||||||||||
| SH2_SOCS_family | cd09923 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ... |
255-309 | 1.15e-26 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198178 Cd Length: 81 Bit Score: 104.59 E-value: 1.15e-26
|
||||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
325-480 | 1.10e-25 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.54 E-value: 1.10e-25
|
||||||||||
| HMG-box_WDHD1 | cd21993 | high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and ... |
1344-1403 | 1.55e-25 | ||||||
high mobility group (HMG)-box found in WD repeat and HMG-box DNA-binding protein 1 (WDHD1) and similar proteins; WDHD1, also called acidic nucleoplasmic DNA-binding protein 1 (And-1), acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Pssm-ID: 438809 [Multi-domain] Cd Length: 62 Bit Score: 100.80 E-value: 1.55e-25
|
||||||||||
| SH2_SOCS5 | cd10386 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 ... |
255-307 | 1.65e-25 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) family; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198249 Cd Length: 81 Bit Score: 101.31 E-value: 1.65e-25
|
||||||||||
| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
325-478 | 1.44e-19 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 90.86 E-value: 1.44e-19
|
||||||||||
| SOCS | pfam12610 | Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and ... |
66-120 | 1.60e-19 | ||||||
Suppressor of cytokine signalling; This domain family is found in bacteria and eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam07525, pfam00017. The suppressors of cytokine signaling (SOCS) family play important roles in regulating a variety of signal transduction pathways that are involved in immunity, growth and development of organizms. Pssm-ID: 432667 Cd Length: 57 Bit Score: 83.29 E-value: 1.60e-19
|
||||||||||
| WD40 | COG2319 | WD40 repeat [General function prediction only]; |
381-612 | 1.53e-17 | ||||||
WD40 repeat [General function prediction only]; Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 86.89 E-value: 1.53e-17
|
||||||||||
| SH2_SOCS6 | cd10387 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
257-333 | 7.94e-17 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198250 Cd Length: 100 Bit Score: 77.19 E-value: 7.94e-17
|
||||||||||
| SH2 | smart00252 | Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides ... |
255-308 | 1.35e-12 | ||||||
Src homology 2 domains; Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. Specificity is provided via interaction with residues that are distinct from the phosphotyrosine. Only a single occurrence of a SH2 domain has been found in S. cerevisiae. Pssm-ID: 214585 [Multi-domain] Cd Length: 84 Bit Score: 64.56 E-value: 1.35e-12
|
||||||||||
| SH2_SOCS7 | cd10388 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
257-307 | 2.18e-12 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198251 Cd Length: 101 Bit Score: 64.68 E-value: 2.18e-12
|
||||||||||
| WD40 | cd00200 | WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
444-612 | 4.24e-12 | ||||||
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 68.52 E-value: 4.24e-12
|
||||||||||
| HMG | smart00398 | high mobility group; |
1346-1415 | 8.70e-12 | ||||||
high mobility group; Pssm-ID: 197700 [Multi-domain] Cd Length: 70 Bit Score: 61.95 E-value: 8.70e-12
|
||||||||||
| SH2 | cd00173 | Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ... |
255-308 | 6.00e-10 | ||||||
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others. Pssm-ID: 198173 [Multi-domain] Cd Length: 79 Bit Score: 57.08 E-value: 6.00e-10
|
||||||||||
| HMG-box_SSRP1-like | cd21994 | high mobility group (HMG)-box found in structure-specific recognition protein 1 (SSRP1) and ... |
1347-1399 | 1.32e-09 | ||||||
high mobility group (HMG)-box found in structure-specific recognition protein 1 (SSRP1) and similar proteins; SSRP1, also called FACT complex subunit SSRP1, chromatin-specific transcription elongation factor 80 kDa subunit, facilitates chromatin transcription complex 80 kDa subunit (FACT 80 kDa subunit or FACTp80), facilitates chromatin transcription complex subunit SSRP1, recombination signal sequence recognition protein 1, or T160, is a factor that facilitates transcript elongation through nucleosomes. It is a component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication, and DNA repair. Pssm-ID: 438810 [Multi-domain] Cd Length: 67 Bit Score: 55.38 E-value: 1.32e-09
|
||||||||||
| SH2 | pfam00017 | SH2 domain; |
257-308 | 3.02e-09 | ||||||
SH2 domain; Pssm-ID: 425423 [Multi-domain] Cd Length: 77 Bit Score: 54.91 E-value: 3.02e-09
|
||||||||||
| HMG-box_SF | cd00084 | high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found ... |
1347-1399 | 4.02e-09 | ||||||
high mobility group (HMG)-box domain superfamily; The High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs bind to the minor groove of DNA and have been classified by DNA binding preferences. Two phylogenetically distinct groups of Class I proteins bind DNA in a sequence specific fashion and contain a single HMG box. One group (SOX-TCF) includes transcription factors, TCF-1, -3, -4, and also SRY and LEF-1, which bind four-way DNA junctions and duplex DNA targets. The second group (MATA) includes fungal mating type gene products MC, MATA1 and Ste11. Class II and III proteins (HMGB-UBF) bind DNA in a non-sequence specific fashion and contain two or more tandem HMG boxes. Class II members include non-histone chromosomal proteins, HMG1 and HMG2, which bind to bent or distorted DNA such as four-way DNA junctions, synthetic DNA cruciforms, kinked cisplatin-modified DNA, DNA bulges, cross-overs in supercoiled DNA, and can cause looping of linear DNA. Class III members include nucleolar and mitochondrial transcription factors, UBF and mtTF1, which bind four-way DNA junctions. Pssm-ID: 438789 [Multi-domain] Cd Length: 59 Bit Score: 54.06 E-value: 4.02e-09
