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P02751

- FINC_HUMAN

UniProt

P02751 - FINC_HUMAN

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Protein

Fibronectin

Gene

FN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei663 – 6631Important for superfibronectin formation
Sitei666 – 6661Important for superfibronectin formation
Sitei2108 – 21081Not glycosylated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi907 – 1172266Add
BLAST

GO - Molecular functioni

  1. collagen binding Source: UniProtKB
  2. heparin binding Source: UniProtKB
  3. integrin binding Source: UniProtKB
  4. peptidase activator activity Source: Ensembl
  5. protease binding Source: BHF-UCL

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. angiogenesis Source: UniProtKB-KW
  3. blood coagulation Source: Reactome
  4. calcium-independent cell-matrix adhesion Source: Ensembl
  5. cell adhesion Source: UniProtKB
  6. cell-substrate junction assembly Source: Ensembl
  7. endodermal cell differentiation Source: UniProtKB
  8. extracellular matrix disassembly Source: Reactome
  9. extracellular matrix organization Source: Reactome
  10. integrin activation Source: UniProtKB
  11. leukocyte migration Source: Reactome
  12. peptide cross-linking Source: BHF-UCL
  13. platelet activation Source: Reactome
  14. platelet degranulation Source: Reactome
  15. positive regulation of axon extension Source: Ensembl
  16. regulation of cell shape Source: UniProtKB-KW
  17. response to wounding Source: UniProtKB
  18. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Acute phase, Angiogenesis, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118779. Extracellular matrix organization.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_160131. Fibronectin matrix formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Alternative name(s):
Cold-insoluble globulin
Short name:
CIG
Cleaved into the following 4 chains:
Gene namesi
Name:FN1
Synonyms:FN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3778. FN1.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. basal lamina Source: Ensembl
  3. blood microparticle Source: UniProt
  4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  5. extracellular matrix Source: UniProtKB
  6. extracellular region Source: UniProtKB
  7. extracellular space Source: BHF-UCL
  8. extracellular vesicular exosome Source: UniProtKB
  9. fibrinogen complex Source: BHF-UCL
  10. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti973 – 9731Y → C in GFND2. 1 Publication
VAR_043918
Natural varianti1834 – 18341W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 Publication
VAR_043919
Natural varianti1883 – 18831L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 Publication
VAR_043920

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi641 – 6411Y → A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683. 1 Publication
Mutagenesisi642 – 6421I → A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692. 1 Publication
Mutagenesisi663 – 6631L → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 K but abolishes polymerization activity; when associated with A-666. 2 Publications
Mutagenesisi666 – 6661Y → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 kinase but abolishes polymerization activity; when associated with A-663. 2 Publications
Mutagenesisi681 – 6811L → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683. 1 Publication
Mutagenesisi682 – 6821I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692. 1 Publication
Mutagenesisi683 – 6831S → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681. 1 Publication
Mutagenesisi684 – 6841I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692. 1 Publication
Mutagenesisi691 – 6911E → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696. 1 Publication
Mutagenesisi692 – 6921V → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684. 1 Publication
Mutagenesisi694 – 6941R → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696. 1 Publication
Mutagenesisi695 – 6951F → A: Loss of ability to form fibronectin aggregates; when associated with A-697. 1 Publication
Mutagenesisi696 – 6961D → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694. 1 Publication
Mutagenesisi697 – 6971F → A: Loss of ability to form fibronectin aggregates; when associated with A-695. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi601894. phenotype.
Orphaneti84090. Fibronectin glomerulopathy.
PharmGKBiPA28194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 23862355FibronectinPRO_0000019235Add
BLAST
Chaini627 – 70276AnastellinPRO_0000390479Add
BLAST
Chaini723 – 911189Ugl-Y1PRO_0000300249Add
BLAST
Chaini723 – 903181Ugl-Y2PRO_0000300250Add
BLAST
Chaini723 – ?Ugl-Y3PRO_0000300251

