| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-315971,
cpath:CPATH-LOCAL-315971,
cpath:CPATH-LOCAL-315972,
cpath:CPATH-LOCAL-315972,
cpath:CPATH-LOCAL-315973,
cpath:CPATH-LOCAL-315973,
cpath:CPATH-LOCAL-315974,
cpath:CPATH-LOCAL-315974,
cpath:CPATH-LOCAL-315975,
cpath:CPATH-LOCAL-315975,
cpath:CPATH-LOCAL-315976,
cpath:CPATH-LOCAL-315976,
cpath:CPATH-LOCAL-315977,
cpath:CPATH-LOCAL-315977,
cpath:CPATH-LOCAL-322000,
cpath:CPATH-LOCAL-322000
|
| http://www.biopax.org/relea... |
Vitronectin,
Vitronectin
|
| http://www.biopax.org/relea... |
VTNC_HUMAN,
VTNC_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
S-protein,
S-protein,
Serum-spreading factor,
Serum-spreading factor,
Somatomedin-B,
Somatomedin-B,
V75,
V75,
Vitronectin V10 subunit,
Vitronectin V10 subunit,
Vitronectin V65 subunit,
Vitronectin V65 subunit
|
| http://www.biopax.org/relea... |
FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. SUBUNIT: Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1 and insulin. SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Plasma. DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin. PTM: Sulfated on 2 tyrosine residues. PTM: N- and O-glycosylated (By similarity). PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both. PTM: Phosphorylation sites are present in the extracelllular medium. SIMILARITY: Contains 4 hemopexin-like domains. SIMILARITY: Contains 1 SMB (somatomedin-B) domain. WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/vtn/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway. FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity. SUBUNIT: Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1 and insulin. SUBCELLULAR LOCATION: Secreted, extracellular space. TISSUE SPECIFICITY: Plasma. DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin. PTM: Sulfated on 2 tyrosine residues. PTM: N- and O-glycosylated (By similarity). PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. PTM: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both. PTM: Phosphorylation sites are present in the extracelllular medium. SIMILARITY: Contains 4 hemopexin-like domains. SIMILARITY: Contains 1 SMB (somatomedin-B) domain. WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/vtn/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| skos:exactMatch | |
| skos:closeMatch |