|
||||||||||
| SH2_SOCS2 | cd10383 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
250-306 | 7.98e-09 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198246 Cd Length: 103 Bit Score: 54.50 E-value: 7.98e-09
|
||||||||||
| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
439-478 | 3.96e-08 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 50.39 E-value: 3.96e-08
|
||||||||||
| WD40 | pfam00400 | WD domain, G-beta repeat; |
440-478 | 7.89e-08 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 49.65 E-value: 7.89e-08
|
||||||||||
| SH2_CIS | cd10718 | Src homology 2 (SH2) domain found in cytokine-inducible SH2-containing protein (CIS); CIS ... |
251-306 | 9.18e-08 | ||||||
Src homology 2 (SH2) domain found in cytokine-inducible SH2-containing protein (CIS); CIS family members are known to be cytokine-inducible negative regulators of cytokine signaling. The expression of the CIS gene can be induced by IL2, IL3, GM-CSF and EPO in hematopoietic cells. Proteasome-mediated degradation of this protein has been shown to be involved in the inactivation of the erythropoietin receptor. Suppressor of cytokine signalling (SOCS) was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198285 Cd Length: 88 Bit Score: 50.91 E-value: 9.18e-08
|
||||||||||
| SH2_SOCS1 | cd10382 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
257-306 | 1.13e-07 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198245 Cd Length: 98 Bit Score: 51.21 E-value: 1.13e-07
|
||||||||||
| HMG_box | pfam00505 | HMG (high mobility group) box; |
1346-1415 | 2.45e-07 | ||||||
HMG (high mobility group) box; Pssm-ID: 459837 [Multi-domain] Cd Length: 68 Bit Score: 49.15 E-value: 2.45e-07
|
||||||||||
| SH2_SOCS3 | cd10384 | Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 ... |
257-307 | 3.13e-07 | ||||||
Src homology 2 (SH2) domain found in suppressor of cytokine signaling (SOCS) proteins; SH2 domain found in SOCS proteins. SOCS was first recognized as a group of cytokine-inducible SH2 (CIS) domain proteins comprising eight family members in human (CIS and SOCS1-SOCS7). In addition to the SH2 domain, SOCS proteins have a variable N-terminal domain and a conserved SOCS box in the C-terminal domain. SOCS proteins bind to a substrate via their SH2 domain. The prototypical members, CIS and SOCS1-SOCS3, have been shown to regulate growth hormone signaling in vitro and in a classic negative feedback response compete for binding at phosphotyrosine sites in JAK kinase and receptor pathways to displace effector proteins and target bound receptors for proteasomal degradation. Loss of SOCS activity results in excessive cytokine signaling associated with a variety of hematopoietic, autoimmune, and inflammatory diseases and certain cancers. Members (SOCS4-SOCS7) were identified by their conserved SOCS box, an adapter motif of 3 helices that associates substrate binding domains, such as the SOCS SH2 domain, ankryin, and WD40 with ubiquitin ligase components. These show limited cytokine induction. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198247 Cd Length: 101 Bit Score: 50.12 E-value: 3.13e-07
|
||||||||||
| eIF2A | pfam08662 | Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
516-608 | 5.33e-07 | ||||||
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors. Pssm-ID: 462552 [Multi-domain] Cd Length: 194 Bit Score: 51.50 E-value: 5.33e-07
|
||||||||||
| NHP6B | COG5648 | Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; |
1311-1446 | 6.51e-07 | ||||||
Chromatin-associated proteins containing the HMG domain [Chromatin structure and dynamics]; Pssm-ID: 227935 [Multi-domain] Cd Length: 211 Bit Score: 51.79 E-value: 6.51e-07
|
||||||||||
| SH2_Vav_family | cd09940 | Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several ... |
255-308 | 1.40e-05 | ||||||
Src homology 2 (SH2) domain found in the Vav family; Vav proteins are involved in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation. Vavs function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. Vav family members have several conserved motifs/domains including: a leucine-rich region, a leucine-zipper, a calponin homology (CH) domain, an acidic domain, a Dbl-homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain, 2 SH3 domains, a proline-rich region, and a SH2 domain. Vavs are the only known Rho GEFs that have both the DH/PH motifs and SH2/SH3 domains in the same protein. The leucine-rich helix-loop-helix (HLH) domain is thought to be involved in protein heterodimerization with other HLH proteins and it may function as a negative regulator by forming inactive heterodimers. The CH domain is usually involved in the association with filamentous actin, but in Vav it controls NFAT stimulation, Ca2+ mobilization, and its transforming activity. Acidic domains are involved in protein-protein interactions and contain regulatory tyrosines. The DH domain is a GDP-GTP exchange factor on Rho/Rac GTPases. The PH domain in involved in interactions with GTP-binding proteins, lipids and/or phosphorylated serine/threonine residues. The SH3 domain is involved in localization of proteins to specific sites within the cell interacting with protein with proline-rich sequences. The SH2 domain mediates a high affinity interaction with tyrosine phosphorylated proteins. There are three Vav mammalian family members: Vav1 which is expressed in the hematopoietic system, Vav2 and Vav3 are more ubiquitously expressed. The members here include insect and amphibian Vavs. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198193 Cd Length: 102 Bit Score: 45.36 E-value: 1.40e-05