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Pyrrolidone carboxylic acid1 Publication
Cross-linki34 – 34Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki35 – 35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki47 – 47Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Disulfide bondi52 ↔ 78
Disulfide bondi76 ↔ 87
Disulfide bondi97 ↔ 125
Disulfide bondi123 ↔ 135
Disulfide bondi141 ↔ 169
Disulfide bondi167 ↔ 179
Disulfide bondi186 ↔ 215
Disulfide bondi213 ↔ 225
Disulfide bondi231 ↔ 260
Disulfide bondi258 ↔ 270
Glycosylationi279 – 2791O-linked (GalNAc...)1 Publication
Disulfide bondi308 ↔ 335
Disulfide bondi333 ↔ 342
Disulfide bondi360 ↔ 386
Disulfide bondi374 ↔ 401
Disulfide bondi420 ↔ 446
Glycosylationi430 – 4301N-linked (GlcNAc...)3 Publications
Disulfide bondi434 ↔ 461
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...) (complex)5 Publications
Glycosylationi542 – 5421N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei876 – 8761SulfotyrosineSequence Analysis
Glycosylationi877 – 8771N-linked (GlcNAc...)2 Publications
Modified residuei881 – 8811SulfotyrosineSequence Analysis
Glycosylationi1007 – 10071N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi1244 – 12441N-linked (GlcNAc...)2 Publications
Glycosylationi2064 – 20641O-linked (GalNAc...)1 Publication
Glycosylationi2065 – 20651O-linked (GalNAc...)1 Publication
Glycosylationi2108 – 21081N-linked (GlcNAc...)1 Publication
Disulfide bondi2206 ↔ 2235By similarity
Disulfide bondi2233 ↔ 2245By similarity
Disulfide bondi2251 ↔ 2278By similarity
Disulfide bondi2276 ↔ 2288By similarity
Disulfide bondi2295 ↔ 2319By similarity
Disulfide bondi2317 ↔ 2333By similarity
Disulfide bondi2367 – 2367Interchain (with C-2371)
Disulfide bondi2371 – 2371Interchain (with C-2367)
Modified residuei2384 – 23841Phosphoserine2 Publications

Post-translational modificationi

Sulfated.1 Publication
It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated.9 Publications
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).
Phosphorylation sites are present in the extracellular medium.2 Publications
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

MaxQBiP02751.
PaxDbiP02751.
PRIDEiP02751.

2D gel databases

DOSAC-COBS-2DPAGEP02751.

PTM databases

PhosphoSiteiP02751.
UniCarbKBiP02751.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age.2 Publications

Gene expression databases

BgeeiP02751.
ExpressionAtlasiP02751. baseline and differential.
GenevestigatoriP02751.

Organism-specific databases

HPAiCAB000126.
HPA027066.

Interactioni

Subunit structurei

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 and MYOC.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-1220319,EBI-6927928From a different organism.
CTGFP292795EBI-1220319,EBI-2835375
FBN1P355552EBI-1220319,EBI-2505934
FBN2P355562EBI-1220319,EBI-6164392
fnbAP1473818EBI-1220319,EBI-8398157From a different organism.
fnbBQ5368219EBI-1220319,EBI-8398005From a different organism.
FYNP062412EBI-7133890,EBI-515315
LPAP085192EBI-1220319,EBI-9232288
SCGB1A1P116843EBI-1220319,EBI-7797649
TGM2P219803EBI-1220319,EBI-727668
VHLP403372EBI-1220319,EBI-301246

Protein-protein interaction databases

BioGridi108621. 724 interactions.
DIPiDIP-29547N.
IntActiP02751. 454 interactions.
MINTiMINT-1779779.

