| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-619930,
cpath:CPATH-LOCAL-619930,
cpath:CPATH-LOCAL-619931,
cpath:CPATH-LOCAL-619931,
cpath:CPATH-LOCAL-619932,
cpath:CPATH-LOCAL-619932,
cpath:CPATH-LOCAL-619933,
cpath:CPATH-LOCAL-619933,
cpath:CPATH-LOCAL-619934,
cpath:CPATH-LOCAL-619934,
cpath:CPATH-LOCAL-619935,
cpath:CPATH-LOCAL-619935,
cpath:CPATH-LOCAL-619936,
cpath:CPATH-LOCAL-619936,
cpath:CPATH-LOCAL-619937,
cpath:CPATH-LOCAL-619937,
cpath:CPATH-LOCAL-619938,
cpath:CPATH-LOCAL-619938,
cpath:CPATH-LOCAL-619939,
cpath:CPATH-LOCAL-619939,
cpath:CPATH-LOCAL-619940,
cpath:CPATH-LOCAL-619940,
cpath:CPATH-LOCAL-619941,
cpath:CPATH-LOCAL-619941,
cpath:CPATH-LOCAL-619942,
cpath:CPATH-LOCAL-619942,
cpath:CPATH-LOCAL-619943,
cpath:CPATH-LOCAL-619943,
cpath:CPATH-LOCAL-619944,
cpath:CPATH-LOCAL-619944,
cpath:CPATH-LOCAL-619945,
cpath:CPATH-LOCAL-619945,
cpath:CPATH-LOCAL-619946,
cpath:CPATH-LOCAL-619946,
cpath:CPATH-LOCAL-619947,
cpath:CPATH-LOCAL-619947,
cpath:CPATH-LOCAL-619948,
cpath:CPATH-LOCAL-619948,
cpath:CPATH-LOCAL-619949,
cpath:CPATH-LOCAL-619949,
cpath:CPATH-LOCAL-619950,
cpath:CPATH-LOCAL-619950,
cpath:CPATH-LOCAL-619951,
cpath:CPATH-LOCAL-619951,
cpath:CPATH-LOCAL-619952,
cpath:CPATH-LOCAL-619952,
cpath:CPATH-LOCAL-619953,
cpath:CPATH-LOCAL-619953,
cpath:CPATH-LOCAL-619954,
cpath:CPATH-LOCAL-619954,
cpath:CPATH-LOCAL-619955,
cpath:CPATH-LOCAL-619955,
cpath:CPATH-LOCAL-619956,
cpath:CPATH-LOCAL-619956,
cpath:CPATH-LOCAL-619957,
cpath:CPATH-LOCAL-619957,
cpath:CPATH-LOCAL-619958,
cpath:CPATH-LOCAL-619958,
cpath:CPATH-LOCAL-619959,
cpath:CPATH-LOCAL-619959,
cpath:CPATH-LOCAL-619960,
cpath:CPATH-LOCAL-619960,
cpath:CPATH-LOCAL-619961,
cpath:CPATH-LOCAL-619961,
cpath:CPATH-LOCAL-619962,
cpath:CPATH-LOCAL-619962,
cpath:CPATH-LOCAL-619963,
cpath:CPATH-LOCAL-619963,
cpath:CPATH-LOCAL-626839,
cpath:CPATH-LOCAL-626839
|
| http://www.biopax.org/relea... |
Fibronectin,
Fibronectin
|
| http://www.biopax.org/relea... |
FINC_HUMAN,
FINC_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Anastellin,
Anastellin,
CIG,
CIG,
Cold-insoluble globulin,
Cold-insoluble globulin,
FN,
FN,
Ugl-Y1,
Ugl-Y1,
Ugl-Y2,
Ugl-Y2,
Ugl-Y3,
Ugl-Y3
|
| http://www.biopax.org/relea... |
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. FUNCTION: Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. SUBUNIT: Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=15; Comment=Additional isoforms seem to exist; Name=1; IsoId=P02751-1; Sequence=Displayed; Name=2; Synonyms=MSF-FN70, Migration stimulation factor FN70; IsoId=P02751-2; Sequence=VSP_003255, VSP_003256, VSP_003257; Name=3; Synonyms=V89; IsoId=P02751-3; Sequence=VSP_008110; Name=4; Synonyms=Fibronectin III-15X; IsoId=P02751-4; Sequence=VSP_008107, VSP_008111, VSP_008112; Name=5; Synonyms=Fibronectin (V+I-10)-; IsoId=P02751-5; Sequence=VSP_008107, VSP_008113; Name=6; Synonyms=Fibronectin (V+III-15)-; IsoId=P02751-6; Sequence=VSP_008109; Name=7; Synonyms=Fibronectin containing extra ED-B domain; IsoId=P02751-7; Sequence=VSP_008104, VSP_008110; Name=8; Synonyms=Fibronectin not containing EIIIA domain; IsoId=P02751-8; Sequence=VSP_008106; Name=9; Synonyms=Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region; IsoId=P02751-9; Sequence=VSP_008106, VSP_008108, VSP_008110; Name=10; IsoId=P02751-10; Sequence=VSP_008106, VSP_008107; Name=11; Synonyms=Fibronectin containing extra type III repeat (EDII), exon x+2; IsoId=P02751-11; Sequence=VSP_008105; Name=12; IsoId=P02751-12; Sequence=VSP_013681, VSP_008106, VSP_008108, VSP_008110; Name=13; IsoId=P02751-13; Sequence=VSP_008104, VSP_008106, VSP_008107; Note=No experimental confirmation available; Name=14; IsoId=P02751-14; Sequence=VSP_008106, VSP_008110; Name=15; IsoId=P02751-15; Sequence=VSP_008104; Note=No experimental confirmation available; TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine. DEVELOPMENTAL