|
||||||||||
| SH2_ShkD_ShkE | cd10357 | Src homology 2 (SH2) domain found in SH2 domain-bearing protein kinases D and E (ShkD and ShkE) ... |
257-306 | 4.43e-05 | ||||||
Src homology 2 (SH2) domain found in SH2 domain-bearing protein kinases D and E (ShkD and ShkE); SH2-bearing genes cloned from Dictyostelium include two transcription factors, STATa and STATc, and a signaling factor, SHK1 (shkA). A database search of the Dictyostelium discoideum genome revealed two additional putative STAT sequences, dd-STATb and dd-STATd, and four additional putative SHK genes, dd-SHK2 (shkB), dd-SHK3 (shkC), dd-SHK4 (shkD), and dd-SHK5 (shkE). This model contains members of shkD and shkE. All of the SHK members are most closely related to the protein kinases found in plants. However these kinases in plants are not conjugated to any SH2 or SH2-like sequences. Alignment data indicates that the SHK SH2 domains carry some features of the STAT SH2 domains in Dictyostelium. When STATc's linker domain was used for a BLAST search, the sequence between the protein kinase domain and the SH2 domain (the linker) of SHK was recovered, suggesting a close relationship among these molecules within this region. SHK's linker domain is predicted to contain an alpha-helix which is indeed homologous to that of STAT. Based on the phylogenetic alignment, SH2 domains can be grouped into two categories, STAT-type and Src-type. SHK family members are in between, but are closer to the STAT-type which indicates a close relationship between SHK and STAT families in their SH2 domains and further supports the notion that SHKs linker-SH2 domain evolved from STAT or STATL (STAT-like Linker-SH2) domain found in plants. In SHK, STAT, and SPT6, the linker-SH2 domains all reside exclusively in the C-terminal regions. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198220 Cd Length: 87 Bit Score: 43.27 E-value: 4.43e-05
|
||||||||||
| SH2_SHB_SHD_SHE_SHF_like | cd09945 | Src homology 2 domain found in SH2 domain-containing adapter proteins B, D, E, and F (SHB, SHD, ... |
255-308 | 5.90e-05 | ||||||
Src homology 2 domain found in SH2 domain-containing adapter proteins B, D, E, and F (SHB, SHD, SHE, SHF); SHB, SHD, SHE, and SHF are SH2 domain-containing proteins that play various roles throughout the cell. SHB functions in generating signaling compounds in response to tyrosine kinase activation. SHB contains proline-rich motifs, a phosphotyrosine binding (PTB) domain, tyrosine phosphorylation sites, and a SH2 domain. SHB mediates certain aspects of platelet-derived growth factor (PDGF) receptor-, fibroblast growth factor (FGF) receptor-, neural growth factor (NGF) receptor TRKA-, T cell receptor-, interleukin-2 (IL-2) receptor- and focal adhesion kinase- (FAK) signaling. SRC-like FYN-Related Kinase FRK/RAK (also named BSK/IYK or GTK) and SHB regulate apoptosis, proliferation and differentiation. SHB promotes apoptosis and is also required for proper mitogenicity, spreading and tubular morphogenesis in endothelial cells. SHB also plays a role in preventing early cavitation of embryoid bodies and reduces differentiation to cells expressing albumin, amylase, insulin and glucagon. SHB is a multifunctional protein that has difference responses in different cells under various conditions. SHE is expressed in heart, lung, brain, and skeletal muscle, while expression of SHD is restricted to the brain. SHF is mainly expressed in skeletal muscle, brain, liver, prostate, testis, ovary, small intestine, and colon. SHD may be a physiological substrate of c-Abl and may function as an adapter protein in the central nervous system. It is also thought to be involved in apoptotic regulation. SHD contains five YXXP motifs, a substrate sequence preferred by Abl tyrosine kinases, in addition to a poly-proline rich region and a C-terminal SH2 domain. SHE contains two pTry protein binding domains, protein interaction domain (PID) and a SH2 domain, followed by a glycine-proline rich region, all of which are N-terminal to the phosphotyrosine binding (PTB) domain. SHF contains four putative tyrosine phosphorylation sites and an SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198198 Cd Length: 98 Bit Score: 43.57 E-value: 5.90e-05
|
||||||||||
| HMG-box_SoxG_SOX15 | cd22035 | high mobility group (HMG)-box found in sex determining region Y (SRY)-box 15 (SOX15) and ... |
1346-1417 | 6.20e-05 | ||||||
high mobility group (HMG)-box found in sex determining region Y (SRY)-box 15 (SOX15) and similar proteins; SOX-15, also called SOX-12, SOX-20, SOX-26, or SOX-27, is a crucial transcription factor involved in the regulation of embryonic development and in cell fate determination. It binds to the 5'-AACAAT-3' sequence. SOX-15 can be a tumor suppressor in multiple cancer types. SOX-5 is the only member of group G SRY-related high-mobility group (HMG) box (Sox) transcription factors. Pssm-ID: 438844 [Multi-domain] Cd Length: 84 Bit Score: 43.15 E-value: 6.20e-05