Structurei

Secondary structure

1
2386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 543Combined sources
Beta strandi57 – 593Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 787Combined sources
Turni81 – 833Combined sources
Beta strandi85 – 895Combined sources
Beta strandi96 – 983Combined sources
Turni100 – 1023Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi119 – 1279Combined sources
Turni128 – 1314Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi161 – 17111Combined sources
Turni172 – 1754Combined sources
Beta strandi176 – 1816Combined sources
Beta strandi185 – 1884Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi200 – 2056Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 2179Combined sources
Turni218 – 2214Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi230 – 2334Combined sources
Turni234 – 2374Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi255 – 2628Combined sources
Turni263 – 2664Combined sources
Beta strandi267 – 2715Combined sources
Beta strandi302 – 3043Combined sources
Beta strandi307 – 3093Combined sources
Turni311 – 3133Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi321 – 3266Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi339 – 3446Combined sources
Turni353 – 3564Combined sources
Beta strandi360 – 3667Combined sources
Beta strandi369 – 3735Combined sources
Beta strandi381 – 3833Combined sources
Beta strandi385 – 3917Combined sources
Helixi392 – 3954Combined sources
Beta strandi398 – 4014Combined sources
Helixi403 – 4053Combined sources
Turni413 – 4175Combined sources
Beta strandi422 – 4265Combined sources
Beta strandi429 – 4335Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi445 – 4517Combined sources
Helixi452 – 4554Combined sources
Beta strandi458 – 4603Combined sources
Helixi465 – 4673Combined sources
Beta strandi469 – 4713Combined sources
Beta strandi477 – 4793Combined sources
Beta strandi483 – 4853Combined sources
Beta strandi490 – 4923Combined sources
Beta strandi495 – 5006Combined sources
Turni501 – 5044Combined sources
Beta strandi505 – 5139Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi523 – 5264Combined sources
Beta strandi529 – 5346Combined sources
Beta strandi540 – 5478Combined sources
Turni548 – 5514Combined sources
Beta strandi552 – 5576Combined sources
Beta strandi559 – 5624Combined sources
Turni564 – 5663Combined sources
Beta strandi569 – 5713Combined sources
Beta strandi575 – 5784Combined sources
Beta strandi585 – 5917Combined sources
Turni592 – 5954Combined sources
Beta strandi596 – 6016Combined sources
Beta strandi613 – 6153Combined sources
Beta strandi626 – 6316Combined sources
Beta strandi634 – 6363Combined sources
Beta strandi638 – 64710Combined sources
Turni648 – 6514Combined sources
Beta strandi655 – 6595Combined sources
Beta strandi661 – 6644Combined sources
Beta strandi665 – 6684Combined sources
Beta strandi673 – 68816Combined sources
Beta strandi690 – 69910Combined sources
Helixi732 – 7343Combined sources
Beta strandi736 – 7394Combined sources
Beta strandi747 – 75610Combined sources
Turni757 – 7593Combined sources
Beta strandi764 – 7696Combined sources
Beta strandi774 – 7774Combined sources
Beta strandi785 – 79410Combined sources
Beta strandi799 – 80810Combined sources
Beta strandi1178 – 11847Combined sources
Beta strandi1186 – 11894Combined sources
Beta strandi1191 – 11966Combined sources
Beta strandi1205 – 12128Combined sources
Turni1213 – 12153Combined sources
Beta strandi1221 – 12255Combined sources
Beta strandi1231 – 12333Combined sources
Beta strandi1243 – 12519Combined sources
Beta strandi1259 – 12635Combined sources
Beta strandi1271 – 12777Combined sources
Beta strandi1283 – 12886Combined sources
Beta strandi1296 – 13049Combined sources
Helixi1308 – 13103Combined sources
Beta strandi1312 – 13165Combined sources
Beta strandi1322 – 13254Combined sources
Beta strandi1333 – 134210Combined sources
Beta strandi1350 – 13556Combined sources
Beta strandi1362 – 13687Combined sources
Beta strandi1374 – 13796Combined sources
Beta strandi1386 – 13949Combined sources
Beta strandi1402 – 14065Combined sources
Beta strandi1412 – 14154Combined sources
Beta strandi1423 – 143210Combined sources
Beta strandi1440 – 14456Combined sources
Beta strandi1452 – 14609Combined sources
Beta strandi1463 – 14697Combined sources
Beta strandi1476 – 14849Combined sources
Turni1485 – 14906Combined sources
Beta strandi1492 – 14976Combined sources
Beta strandi1502 – 15054Combined sources
Beta strandi1513 – 152210Combined sources
Beta strandi1525 – 15273Combined sources
Beta strandi1534 – 15396Combined sources
Beta strandi1639 – 16446Combined sources
Beta strandi1647 – 16515Combined sources
Beta strandi1662 – 16687Combined sources
Turni1669 – 16713Combined sources
Beta strandi1672 – 16765Combined sources
Beta strandi1686 – 16894Combined sources
Beta strandi1696 – 17049Combined sources
Beta strandi1706 – 17083Combined sources
Beta strandi1714 – 17196Combined sources