STAGE: Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. PTM: Sulfated. PTM: It is not known whether both or only one of Thr-2064 and Thr- 2065 are/is glycosylated. PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). PTM: Phosphorylation sites are present in the extracelllular medium. PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. DISEASE: Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life. SIMILARITY: Contains 12 fibronectin type-I domains. SIMILARITY: Contains 2 fibronectin type-II domains. SIMILARITY: Contains 16 fibronectin type-III domains. SEQUENCE CAUTION: Sequence=AAX76513.1; Type=Erroneous gene model prediction; Sequence=BAD93077.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD91166.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD97964.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD97965.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAH18136.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Wikipedia; Note=Fibronectin entry; URL="http://en.wikipedia.org/wiki/Fibronectin"; GENE SYNONYMS: FN. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. FUNCTION: Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. SUBUNIT: Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=15; Comment=Additional isoforms seem to exist; Name=1; IsoId=P02751-1; Sequence=Displayed; Name=2; Synonyms=MSF-FN70, Migration stimulation factor FN70; IsoId=P02751-2; Sequence=VSP_003255, VSP_003256, VSP_003257; Name=3; Synonyms=V89; IsoId=P02751-3; Sequence=VSP_008110; Name=4; Synonyms=Fibronectin III-15X; IsoId=P02751-4; Sequence=VSP_008107, VSP_008111, VSP_008112; Name=5; Synonyms=Fibronectin (V+I-10)-; IsoId=P02751-5; Sequence=VSP_008107, VSP_008113; Name=6; Synonyms=Fibronectin (V+III-15)-; IsoId=P02751-6; Sequence=VSP_008109; Name=7; Synonyms=Fibronectin containing extra ED-B domain; IsoId=P02751-7; Sequence=VSP_008104, VSP_008110; Name=8; Synonyms=Fibronectin not containing EIIIA domain; IsoId=P02751-8; Sequence=VSP_008106; Name=9; Synonyms=Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region; IsoId=P02751-9; Sequence=VSP_008106, VSP_008108, VSP_008110; Name=10; IsoId=P02751-10; Sequence=VSP_008106, VSP_008107; Name=11; Synonyms=Fibronectin containing extra type III repeat (EDII), exon x+2; IsoId=P02751-11; Sequence=VSP_008105; Name=12; IsoId=P02751-12; Sequence=VSP_013681, VSP_008106, VSP_008108, VSP_008110; Name=13; IsoId=P02751-13; Sequence=VSP_008104, VSP_008106, VSP_008107; Note=No experimental confirmation available; Name=14; IsoId=P02751-14; Sequence=VSP_008106, VSP_008110; Name=15; IsoId=P02751-15; Sequence=VSP_008104; Note=No experimental confirmation available; TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine. DEVELOPMENTAL STAGE: Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. PTM: Sulfated. PTM: It is not known whether both or only one of Thr-2064 and Thr- 2065 are/is glycosylated. PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). PTM: Phosphorylation sites are present in the extracelllular medium. PTM: Proteolytic processing produces the C-terminal NC1 peptide, anastellin. DISEASE: Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life. SIMILARITY: Contains 12 fibronectin type-I domains. SIMILARITY: Contains 2 fibronectin type-II domains. SIMILARITY: Contains 16 fibronectin type-III domains. SEQUENCE CAUTION: Sequence=AAX76513.1; Type=Erroneous gene model prediction; Sequence=BAD93077.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD91166.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD97964.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAD97965.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAH18136.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Wikipedia; Note=Fibronectin entry; URL="http://en.wikipedia.org/wiki/Fibronectin"; GENE SYNONYMS: FN. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| skos:exactMatch |