|
||||||||||
| HMG-box_EGL13-like | cd22042 | high mobility group (HMG)-box found in Caenorhabditis elegans protein egg laying defective 13 ... |
1346-1396 | 6.34e-05 | ||||||
high mobility group (HMG)-box found in Caenorhabditis elegans protein egg laying defective 13 (EGL-13) and similar proteins; EGL-13 may act as a transcription factor that is required for uterine cell fate decisions in Caenorhabditis elegans. It controls genes required for the specification and differentiation of O(2) and CO(2)-sensing neurons and for maintaining URX sensory neuronal cell fate. Pssm-ID: 438848 [Multi-domain] Cd Length: 78 Bit Score: 42.58 E-value: 6.34e-05
|
||||||||||
| HMG-box_AtHMGB1-like | cd22005 | high mobility group (HMG)-box found in Arabidopsis thaliana high mobility group B protein 1 ... |
1346-1398 | 6.82e-05 | ||||||
high mobility group (HMG)-box found in Arabidopsis thaliana high mobility group B protein 1 (HMGB1) and similar proteins; This subfamily contains a group of Arabidopsis thaliana HMGB family proteins, including HMGB1, 2, 3, 4, 5, 7, 12 and 14. They bind preferentially to double-stranded DNA. HMGB1 modulates general plant growth and stress tolerance and confers sensitivity to salt and genotoxic (methyl methanesulfonate, MMS) stresses. HMGB2 and HMGB5 confer sensitivity to salt and drought stresses. HMGB7 is required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus. Members of this subfamily contain only one HMG-box domain. Pssm-ID: 438821 [Multi-domain] Cd Length: 60 Bit Score: 41.91 E-value: 6.82e-05
|
||||||||||
| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
325-355 | 1.32e-04 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 40.76 E-value: 1.32e-04
|
||||||||||
| SH2_a2chimerin_b2chimerin | cd10352 | Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins; Chimerins ... |
257-305 | 1.63e-04 | ||||||
Src homology 2 (SH2) domain found in alpha2-chimerin and beta2-chimerin proteins; Chimerins are a family of phorbol ester- and diacylglycerol-responsive GTPase-activating proteins. Alpha1-chimerin (formerly known as n-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All of the isoforms contain a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. Other C1 domain-containing diacylglycerol receptors including: PKC, Munc-13 proteins, phorbol ester binding scaffolding proteins involved in Ca2+-stimulated exocytosis, and RasGRPs, diacylglycerol-activated guanine-nucleotide exchange factors (GEFs) for Ras and Rap1. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198215 Cd Length: 91 Bit Score: 41.97 E-value: 1.63e-04
|
||||||||||
| SH2_C-SH2_PLC_gamma_like | cd09932 | C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a ... |
253-307 | 2.35e-04 | ||||||
C-terminal Src homology 2 (C-SH2) domain in Phospholipase C gamma; Phospholipase C gamma is a signaling molecule that is recruited to the C-terminal tail of the receptor upon autophosphorylation of a highly conserved tyrosine. PLCgamma is composed of a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, 2 catalytic regions of PLC domains that flank 2 tandem SH2 domains (N-SH2, C-SH2), and ending with a SH3 domain and C2 domain. N-SH2 SH2 domain-mediated interactions represent a crucial step in transmembrane signaling by receptor tyrosine kinases. SH2 domains recognize phosphotyrosine (pY) in the context of particular sequence motifs in receptor phosphorylation sites. Both N-SH2 and C-SH2 have a very similar binding affinity to pY. But in growth factor stimulated cells these domains bind to different target proteins. N-SH2 binds to pY containing sites in the C-terminal tails of tyrosine kinases and other receptors. Recently it has been shown that this interaction is mediated by phosphorylation-independent interactions between a secondary binding site found exclusively on the N-SH2 domain and a region of the FGFR1 tyrosine kinase domain. This secondary site on the SH2 cooperates with the canonical pY site to regulate selectivity in mediating a specific cellular process. C-SH2 binds to an intramolecular site on PLCgamma itself which allows it to hydrolyze phosphatidylinositol-4,5-bisphosphate into diacylglycerol and inositol triphosphate. These then activate protein kinase C and release calcium. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198186 Cd Length: 104 Bit Score: 41.87 E-value: 2.35e-04
|
||||||||||
| SH2_CRK_like | cd09926 | Src homology 2 domain found in cancer-related signaling adaptor protein CRK; SH2 domain in the ... |
257-293 | 2.66e-04 | ||||||