Beta strandi1726 – 17338Combined sources
Beta strandi1738 – 17436Combined sources
Beta strandi1751 – 176313Combined sources
Beta strandi1766 – 17705Combined sources
Beta strandi1776 – 17794Combined sources
Beta strandi1787 – 179610Combined sources
Beta strandi1804 – 18096Combined sources
Beta strandi1818 – 18258Combined sources
Beta strandi1830 – 18356Combined sources
Beta strandi1843 – 185311Combined sources
Beta strandi1857 – 18615Combined sources
Beta strandi1866 – 18705Combined sources
Beta strandi1878 – 188710Combined sources
Beta strandi1895 – 19006Combined sources
Beta strandi1907 – 19159Combined sources
Beta strandi1918 – 19247Combined sources
Beta strandi1932 – 19387Combined sources
Beta strandi1957 – 19604Combined sources
Beta strandi1968 – 197710Combined sources
Beta strandi1985 – 19906Combined sources
Beta strandi2253 – 22553Combined sources
Beta strandi2263 – 22675Combined sources
Beta strandi2269 – 228012Combined sources
Turni2281 – 22844Combined sources
Beta strandi2285 – 22906Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E88NMR-A305-464[»]
1E8BNMR-A305-464[»]
1FBRNMR-A183-275[»]
1FNAX-ray1.80A1452-1542[»]
1FNFX-ray2.00A1173-1540[»]
1FNHX-ray2.80A1721-1991[»]
1J8KNMR-A1631-1724[»]
1O9ANMR-A48-140[»]
1OWWNMR-A608-701[»]
1Q38NMR-A631-705[»]
1QGBNMR-A48-140[»]
1QO6NMR-A305-405[»]
1TTFNMR-A1447-1540[»]
1TTGNMR-A1447-1540[»]
2CG6X-ray1.55A93-182[»]
2CG7X-ray1.20A93-182[»]
2CK2X-ray2.00A/B1447-1542[»]
2CKUNMR-A93-182[»]
2EC3NMR-A2239-2299[»]
2FN2NMR-A406-464[»]
2FNBNMR-A1265-1355[»]
2GEEX-ray2.01A1205-1356[»]
2H41NMR-A721-809[»]
2H45NMR-A721-809[»]
2HA1NMR-A609-809[»]
2OCFX-ray2.95D1447-1540[»]
2RKYX-ray1.80A/C183-275[»]
2RKZX-ray2.00A/B/C/D/E/F93-182[»]
2RL0X-ray2.00A/B/D/F/I/K184-272[»]
3CALX-ray1.70A/C93-182[»]
3EJHX-ray2.10A/B516-608[»]
3GXEX-ray2.60A/B516-608[»]
3M7PX-ray2.50A297-604[»]
3MQLX-ray3.00A308-515[»]
3R8QX-ray2.40A1721-1991[»]
3T1WX-ray2.40A1173-1448[»]
3ZRZX-ray1.70A/B93-182[»]
4GH7X-ray2.60B/D1173-1427[»]
4JE4X-ray2.31B1450-1540[»]
4JEGX-ray2.30B1450-1540[»]
4LXOX-ray1.42A/B1357-1540[»]
4MMXX-ray3.32C1448-1540[»]
4MMYX-ray3.18C1448-1540[»]
4MMZX-ray3.10C1448-1540[»]
4PZ5X-ray1.96A93-182[»]
ProteinModelPortaliP02751.
SMRiP02751. Positions 48-274, 297-606, 609-809, 1173-1540, 1631-1991, 2242-2299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 9041Fibronectin type-I 1PROSITE-ProRule annotationAdd
BLAST
Domaini95 – 13844Fibronectin type-I 2PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 18244Fibronectin type-I 3PROSITE-ProRule annotationAdd
BLAST
Domaini184 – 22845Fibronectin type-I 4PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 27345Fibronectin type-I 5PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 34540Fibronectin type-I 6PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 40349Fibronectin type-II 1PROSITE-ProRule annotationAdd
BLAST
Domaini415 – 46349Fibronectin type-II 2PROSITE-ProRule annotationAdd
BLAST
Domaini468 – 51144Fibronectin type-I 7PROSITE-ProRule annotationAdd
BLAST
Domaini516 – 55843Fibronectin type-I 8PROSITE-ProRule annotationAdd
BLAST
Domaini559 – 60244Fibronectin type-I 9PROSITE-ProRule annotationAdd
BLAST
Domaini610 – 70293Fibronectin type-III 1Add
BLAST
Domaini722 – 81291Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini813 – 90492Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini909 – 99890Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini999 – 108890Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini1089 – 117587Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini1176 – 126691Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1269 – 136193Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1362 – 144988Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1450 – 154394Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1544 – 163592Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini1636 – 172388Fibronectin type-III 12; extra domainPROSITE-ProRule annotationAdd
BLAST
Domaini1724 – 181794Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini1818 – 190487Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini1905 – 199591Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini2103 – 219795Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini2204 – 224845Fibronectin type-I 10PROSITE-ProRule annotationAdd
BLAST
Domaini2249 – 229143Fibronectin type-I 11PROSITE-ProRule annotationAdd
BLAST
Domaini2293 – 233644Fibronectin type-I 12PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 272221Fibrin- and heparin-binding 1Add
BLAST
Regioni308 – 608301Collagen-bindingAdd
BLAST
Regioni464 – 47714Critical for collagen bindingAdd
BLAST
Regioni1267 – 1540274Cell-attachmentAdd
BLAST
Regioni1721 – 1991271Heparin-binding 2Add
BLAST
Regioni1813 – 1991179Binds to FBLN1Add
BLAST
Regioni1992 – 2102111Connecting strand 3 (CS-3) (V region)Add
BLAST
Regioni2206 – 2337132Fibrin-binding 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1524 – 15263Cell attachment site

