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Protein

Fibronectin

Gene

FN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei663Important for superfibronectin formation1
Sitei666Important for superfibronectin formation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi907 – 1172Add BLAST266

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • peptidase activator activity Source: Ensembl
  • protease binding Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • angiogenesis Source: UniProtKB-KW
  • calcium-independent cell-matrix adhesion Source: Ensembl
  • cell adhesion Source: UniProtKB
  • cell-substrate junction assembly Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • integrin activation Source: UniProtKB
  • leukocyte migration Source: Reactome
  • negative regulation of transforming growth factor-beta secretion Source: UniProtKB
  • peptide cross-linking Source: BHF-UCL
  • platelet degranulation Source: Reactome
  • positive regulation of axon extension Source: Ensembl
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of substrate-dependent cell migration, cell attachment to substrate Source: UniProtKB
  • regulation of cell shape Source: UniProtKB-KW
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of protein phosphorylation Source: UniProtKB
  • response to wounding Source: UniProtKB
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Acute phase, Angiogenesis, Cell adhesion, Cell shape

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1566977. Fibronectin matrix formation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP02751.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3778. FN1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basal lamina Source: Ensembl
  • blood microparticle Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • fibrinogen complex Source: BHF-UCL
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionGenetically 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.
See also OMIM:601894
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant rs137854488dbSNPEnsembl.1
Natural variantiVAR_0439191834W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant rs137854486dbSNPEnsembl.1
Natural variantiVAR_0439201883L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant rs137854487dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi641Y → A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683. 1 Publication1
Mutagenesisi642I → A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692. 1 Publication1
Mutagenesisi663L → 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 Publications1
Mutagenesisi666Y → 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 Publications1
Mutagenesisi681L → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683. 1 Publication1
Mutagenesisi682I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692. 1 Publication1
Mutagenesisi683S → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681. 1 Publication1
Mutagenesisi684I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692. 1 Publication1
Mutagenesisi691E → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696. 1 Publication1
Mutagenesisi692V → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684. 1 Publication1
Mutagenesisi694R → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696. 1 Publication1
Mutagenesisi695F → A: Loss of ability to form fibronectin aggregates; when associated with A-697. 1 Publication1
Mutagenesisi696D → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694. 1 Publication1
Mutagenesisi697F → A: Loss of ability to form fibronectin aggregates; when associated with A-695. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2335.
MalaCardsiFN1.
MIMi601894. phenotype.
OpenTargetsiENSG00000115414.
Orphaneti84090. Fibronectin glomerulopathy.
PharmGKBiPA28194.

Chemistry databases

ChEMBLiCHEMBL3810.
DrugBankiDB08888. Ocriplasmin.

Polymorphism and mutation databases

BioMutaiFN1.
DMDMi300669710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000001923532 – 2386FibronectinAdd BLAST2355
ChainiPRO_0000390479627 – 702AnastellinAdd BLAST76
ChainiPRO_0000300249723 – 911Ugl-Y1Add BLAST189
ChainiPRO_0000300250723 – 903Ugl-Y2Add BLAST181
ChainiPRO_0000300251723 – ?Ugl-Y3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Pyrrolidone carboxylic acid1 Publication1
Cross-linki34Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki47Isoglutamyl 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
Glycosylationi279O-linked (GalNAc...)1 Publication1
Disulfide bondi308 ↔ 335
Disulfide bondi333 ↔ 342
Disulfide bondi360 ↔ 386
Disulfide bondi374 ↔ 401
Disulfide bondi420 ↔ 446
Glycosylationi430N-linked (GlcNAc...)3 Publications1
Disulfide bondi434 ↔ 461
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...) (complex)5 Publications1
Glycosylationi542N-linked (GlcNAc...) (complex)3 Publications1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei876SulfotyrosineSequence analysis1
Glycosylationi877N-linked (GlcNAc...)2 Publications1
Modified residuei881SulfotyrosineSequence analysis1
Glycosylationi1007N-linked (GlcNAc...) (complex)4 Publications1
Glycosylationi1244N-linked (GlcNAc...)2 Publications1
Glycosylationi2064O-linked (GalNAc...)1 Publication1
Glycosylationi2065O-linked (GalNAc...)1 Publication1
Glycosylationi2108N-linked (GlcNAc...)1 Publication1
Disulfide bondi2206 ↔ 2235By similarity
Disulfide bondi2233 ↔ 2245By similarity
Disulfide bondi2251 ↔ 2278By similarity
Disulfide bondi2276 ↔ 2288By similarity
Disulfide bondi2295 ↔ 2319By similarity
Disulfide bondi2317 ↔ 2333By similarity
Modified residuei2363PhosphothreonineCombined sources1
Disulfide bondi2367Interchain (with C-2371)
Disulfide bondi2371Interchain (with C-2367)
Modified residuei2384Phosphoserine; by FAM20CCombined sources1 Publication1

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).
Phosphorylated by FAM20C in the extracellular medium.1 Publication
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2108Not glycosylated1

Keywords - PTMi

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

Proteomic databases

EPDiP02751.
MaxQBiP02751.
PeptideAtlasiP02751.
PRIDEiP02751.