Src homology 2 domain found in cancer-related signaling adaptor protein CRK; SH2 domain in the CRK proteins. CRKI (SH2-SH3) and CRKII (SH2-SH3-SH3) are splicing isoforms of the oncoprotein CRK. CRKs regulate transcription and cytoskeletal reorganization for cell growth and motility by linking tyrosine kinases to small G proteins. The SH2 domain of CRK associates with tyrosine-phosphorylated receptors or components of focal adhesions, such as p130Cas and paxillin. CRK transmits signals to small G proteins through effectors that bind its SH3 domain, such as C3G, the guanine-nucleotide exchange factor (GEF) for Rap1 and R-Ras, and DOCK180, the GEF for Rac6. The binding of p130Cas to the CRK-C3G complex activates Rap1, leading to regulation of cell adhesion, and activates R-Ras, leading to JNK-mediated activation of cell proliferation, whereas the binding of CRK DOCK180 induces Rac1-mediated activation of cellular migration. The activity of the different splicing isoforms varies greatly with CRKI displaying substantial transforming activity, CRKII less so, and phosphorylated CRKII with no biological activity whatsoever. CRKII has a linker region with a phosphorylated Tyr and an additional C-terminal SH3 domain. The phosphorylated Tyr creates a binding site for its SH2 domain which disrupts the association between CRK and its SH2 target proteins. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198180 [Multi-domain] Cd Length: 106 Bit Score: 41.69 E-value: 2.66e-04
|
||||||||||
| SH2_Nck_family | cd09943 | Src homology 2 (SH2) domain found in the Nck family; Nck proteins are adaptors that modulate ... |
254-310 | 3.53e-04 | ||||||
Src homology 2 (SH2) domain found in the Nck family; Nck proteins are adaptors that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. There are two members known in this family: Nck1 (Nckalpha) and Nck2 (Nckbeta and Growth factor receptor-bound protein 4 (Grb4)). They are characterized by having 3 SH3 domains and a C-terminal SH2 domain. Nck1 and Nck2 have overlapping functions as determined by gene knockouts. Both bind receptor tyrosine kinases and other tyrosine-phosphorylated proteins through their SH2 domains. In addition they also bind distinct targets. Neuronal signaling proteins: EphrinB1, EphrinB2, and Disabled-1 (Dab-1) all bind to Nck-2 exclusively. And in the case of PDGFR, Tyr(P)751 binds to Nck1 while Tyr(P)1009 binds to Nck2. Nck1 and Nck2 have a role in the infection process of enteropathogenic Escherichia coli (EPEC). Their SH3 domains are involved in recruiting and activating the N-WASP/Arp2/3 complex inducing actin polymerization resulting in the production of pedestals, dynamic bacteria-presenting protrusions of the plasma membrane. A similar thing occurs in the vaccinia virus where motile plasma membrane projections are formed beneath the virus. Recently it has been shown that the SH2 domains of both Nck1 and Nck2 bind the G-protein coupled receptor kinase-interacting protein 1 (GIT1) in a phosphorylation-dependent manner. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198196 Cd Length: 93 Bit Score: 40.96 E-value: 3.53e-04
|
||||||||||
| HMG-box_BHMG1 | cd21977 | high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing ... |
1351-1399 | 4.30e-04 | ||||||
high mobility group (HMG)-box found in basic helix-loop-helix and HMG box domain-containing protein 1 (BHMG1) and similar proteins; BHMG1 is an uncharacterized HMG-box containing protein that contains a degenerate basic motif not likely to bind DNA. Pssm-ID: 438793 [Multi-domain] Cd Length: 66 Bit Score: 39.99 E-value: 4.30e-04
|
||||||||||
| HMG-box_SoxF_SOX7 | cd22046 | high mobility group (HMG)-box found in sex determining region Y (SRY)-box 7 (SOX7) and similar ... |
1335-1399 | 5.32e-04 | ||||||
high mobility group (HMG)-box found in sex determining region Y (SRY)-box 7 (SOX7) and similar proteins; SOX-7 is an endothelial-associated transcription factor that acts as a tumor suppressor in a number of cancer types. It binds the DNA sequence 5'-AACAAT-3'. SOX-7 belongs to the group F of SRY-related high-mobility group (HMG) box (Sox) transcription factors. Pssm-ID: 438849 [Multi-domain] Cd Length: 88 Bit Score: 40.44 E-value: 5.32e-04
|
||||||||||
| SH2_Grb2_like | cd09941 | Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar ... |
255-305 | 6.95e-04 | ||||||
Src homology 2 domain found in Growth factor receptor-bound protein 2 (Grb2) and similar proteins; The adaptor proteins here include homologs Grb2 in humans, Sex muscle abnormal protein 5 (Sem-5) in Caenorhabditis elegans, and Downstream of receptor kinase (drk) in Drosophila melanogaster. They are composed of one SH2 and two SH3 domains. Grb2/Sem-5/drk regulates the Ras pathway by linking the tyrosine kinases to the Ras guanine nucleotide releasing protein Sos, which converts Ras to the active GTP-bound state. The SH2 domain of Grb2/Sem-5/drk binds class II phosphotyrosyl peptides while its SH3 domain binds to Sos and Sos-derived, proline-rich peptides. Besides it function in Ras signaling, Grb2 is also thought to play a role in apoptosis. Unlike most SH2 structures in which the peptide binds in an extended conformation (such that the +3 peptide residue occupies a hydrophobic pocket in the protein, conferring a modest degree of selectivity), Grb2 forms several hydrogen bonds via main chain atoms with the side chain of +2 Asn. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 199828 Cd Length: 95 Bit Score: 40.33 E-value: 6.95e-04
|
||||||||||
| HMG-box_PB1 | cd21984 | high mobility group (HMG)-box found in protein polybromo-1 (PB1) and similar proteins; PB1, ... |
1346-1401 | 7.00e-04 | ||||||
high mobility group (HMG)-box found in protein polybromo-1 (PB1) and similar proteins; PB1, also called BRG1-associated factor 180 (BAF180), or polybromo-1D, is a subunit of the PBAF (polybromo/Brg1-associated factor) chromatin-remodeling complex required for kinetochore localization during mitosis and the transcription of estrogen-responsive genes. It is involved in transcriptional activation and repression of select genes by chromatin remodeling. It acts as a negative regulator of cell proliferation. Pssm-ID: 438800 [Multi-domain] Cd Length: 60 Bit Score: 39.15 E-value: 7.00e-04