Sequence similaritiesi

Contains 12 fibronectin type-I domains.PROSITE-ProRule annotation
Contains 2 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 16 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119000.
HOVERGENiHBG005731.
InParanoidiP02751.
KOiK05717.
OMAiIPGHLNS.
OrthoDBiEOG7X9G60.
PhylomeDBiP02751.
TreeFamiTF329915.

Family and domain databases

Gene3Di2.10.10.10. 2 hits.
2.60.40.10. 16 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view]
PfamiPF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 16 hits.
[Graphical view]
SMARTiSM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 16 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 10 hits.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. EGF_1. 2 hits.
PS01253. FN1_1. 12 hits.
PS51091. FN1_2. 12 hits.
PS00023. FN2_1. 2 hits.
PS51092. FN2_2. 2 hits.
PS50853. FN3. 16 hits.
[Graphical view]

Sequences (17)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 17 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P02751-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP
60 70 80 90 100
GCYDNGKHYQ INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK
110 120 130 140 150
YTGNTYRVGD TYERPKDSMI WDCTCIGAGR GRISCTIANR CHEGGQSYKI
160 170 180 190 200
GDTWRRPHET GGYMLECVCL GNGKGEWTCK PIAEKCFDHA AGTSYVVGET
210 220 230 240 250
WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY RIGDTWSKKD
260 270 280 290 300
NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP
310 320 330 340 350
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHTVLVQT RGGNSNGALC HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDM GHMMRCTCVG
510 520 530 540 550
NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS
660 670 680 690 700
VGRWKEATIP GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT
710 720 730 740 750
STSTPVTSNT VTGETTPFSP LVATSESVTE ITASSFVVSW VSASDTVSGF
760 770 780 790 800
RVEYELSEEG DEPQYLDLPS TATSVNIPDL LPGRKYIVNV YQISEDGEQS
810 820 830 840 850
LILSTSQTTA PDAPPDTTVD QVDDTSIVVR WSRPQAPITG YRIVYSPSVE
860 870 880 890 900
GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG
910 920 930 940 950
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH
960 970 980 990 1000
GQRLPISRNT FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP
1010 1020 1030 1040 1050
TNLQFVNETD STVLVRWTPP RAQITGYRLT VGLTRRGQPR QYNVGPSVSK
1060 1070 1080 1090 1100
YPLRNLQPAS EYTVSLVAIK GNQESPKATG VFTTLQPGSS IPPYNTEVTE
1110 1120 1130 1140 1150
TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV SGLTPGVEYV
1160 1170 1180 1190 1200
YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
1210 1220 1230 1240 1250
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV
1260 1270 1280 1290 1300
KDDKESVPIS DTIIPAVPPP TDLRFTNIGP DTMRVTWAPP PSIDLTNFLV
1310 1320 1330 1340 1350
RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYVVSVSS VYEQHESTPL
1360 1370 1380 1390 1400
RGRQKTGLDS PTGIDFSDIT ANSFTVHWIA PRATITGYRI RHHPEHFSGR
1410 1420 1430 1440 1450
PREDRVPHSR NSITLTNLTP GTEYVVSIVA LNGREESPLL IGQQSTVSDV
1460 1470 1480 1490 1500
PRDLEVVAAT PTSLLISWDA PAVTVRYYRI TYGETGGNSP VQEFTVPGSK
1510 1520 1530 1540 1550
STATISGLKP GVDYTITVYA VTGRGDSPAS SKPISINYRT EIDKPSQMQV
1560 1570 1580 1590 1600
TDVQDNSISV KWLPSSSPVT GYRVTTTPKN GPGPTKTKTA GPDQTEMTIE
1610 1620 1630 1640 1650
GLQPTVEYVV SVYAQNPSGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
1660 1670 1680 1690 1700
AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGEEDTAELQ GLRPGSEYTV
1710 1720 1730 1740 1750
SVVALHDDME SQPLIGTQST AIPAPTDLKF TQVTPTSLSA QWTPPNVQLT
1760 1770 1780 1790 1800
GYRVRVTPKE KTGPMKEINL APDSSSVVVS GLMVATKYEV SVYALKDTLT
1810 1820 1830 1840 1850
SRPAQGVVTT LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAVP
1860 1870 1880 1890 1900
ANGQTPIQRT IKPDVRSYTI TGLQPGTDYK IYLYTLNDNA RSSPVVIDAS
1910 1920 1930 1940 1950
TAIDAPSNLR FLATTPNSLL VSWQPPRARI TGYIIKYEKP GSPPREVVPR
1960 1970 1980 1990 2000
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL
2010 2020 2030 2040 2050
PHPNLHGPEI LDVPSTVQKT PFVTHPGYDT GNGIQLPGTS GQQPSVGQQM
2060 2070 2080 2090 2100
IFEEHGFRRT TPPTTATPIR HRPRPYPPNV GEEIQIGHIP REDVDYHLYP
2110 2120 2130 2140 2150
HGPGLNPNAS TGQEALSQTT ISWAPFQDTS EYIISCHPVG TDEEPLQFRV
2160 2170 2180 2190 2200
PGTSTSATLT GLTRGATYNV IVEALKDQQR HKVREEVVTV GNSVNEGLNQ
2210 2220 2230 2240 2250
PTDDSCFDPY TVSHYAVGDE WERMSESGFK LLCQCLGFGS GHFRCDSSRW
2260 2270 2280 2290 2300
CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG NGKGEFKCDP HEATCYDDGK
2310 2320 2330 2340 2350
TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP SPEGTTGQSY
2360 2370 2380
NQYSQRYHQR TNTNVNCPIE CFMPLDVQAD REDSRE
Length:2,386
Mass (Da):262,625
Last modified:July 13, 2010 - v4
Checksum:i5F7EDB9700335098
GO
Isoform 2 (identifier: P02751-2) [UniParc]FASTAAdd to Basket