2D gel databases

DOSAC-COBS-2DPAGEP02751.

PTM databases

iPTMnetiP02751.
PhosphoSitePlusiP02751.
SwissPalmiP02751.
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

BgeeiENSG00000115414.
ExpressionAtlasiP02751. baseline and differential.
GenevisibleiP02751. HS.

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 (PubMed:12225811). Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC.By similarity9 Publications
(Microbial infection) Interacts with S.aureus fnbA (PubMed:12736686). Interacts with M.bovis fbpB via the collagen-binding region; also interacts with fibronectin-binding proteins from other Mycobacteria (PubMed:8406884).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1220319,EBI-1220319
Q99IB83EBI-1220319,EBI-6927928From a different organism.
CTGFP292795EBI-1220319,EBI-2835375
DCNP075859EBI-1220319,EBI-9663608
FBN1P355552EBI-1220319,EBI-2505934
FBN2P355562EBI-1220319,EBI-6164392
fnbAP1473818EBI-1220319,EBI-8398157From a different organism.
fnbBQ5368219EBI-1220319,EBI-8398005From a different organism.
fneQ93ED68EBI-1220319,EBI-9826140From a different organism.
FYNP062412EBI-7133890,EBI-515315
LPAP085192EBI-1220319,EBI-9232288
PM1665Q9CKF65EBI-1220319,EBI-11164515From a different organism.
SCGB1A1P116843EBI-1220319,EBI-7797649
TGM2P219803EBI-1220319,EBI-727668
THBS1P079962EBI-1220319,EBI-2530274
TNFAIP6P980668EBI-1220319,EBI-11700693
UBQLN1Q9UMX03EBI-1220319,EBI-741480
VHLP403372EBI-1220319,EBI-301246

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • protease binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108621. 736 interactors.
DIPiDIP-29547N.
IntActiP02751. 473 interactors.
MINTiMINT-1779779.

Chemistry databases

BindingDBiP02751.