|
||||||||||
| WD40 | pfam00400 | WD domain, G-beta repeat; |
325-355 | 7.94e-04 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 7.94e-04
|
||||||||||
| WD40 | smart00320 | WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
553-581 | 9.54e-04 | ||||||
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain. Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 38.06 E-value: 9.54e-04
|
||||||||||
| HMG-box_PMS1 | cd21985 | high mobility group (HMG)-box found in PMS1 protein homolog 1 (PMS1) and similar proteins; ... |
1346-1417 | 1.09e-03 | ||||||
high mobility group (HMG)-box found in PMS1 protein homolog 1 (PMS1) and similar proteins; PMS1, also called DNA mismatch repair protein PMS1, is probably involved in the repair of mismatches in DNA. Pssm-ID: 438801 [Multi-domain] Cd Length: 73 Bit Score: 39.07 E-value: 1.09e-03
|
||||||||||
| SH2_cSH2_p85_like | cd09930 | C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ... |
257-292 | 1.19e-03 | ||||||
C-terminal Src homology 2 (cSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, a inter SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and 2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: 1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, 2) p85 iSH2 domain with C2 domain of p110alpha, and 3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198184 Cd Length: 104 Bit Score: 39.70 E-value: 1.19e-03
|
||||||||||
| SH2_Src_Src42 | cd10370 | Src homology 2 (SH2) domain found in the Src oncogene at 42A (Src42); Src42 is a member of the ... |
255-307 | 1.23e-03 | ||||||
Src homology 2 (SH2) domain found in the Src oncogene at 42A (Src42); Src42 is a member of the Src non-receptor type tyrosine kinase family of proteins. The integration of receptor tyrosine kinase-induced RAS and Src42 signals by Connector eNhancer of KSR (CNK) as a two-component input is essential for RAF activation in Drosophila. Src42 is present in a wide variety of organisms including: California sea hare, pea aphid, yellow fever mosquito, honey bee, Panamanian leafcutter ant, and sea urchin. Src42 has a unique N-terminal domain, an SH3 domain, an SH2 domain, a kinase domain and a regulatory tail, as do the other members of the family. Like the other members of the Src family the SH2 domain in addition to binding the target, also plays an autoinhibitory role by binding to its C-terminal tail. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198233 Cd Length: 96 Bit Score: 39.41 E-value: 1.23e-03
|
||||||||||
| HMG-box_UBF1_rpt4 | cd22001 | fourth high mobility group (HMG)-box found in upstream-binding factor 1 (UBF1) and similar ... |
1346-1391 | 1.43e-03 | ||||||
fourth high mobility group (HMG)-box found in upstream-binding factor 1 (UBF1) and similar proteins; UBF1, also called UBTF, nucleolar transcription factor 1, or auto-antigen NOR-90, is a nucleolar transcription factor that recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. UBF1 contains six HMG-box domains. This model corresponds to the fourth one. Pssm-ID: 438817 [Multi-domain] Cd Length: 66 Bit Score: 38.43 E-value: 1.43e-03
|
||||||||||
| HMG-box_AtHMGB6-like_rpt1 | cd22006 | first high mobility group (HMG)-box found in Arabidopsis thaliana high mobility group B ... |
1346-1399 | 1.43e-03 | ||||||
first high mobility group (HMG)-box found in Arabidopsis thaliana high mobility group B protein 6 (HMGB6) and similar proteins; HMGB6, also called nucleosome/chromatin assembly factor group D 06 (or D 6), WRKY transcription factor 53 (WRKY53), or WRKY DNA-binding protein 53, is a master regulator of age-induced leaf senescence. It acts in a complex transcription factor signaling network regulating senescence specific gene expression; hydrogen peroxide might be involved in signal transduction. The subfamily also includes Arabidopsis thaliana HMGB13 (also known as nucleosome/chromatin assembly factor group D 13). Both HMGB6 and HMGB13 contain three HMG-box domains. This model corresponds to the first one. Pssm-ID: 438822 [Multi-domain] Cd Length: 68 Bit Score: 38.59 E-value: 1.43e-03
|
||||||||||
| SH2_nSH2_p85_like | cd09942 | N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are ... |
246-283 | 1.47e-03 | ||||||
N-terminal Src homology 2 (nSH2) domain found in p85; Phosphoinositide 3-kinases (PI3Ks) are essential for cell growth, migration, and survival. p110, the catalytic subunit, is composed of an adaptor-binding domain, a Ras-binding domain, a C2 domain, a helical domain, and a kinase domain. The regulatory unit is called p85 and is composed of an SH3 domain, a RhoGap domain, a N-terminal SH2 (nSH2) domain, an internal SH2 (iSH2) domain, and C-terminal (cSH2) domain. There are 2 inhibitory interactions between p110alpha and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110alpha and (2) p85 iSH2 domain with C2 domain of p110alpha. There are 3 inhibitory interactions between p110beta and p85 of P13K: (1) p85 nSH2 domain with the C2, helical, and kinase domains of p110beta, (2) p85 iSH2 domain with C2 domain of p110alpha, and (3) p85 cSH2 domain with the kinase domain of p110alpha. It is interesting to note that p110beta is oncogenic as a wild type protein while p110alpha lacks this ability. One explanation is the idea that the regulation of p110beta by p85 is unique because of the addition of inhibitory contacts from the cSH2 domain and the loss of contacts in the iSH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198195 Cd Length: 110 Bit Score: 39.61 E-value: 1.47e-03
