integrin beta-1-binding protein 1 isoform 2 [Homo sapiens]
Protein Classification
PH domain-containing protein( domain architecture ID 106840)
Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner
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 ... |
1-150 | 5.45e-83 | ||||
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 pfam10480: Pssm-ID: 473070 Cd Length: 200 Bit Score: 242.29 E-value: 5.45e-83
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| Name | Accession | Description | Interval | E-value | ||||
| ICAP-1_inte_bdg | pfam10480 | Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ... |
1-150 | 5.45e-83 | ||||
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state, Pssm-ID: 119000 Cd Length: 200 Bit Score: 242.29 E-value: 5.45e-83
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| PTB_ICAP1 | cd13163 | Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ... |
61-141 | 6.18e-37 | ||||
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal 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 is part of the Dab-like subgroup. Pssm-ID: 269985 Cd Length: 129 Bit Score: 122.95 E-value: 6.18e-37
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
58-126 | 4.22e-05 | ||||
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: 40.76 E-value: 4.22e-05
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| Name | Accession | Description | Interval | E-value | ||||
| ICAP-1_inte_bdg | pfam10480 | Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the ... |
1-150 | 5.45e-83 | ||||
Beta-1 integrin binding protein; ICAP-1 is a serine/threonine-rich protein that binds to the cytoplasmic domains of beta-1 integrins in a highly specific manner, binding to a NPXY sequence motif on the beta-1 integrin. The cytoplasmic domains of integrins are essential for cell adhesion, and the fact that phosphorylation of ICAP-1 by interaction with the cell-matrix implies an important role of ICAP-1 during integrin-dependent cell adhesion. Overexpression of ICAP-1 strongly reduces the integrin-mediated cell spreading on extracellular matrix and inhibits both Cdc42 and Rac1. In addition, ICAP-1 induces release of Cdc42 from cellular membranes and prevents the dissociation of GDP from this GTPase. An additional function of ICAP-1 is to promote differentiation of osteoprogenitors by supporting their condensation through modulating the integrin high affinity state, Pssm-ID: 119000 Cd Length: 200 Bit Score: 242.29 E-value: 5.45e-83
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| PTB_ICAP1 | cd13163 | Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also ... |
61-141 | 6.18e-37 | ||||
Integrin beta-1-binding protein 1 Phosphotyrosine-binding (PTB) PH-like fold; ICAP1 (also called Integrin cytoplasmic domain-associated protein 1) binds specifically to the beta1 integrin subunit cytoplasmic domain and the cerebral cavernous malformation (CCM) protein CCM1. It regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation. ICAP1 recruits CCM1 to the cell membrane and activates CCM1 by changing its conformation. Since CCM1 plays role in cardiovascular development, it is hypothesized ICAP1 is involved in vascular differentiation. ICAP-1 has an N-terminal domain that rich in serine and threonine and a C-terminal 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 is part of the Dab-like subgroup. Pssm-ID: 269985 Cd Length: 129 Bit Score: 122.95 E-value: 6.18e-37
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| PTB | smart00462 | Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ... |
58-126 | 4.22e-05 | ||||
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: 40.76 E-value: 4.22e-05
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| Blast search parameters | ||||
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