Structurei

Secondary structure

12386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi52 – 54Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 78Combined sources7
Turni81 – 83Combined sources3
Beta strandi85 – 89Combined sources5
Beta strandi96 – 98Combined sources3
Turni100 – 102Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi111 – 116Combined sources6
Beta strandi119 – 127Combined sources9
Turni128 – 131Combined sources4
Beta strandi132 – 136Combined sources5
Beta strandi140 – 143Combined sources4
Beta strandi146 – 149Combined sources4
Beta strandi153 – 157Combined sources5
Beta strandi161 – 171Combined sources11
Turni172 – 175Combined sources4
Beta strandi176 – 181Combined sources6
Beta strandi185 – 188Combined sources4
Turni189 – 192Combined sources4
Beta strandi193 – 196Combined sources4
Beta strandi200 – 205Combined sources6
Turni206 – 208Combined sources3
Beta strandi209 – 217Combined sources9
Turni218 – 221Combined sources4
Beta strandi222 – 226Combined sources5
Beta strandi230 – 233Combined sources4
Turni234 – 237Combined sources4
Beta strandi238 – 241Combined sources4
Beta strandi245 – 249Combined sources5
Beta strandi251 – 253Combined sources3
Beta strandi255 – 262Combined sources8
Turni263 – 266Combined sources4
Beta strandi267 – 271Combined sources5
Beta strandi302 – 304Combined sources3
Beta strandi307 – 309Combined sources3
Turni311 – 313Combined sources3
Beta strandi315 – 317Combined sources3
Beta strandi321 – 326Combined sources6
Beta strandi329 – 336Combined sources8
Beta strandi339 – 344Combined sources6
Turni353 – 356Combined sources4
Beta strandi360 – 366Combined sources7
Beta strandi369 – 373Combined sources5
Beta strandi381 – 383Combined sources3
Beta strandi385 – 391Combined sources7
Helixi392 – 395Combined sources4
Beta strandi398 – 401Combined sources4
Helixi403 – 405Combined sources3
Turni413 – 417Combined sources5
Beta strandi422 – 426Combined sources5
Beta strandi429 – 433Combined sources5
Beta strandi440 – 442Combined sources3
Beta strandi445 – 451Combined sources7
Helixi452 – 455Combined sources4
Beta strandi458 – 460Combined sources3
Helixi465 – 467Combined sources3
Beta strandi469 – 471Combined sources3
Beta strandi477 – 479Combined sources3
Beta strandi483 – 485Combined sources3
Beta strandi490 – 492Combined sources3
Beta strandi495 – 500Combined sources6
Turni501 – 504Combined sources4
Beta strandi505 – 513Combined sources9
Beta strandi517 – 520Combined sources4
Beta strandi523 – 526Combined sources4
Beta strandi529 – 534Combined sources6
Beta strandi540 – 547Combined sources8
Turni548 – 551Combined sources4
Beta strandi552 – 557Combined sources6
Beta strandi559 – 562Combined sources4
Turni564 – 566Combined sources3
Beta strandi569 – 571Combined sources3
Beta strandi575 – 578Combined sources4
Beta strandi585 – 591Combined sources7
Turni592 – 595Combined sources4
Beta strandi596 – 601Combined sources6
Beta strandi613 – 615Combined sources3
Beta strandi626 – 631Combined sources6
Beta strandi634 – 636Combined sources3
Beta strandi638 – 647Combined sources10
Turni648 – 651Combined sources4
Beta strandi655 – 659Combined sources5
Beta strandi661 – 664Combined sources4
Beta strandi665 – 668Combined sources4
Beta strandi673 – 688Combined sources16
Beta strandi690 – 699Combined sources10
Helixi732 – 734Combined sources3
Beta strandi736 – 739Combined sources4
Beta strandi747 – 756Combined sources10
Turni757 – 759Combined sources3
Beta strandi764 – 769Combined sources6
Beta strandi774 – 777Combined sources4
Beta strandi785 – 794Combined sources10
Beta strandi799 – 808Combined sources10
Beta strandi818 – 822Combined sources5
Beta strandi824 – 830Combined sources7
Beta strandi839 – 847Combined sources9
Beta strandi854 – 859Combined sources6
Beta strandi864 – 869Combined sources6
Beta strandi875 – 883Combined sources9
Beta strandi892 – 897Combined sources6
Beta strandi1178 – 1184Combined sources7
Beta strandi1186 – 1189Combined sources4
Beta strandi1191 – 1196Combined sources6
Beta strandi1205 – 1212Combined sources8
Turni1213 – 1215Combined sources3
Beta strandi1221 – 1225Combined sources5
Beta strandi1231 – 1233Combined sources3
Beta strandi1243 – 1251Combined sources9
Beta strandi1259 – 1263Combined sources5
Beta strandi1271 – 1277Combined sources7
Beta strandi1283 – 1288Combined sources6
Beta strandi1296 – 1304Combined sources9
Helixi1305 – 1307Combined sources3
Helixi1308 – 1310Combined sources3
Beta strandi1312 – 1316Combined sources5
Beta strandi1322 – 1325Combined sources4
Beta strandi1333 – 1342Combined sources10
Beta strandi1350 – 1355Combined sources6
Beta strandi1362 – 1368Combined sources7
Beta strandi1374 – 1379Combined sources6
Beta strandi1386 – 1394Combined sources9
Beta strandi1402 – 1406Combined sources5
Beta strandi1412 – 1415Combined sources4
Beta strandi1423 – 1432Combined sources10
Beta strandi1440 – 1445Combined sources6
Beta strandi1452 – 1460Combined sources9
Beta strandi1463 – 1469Combined sources7
Beta strandi1476 – 1484Combined sources9
Beta strandi1487 – 1489Combined sources3
Beta strandi1492 – 1497Combined sources6
Beta strandi1502 – 1505Combined sources4
Beta strandi1513 – 1522Combined sources10
Beta strandi1525 – 1527Combined sources3
Beta strandi1534 – 1539Combined sources6
Beta strandi1548 – 1553Combined sources6
Beta strandi1558 – 1562Combined sources5