|
||||||||||
| HMG-box_SoxC | cd22029 | high mobility group (HMG)-box found in group C SRY-related high-mobility group (HMG) box (Sox) ... |
1346-1398 | 1.64e-03 | ||||||
high mobility group (HMG)-box found in group C SRY-related high-mobility group (HMG) box (Sox) transcription factors; SoxC transcription factors includes three members: SOX4, SOX11 and SOX12. They play key roles, often in redundancy, in multiple developmental pathways, including neurogenesis and skeletogenesis. SOX-4 is a transcriptional activator that promotes neuronal differentiation both in the adult and embryonic neural progenitors. It binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif. SOX-4 is abnormally expressed in various cancers. SOX-11 is a neural transcriptional factor involved in precursor survival, neuronal fate determination, migration and morphogenesis. SOX-12, also called SOX-22, is a transcription factor essential for embryonic development and cell fate determination. It binds to the sequence 5'-AACAAT-3'. Pssm-ID: 438838 [Multi-domain] Cd Length: 76 Bit Score: 38.57 E-value: 1.64e-03
|
||||||||||
| HMG-box_ABF2_IXR1-like_rpt2 | cd22012 | second high mobility group (HMG)-box found in Saccharomyces cerevisiae mitochondrial ... |
1346-1391 | 1.79e-03 | ||||||
second high mobility group (HMG)-box found in Saccharomyces cerevisiae mitochondrial ARS-binding factor 2 (ABF2), intrastrand cross-link recognition protein (Ixr1) and similar proteins; ABF2 is a close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. It specifically binds to the autonomously replicating sequence 1 (ARS1). It might play a positive role in gene expression and replication. Ixr1, also called structure-specific recognition protein (SSRP), is a homolog of the yeast mitochondrial regulator ABF2. It binds to platinated DNA and confers sensitivity to the anticancer drug cisplatin. Both ABF2 and Ixr1 contain two HMG-box domains. This model corresponds to the second one. Pssm-ID: 438828 [Multi-domain] Cd Length: 64 Bit Score: 38.04 E-value: 1.79e-03
|
||||||||||
| HMG-box_HMGXB4 | cd21982 | high mobility group (HMG)-box found in HMG domain-containing protein 4 (HMGXB4) and similar ... |
1346-1399 | 2.00e-03 | ||||||
high mobility group (HMG)-box found in HMG domain-containing protein 4 (HMGXB4) and similar proteins; HMGXB4, also called HMG box-containing protein 4, high mobility group protein 2-like 1 (HMG2L1), or protein HMGBCG, is a non-histone chromosomal protein that negatively regulates Wnt/beta-catenin signaling during development. It plays a role in the hematopoietic system. Pssm-ID: 438798 [Multi-domain] Cd Length: 61 Bit Score: 38.03 E-value: 2.00e-03
|
||||||||||
| SH2_SLAP | cd10344 | Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of ... |
261-313 | 2.14e-03 | ||||||
Src homology 2 domain found in Src-like adaptor proteins; SLAP belongs to the subfamily of adapter proteins that negatively regulate cellular signaling initiated by tyrosine kinases. It has a myristylated N-terminus, SH3 and SH2 domains with high homology to Src family tyrosine kinases, and a unique C-terminal tail, which is important for c-Cbl binding. SLAP negatively regulates platelet-derived growth factor (PDGF)-induced mitogenesis in fibroblasts and regulates F-actin assembly for dorsal ruffles formation. c-Cbl mediated SLAP inhibition towards actin remodeling. Moreover, SLAP enhanced PDGF-induced c-Cbl phosphorylation by SFK. In contrast, SLAP mitogenic inhibition was not mediated by c-Cbl, but it rather involved a competitive mechanism with SFK for PDGF-receptor (PDGFR) association and mitogenic signaling. Accordingly, phosphorylation of the Src mitogenic substrates Stat3 and Shc were reduced by SLAP. Thus, we concluded that SLAP regulates PDGFR signaling by two independent mechanisms: a competitive mechanism for PDGF-induced Src mitogenic signaling and a non-competitive mechanism for dorsal ruffles formation mediated by c-Cbl. SLAP is a hematopoietic adaptor containing Src homology (SH)3 and SH2 motifs and a unique carboxy terminus. Unlike c-Src, SLAP lacks a tyrosine kinase domain. Unlike c-Src, SLAP does not impact resorptive function of mature osteoclasts but induces their early apoptosis. SLAP negatively regulates differentiation of osteoclasts and proliferation of their precursors. Conversely, SLAP decreases osteoclast death by inhibiting activation of caspase 3. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 198207 Cd Length: 104 Bit Score: 39.01 E-value: 2.14e-03
|
||||||||||
| HMG-box_ABF2-like_rpt1 | cd22010 | first high mobility group (HMG)-box found in Saccharomyces cerevisiae mitochondrial ... |
1346-1399 | 2.92e-03 | ||||||
first high mobility group (HMG)-box found in Saccharomyces cerevisiae mitochondrial ARS-binding factor 2 (ABF2) and similar proteins; ABF2 is a close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. It specifically binds to the autonomously replicating sequence 1 (ARS1). It might play a positive role in gene expression and replication. ABF2 contains two HMG-box domains. This model corresponds to the first one. Pssm-ID: 438826 [Multi-domain] Cd Length: 68 Bit Score: 37.52 E-value: 2.92e-03