Also known as: MSF-FN70, Migration stimulation factor FN70

The sequence of this isoform differs from the canonical sequence as follows:
     368-388: GRTFYSCTTEGRQDGHLWCST → DRTDST
     648-657: KNSVGRWKEA → VSIPPRNLGY
     658-2386: Missing.

Show »
Length:642
Mass (Da):71,971
Checksum:iC66606885E3FA200
GO
Isoform 3 (identifier: P02751-3) [UniParc]FASTAAdd to Basket

Also known as: V89

The sequence of this isoform differs from the canonical sequence as follows:
     2081-2111: Missing.

Show »
Length:2,355
Mass (Da):259,216
Checksum:i6AAF44283F1E04C6
GO
Isoform 4 (identifier: P02751-4) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin III-15X

The sequence of this isoform differs from the canonical sequence as follows:
     1991-2110: Missing.
     2148-2151: FRVP → STKA
     2152-2386: Missing.

Show »
Length:2,031
Mass (Da):222,976
Checksum:i92B5303A584A0FB1
GO
Isoform 5 (identifier: P02751-5) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin (V+I-10)-

The sequence of this isoform differs from the canonical sequence as follows:
     1991-2110: Missing.
     2193-2247: Missing.

Show »
Length:2,211
Mass (Da):243,334
Checksum:iA2F5D57DDD663FA0
GO
Isoform 6 (identifier: P02751-6) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin (V+III-15)-

The sequence of this isoform differs from the canonical sequence as follows:
     1992-2193: Missing.

Show »
Length:2,184
Mass (Da):240,509
Checksum:i72C662DC4C18DA2B
GO
Isoform 7 (identifier: P02751-7) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin containing extra ED-B domain

The sequence of this isoform differs from the canonical sequence as follows:
     1265-1265: P → PEVPQLTDLS...SAPTTLTQQT
     2081-2111: Missing.

Show »
Length:2,446
Mass (Da):268,912
Checksum:i630CB516DE884514
GO
Isoform 8 (identifier: P02751-8) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin not containing EIIIA domain

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T

Show »
Length:2,296
Mass (Da):252,811
Checksum:i2C4DEB94AD4D5435
GO
Isoform 9 (identifier: P02751-9) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     1991-2015: Missing.
     2081-2111: Missing.

Show »
Length:2,240
Mass (Da):246,688
Checksum:i5C46F0CECC71F96F
GO
Isoform 10 (identifier: P02751-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     1991-2110: Missing.