|
||||||||||
| HMG-box_SoxC_SOX12 | cd22038 | high mobility group (HMG)-box found in sex determining region Y (SRY)-box 12 (SOX12) and ... |
1346-1416 | 3.34e-03 | ||||||
high mobility group (HMG)-box found in sex determining region Y (SRY)-box 12 (SOX12) and similar proteins; SOX-12, also called SOX-22, is a transcription factor essential for embryonic development and cell fate determination. It binds to the sequence 5'-AACAAT-3'. SOX-12 belongs to the group C of SRY-related high-mobility group (HMG) box (Sox) transcription factors. Pssm-ID: 438847 [Multi-domain] Cd Length: 88 Bit Score: 38.12 E-value: 3.34e-03
|
||||||||||
| SH2_SH2D2A_SH2D7 | cd10349 | Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); ... |
255-307 | 3.87e-03 | ||||||
Src homology 2 domain found in the SH2 domain containing protein 2A and 7 (SH2D2A and SH2D7); SH2D2A and SH7 both contain a single SH2 domain. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. Pssm-ID: 199830 Cd Length: 77 Bit Score: 37.50 E-value: 3.87e-03
|
||||||||||
| HMG-box_HMGB_rpt2 | cd21979 | second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; ... |
1346-1398 | 4.30e-03 | ||||||
second high mobility group (HMG)-box found in the high mobility group protein B (HMGB) family; HMGB proteins are chromatin-associated nuclear proteins that act as architectural factors in nucleoprotein structures, which regulate DNA-dependent processes including transcription. In mammals, four family members are present: HMGB1, HMGB2, HMGB3 and HMGB4. They regulate the expression of a wide range of genes through architectural remodeling of the chromatin structure. HMGB1, also called high mobility group protein 1 (HMG-1), is a prototypical alarmin or damage-associated molecular pattern (DAMP) molecule when released from cells. It plays important roles in the regulation of a wide range of processes, including transcription, replication, DNA repair, and nucleosome formation, in the nucleus. It also plays multiple roles in regulating inflammation and responses to cell and tissue stress. HMGB2, also called high mobility group protein 2 (HMG-2), has been implicated in numerous cellular processes, including proliferation, differentiation, apoptosis, and tumor growth. It acts as a chromatin-associated nonhistone protein involved in transcriptional regulation and nucleic-acid-mediated innate immune responses in mammalian. It binds DNA to stabilize nucleosomes and promote transcription. HMGB3, also called high mobility group protein 2a (HMG-2a), or high mobility group protein 4 (HMG-4), is an X-linked member of HMGB family and functions as a universal sentinel for nucleic acid-mediated innate immune responses. HMGB3 has been implicated in the regulation of cellular proliferation and differentiation, as well as inflammatory response. HMGB4 is expressed by neuronal cells and affects the expression of genes involved in neural differentiation. It is a factor that regulates chromatin and expression of neuronal differentiation markers. The family also includes high mobility group protein B1 pseudogene 1 (HMGB1P1) and nuclear auto-antigen Sp-100. HMGB1P1, also called putative high mobility group protein B1-like 1 (HMGB1L1), or putative high mobility group protein 1-like 1 (HMG-1L1), is an HMG-box containing protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. Sp-100, also called nuclear dot-associated Sp100 protein, or speckled 100 kDa. It is a tumor suppressor that is a major constituent of the promyelocytic leukemia (PML) bodies, a subnuclear organelle involved in many physiological processes including cell growth, differentiation and apoptosis. Through the regulation of ETS1, Sp-100 may play a role in angiogenesis, controlling endothelial cell motility and invasion. It may also play roles in the regulation of telomeres lengthening, TP53-mediated transcription, FAS-mediated apoptosis, etc. In addition, the family includes Drosophila melanogaster high mobility group protein DSP1 (dDSP1) and similar proteins. dDSP1, also called protein dorsal switch 1, is a Drosophila HMG1 protein that binds preferentially single-stranded DNA and unwinds double-stranded DNA. It converts Dorsal and nuclear factor (NF)-kappa B from transcriptional activators to repressors. Members of the HMGB family contain two HMG-box domains. This model corresponds to the second one. Pssm-ID: 438795 [Multi-domain] Cd Length: 71 Bit Score: 37.39 E-value: 4.30e-03
|
||||||||||
| WD40 | pfam00400 | WD domain, G-beta repeat; |
553-581 | 9.50e-03 | ||||||
WD domain, G-beta repeat; Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.40 E-value: 9.50e-03
|
||||||||||
| HMG-box_SoxC_SOX4 | cd22036 | high mobility group (HMG)-box found in sex determining region Y (SRY)-box 4 (SOX4) and similar ... |
1346-1415 | 9.55e-03 | ||||||
high mobility group (HMG)-box found in sex determining region Y (SRY)-box 4 (SOX4) and similar proteins; SOX-4 is a transcriptional activator that promotes neuronal differentiation both in the adult and embryonic neural progenitors. It binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif. SOX-4 is abnormally expressed in various cancers. SOX-4 belongs to group C SRY-related high-mobility group (HMG) box (Sox) transcription factors. Pssm-ID: 438845 [Multi-domain] Cd Length: 79 Bit Score: 36.65 E-value: 9.55e-03
|
||||||||||
| Blast search parameters | ||||
|