Show »
Length:2,176
Mass (Da):239,626
Checksum:i1CABF440AE6185E2
GO
Isoform 11 (identifier: P02751-11) [UniParc]FASTAAdd to Basket

Also known as: Fibronectin containing extra type III repeat (EDII), exon x+2

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1365: AVPPPTDLRF...TGLDSPTGID → EVPQLTDLSF...TAVPPPTDLR

Show »
Length:2,386
Mass (Da):262,406
Checksum:i380E6ABFF8AA6361
GO
Isoform 12 (identifier: P02751-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1256-1487: Missing.
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     1991-2015: Missing.
     2081-2111: Missing.

Show »
Length:2,008
Mass (Da):221,292
Checksum:i697C36C79E89EB78
GO
Isoform 13 (identifier: P02751-13) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1265-1265: P → PEVPQLTDLS...SAPTTLTQQT
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     1991-2110: Missing.

Note: No experimental confirmation available.

Show »
Length:2,267
Mass (Da):249,322
Checksum:i4C45B65A37F78909
GO
Isoform 14 (identifier: P02751-14) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     2081-2111: Missing.

Show »
Length:2,265
Mass (Da):249,402
Checksum:iAC05A50EA66B26C5
GO
Isoform 15 (identifier: P02751-15) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1265-1265: P → PEVPQLTDLS...SAPTTLTQQT

Note: No experimental confirmation available.

Show »
Length:2,477
Mass (Da):272,320
Checksum:i6C436A7A5FEE6DEB
GO
Isoform 16 (identifier: P02751-16) [UniParc]FASTAAdd to Basket

Also known as: Migration stimulation factor, MSF

The sequence of this isoform differs from the canonical sequence as follows:
     648-657: KNSVGRWKEA → VSIPPRNLGY
     658-2386: Missing.

Note: Expressed by fetal and tumor-associated cells.

Show »
Length:657
Mass (Da):73,683
Checksum:iFDEBA031AD18C721
GO
Isoform 17 (identifier: P02751-17) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1992-2016: Missing.
     2082-2112: Missing.

Note: Gene prediction based on EST data.

Show »
Length:2,330
Mass (Da):256,502
Checksum:iFAACAE02C878443E
GO

Sequence cautioni

The sequence AAX76513.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAD93077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD91166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD97964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD97965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD97984.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAH18136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321Q → R in CAH18171. (PubMed:17974005)Curated
Sequence conflicti69 – 691Y → N in CAH18172. (PubMed:17974005)Curated
Sequence conflicti73 – 731A → V in CAA26536. (PubMed:2992939)Curated
Sequence conflicti126 – 1261I → V in CAH18136. (PubMed:17974005)Curated
Sequence conflicti199 – 1991E → G in CAD91166. (PubMed:17974005)Curated
Sequence conflicti247 – 2471S → R in CAD59389. (PubMed:11737888)Curated
Sequence conflicti247 – 2471S → R in CAH60958. (PubMed:16322219)Curated
Sequence conflicti260 – 2601C → R in CAH18172. (PubMed:17974005)Curated
Sequence conflicti289 – 2891V → A in CAE45847. (PubMed:17974005)Curated
Sequence conflicti355 – 3551S → L in AAD00015. 1 PublicationCurated
Sequence conflicti357 – 3571G → E in CAD97984. (PubMed:17974005)Curated
Sequence conflicti375 – 3751T → A in CAH18136. (PubMed:17974005)Curated
Sequence conflicti411 – 4111R → Q in AAD00015. 1 PublicationCurated
Sequence conflicti518 – 5181C → R in CAD97791. (PubMed:17974005)Curated
Sequence conflicti552 – 5521R → K in CAD97965. (PubMed:17974005)Curated
Sequence conflicti552 – 5521R → K in CAD97964. (PubMed:17974005)Curated
Sequence conflicti580 – 5801V → A in CAH18172. (PubMed:17974005)Curated
Sequence conflicti678 – 6781E → Q AA sequence (PubMed:3900070)Curated
Sequence conflicti704 – 7052TP → PT AA sequence (PubMed:3900070)Curated
Sequence conflicti980 – 9801V → L in CAD97791. (PubMed:17974005)Curated
Sequence conflicti1030 – 10301T → A in CAH18136. (PubMed:17974005)Curated
Sequence conflicti1048 – 10481V → D in CAD97965. (PubMed:17974005)Curated
Sequence conflicti1048 – 10481V → D in CAD97964. (PubMed:17974005)Curated
Sequence conflicti1134 – 11341D → G in CAH18136. (PubMed:17974005)Curated
Sequence conflicti1137 – 11371S → N in CAD97965. (PubMed:17974005)Curated
Sequence conflicti1137 – 11371S → N in CAD97964. (PubMed:17974005)Curated
Sequence conflicti1152 – 11521T → I in CAH18136. (PubMed:17974005)Curated
Sequence conflicti1222 – 12221E → G in CAD97791. (PubMed:17974005)Curated
Sequence conflicti1226 – 12261H → Q in CAE45932. (PubMed:17974005)Curated
Sequence conflicti1555 – 15551D → G in CAE45714. (PubMed:17974005)Curated
Sequence conflicti1601 – 16011G → S in CAD97965. (PubMed:17974005)Curated
Sequence conflicti1601 – 16011G → S in CAD97964. (PubMed:17974005)Curated
Sequence conflicti1622 – 16221Q → E AA sequence (PubMed:2012601)Curated
Sequence conflicti1715 – 17217IGTQSTA → VQTAVTT in AAA52463. (PubMed:3021206)Curated
Sequence conflicti1726 – 17261T → A in CAE45847. (PubMed:17974005)Curated
Sequence conflicti1755 – 17551R → W in CAH18136. (PubMed:17974005)Curated
Sequence conflicti1768 – 17681I → V in CAB52436. (PubMed:3375063)Curated
Sequence conflicti1783 – 17831M → T in CAE45932. (PubMed:17974005)Curated
Sequence conflicti1927 – 19271R → C in AAD00014. 1 PublicationCurated
Sequence conflicti1934 – 19341I → V in CAH18172. (PubMed:17974005)Curated
Sequence conflicti1992 – 19921D → G in CAD97965. (PubMed:17974005)Curated
Sequence conflicti1992 – 19921D → G in CAD97964. (PubMed:17974005)Curated
Sequence conflicti2023 – 20231V → A in CAD97965. (PubMed:17974005)Curated
Sequence conflicti2023 – 20231V → A in CAD97964. (PubMed:17974005)Curated
Sequence conflicti2027 – 20271G → R in CAD97965. (PubMed:17974005)Curated
Sequence conflicti2027 – 20271G → R in CAD97964. (PubMed:17974005)Curated
Sequence conflicti2251 – 22511C → R in CAH18172. (PubMed:17974005)Curated
Sequence conflicti2312 – 23121Y → N in CAD97965. (PubMed:17974005)Curated
Sequence conflicti2312 – 23121Y → N in CAD97964. (PubMed:17974005)Curated
Sequence conflicti2341 – 23411S → T in CAE45714. (PubMed:17974005)Curated
Sequence conflicti2341 – 23411S → T in CAH18171. (PubMed:17974005)Curated
Sequence conflicti2341 – 23411S → T in CAH18172. (PubMed:17974005)Curated
Sequence conflicti2341 – 23411S → T in CAE45958. (PubMed:17974005)Curated
Sequence conflicti2367 – 23671C → Y in CAE45932. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151Q → L.5 Publications
Corresponds to variant rs1250259 [ dbSNP | Ensembl ].
VAR_043917
Natural varianti817 – 8171T → P.7 Publications
Corresponds to variant rs2577301 [ dbSNP | Ensembl ].
VAR_059529
Natural varianti940 – 9401D → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036018
Natural varianti973 – 9731Y → C in GFND2. 1 Publication
VAR_043918
Natural varianti1120 – 11201R → P in a breast cancer sample; somatic mutation. 1 Publication
VAR_036019
Natural varianti1467 – 14671S → R.
Corresponds to variant rs11687611 [ dbSNP | Ensembl ].
VAR_056576
Natural varianti1834 – 18341W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 Publication
VAR_043919
Natural varianti1883 – 18831L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 Publication
VAR_043920
Natural varianti1960 – 19601I → V.1 Publication
Corresponds to variant rs1250209 [ dbSNP | Ensembl ].
VAR_043921
Natural varianti2121 – 21211I → V.
Corresponds to variant rs17449032 [ dbSNP | Ensembl ].
VAR_056577
Natural varianti2170 – 21701V → I.12 Publications
Corresponds to variant rs1250209 [ dbSNP | Ensembl ].
VAR_061486
Natural varianti2380 – 23801D → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036020

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei368 – 38821GRTFY…LWCST → DRTDST in isoform 2. 1 PublicationVSP_003255Add
BLAST
Alternative sequencei648 – 65710KNSVGRWKEA → VSIPPRNLGY in isoform 2 and isoform 16. 3 PublicationsVSP_003256
Alternative sequencei658 – 23861729Missing in isoform 2 and isoform 16. 3 PublicationsVSP_003257Add
BLAST