Beta strandi1570 – 1581Combined sources12
Beta strandi1586 – 1590Combined sources5
Beta strandi1596 – 1599Combined sources4
Beta strandi1607 – 1615Combined sources9
Beta strandi1621 – 1630Combined sources10
Beta strandi1639 – 1644Combined sources6
Beta strandi1647 – 1651Combined sources5
Beta strandi1662 – 1668Combined sources7
Turni1669 – 1671Combined sources3
Beta strandi1672 – 1676Combined sources5
Beta strandi1686 – 1689Combined sources4
Beta strandi1696 – 1704Combined sources9
Beta strandi1706 – 1708Combined sources3
Beta strandi1714 – 1719Combined sources6
Beta strandi1726 – 1733Combined sources8
Beta strandi1738 – 1743Combined sources6
Beta strandi1751 – 1763Combined sources13
Beta strandi1766 – 1770Combined sources5
Beta strandi1776 – 1779Combined sources4
Beta strandi1787 – 1796Combined sources10
Beta strandi1804 – 1809Combined sources6
Beta strandi1818 – 1825Combined sources8
Beta strandi1830 – 1835Combined sources6
Beta strandi1843 – 1853Combined sources11
Beta strandi1857 – 1861Combined sources5
Beta strandi1866 – 1870Combined sources5
Beta strandi1878 – 1887Combined sources10
Beta strandi1895 – 1900Combined sources6
Beta strandi1907 – 1915Combined sources9
Beta strandi1918 – 1924Combined sources7
Beta strandi1932 – 1938Combined sources7
Beta strandi1957 – 1960Combined sources4
Beta strandi1968 – 1977Combined sources10
Beta strandi1985 – 1990Combined sources6
Beta strandi2253 – 2255Combined sources3
Beta strandi2263 – 2267Combined sources5
Beta strandi2269 – 2280Combined sources12
Turni2281 – 2284Combined sources4
Beta strandi2285 – 2290Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N1KNMR-A808-905[»]
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[»]
5DC0X-ray2.23A1447-1540[»]
5DC4X-ray1.48B1445-1540[»]
5DC9X-ray1.56B1445-1540[»]
5DFTX-ray2.50A/B/C/D/E/F/G/H/I/J1539-1635[»]
5J7CX-ray2.54C/D1447-1540[»]
ProteinModelPortaliP02751.
SMRiP02751.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02751.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 90Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST41
Domaini95 – 138Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST44
Domaini139 – 182Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST44
Domaini184 – 228Fibronectin type-I 4PROSITE-ProRule annotationAdd BLAST45
Domaini229 – 273Fibronectin type-I 5PROSITE-ProRule annotationAdd BLAST45
Domaini306 – 345Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST40
Domaini355 – 403Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini415 – 463Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini468 – 511Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST44
Domaini516 – 558Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST43
Domaini559 – 602Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST44
Domaini610 – 702Fibronectin type-III 1Add BLAST93
Domaini722 – 812Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST91
Domaini813 – 904Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini909 – 998Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST90
Domaini999 – 1088Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST90
Domaini1089 – 1175Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST87
Domaini1176 – 1266Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST91
Domaini1269 – 1361Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST93
Domaini1362 – 1449Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST88
Domaini1450 – 1543Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST94
Domaini1544 – 1635Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST92
Domaini1636 – 1723Fibronectin type-III 12; extra domainPROSITE-ProRule annotationAdd BLAST88
Domaini1724 – 1817Fibronectin type-III 13PROSITE-ProRule annotationAdd BLAST94
Domaini1818 – 1904Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST87
Domaini1905 – 1995Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST91
Domaini2103 – 2197Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST95
Domaini2204 – 2248Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST45
Domaini2249 – 2291Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST43
Domaini2293 – 2336Fibronectin type-I 12PROSITE-ProRule annotationAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 272Fibrin- and heparin-binding 1Add BLAST221
Regioni308 – 608Collagen-bindingAdd BLAST301
Regioni464 – 477Critical for collagen bindingAdd BLAST14
Regioni1267 – 1540Cell-attachmentAdd BLAST274
Regioni1721 – 1991Heparin-binding 2Add BLAST271
Regioni1813 – 1991Binds to FBLN1Add BLAST179
Regioni1992 – 2102Connecting strand 3 (CS-3) (V region)Add BLAST111
Regioni2206 – 2337Fibrin-binding 2Add BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1524 – 1526Cell attachment site3

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

GeneTreeiENSGT00830000128240.
HOGENOMiHOG000234344.
HOVERGENiHBG005731.
InParanoidiP02751.
KOiK05717.
OMAiVTLPHPN.
OrthoDBiEOG091G116D.
PhylomeDBiP02751.
TreeFamiTF329915.

Family and domain databases

CDDicd00062. FN2. 2 hits.
cd00063. FN3. 16 hits.
Gene3Di2.10.10.10. 2 hits.
2.60.40.10. 16 hits.
InterProiIPR000083. Fibronectin_type1.
IPR003961. FN3_dom.
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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32Q → R in CAH18171 (PubMed:17974005).Curated1
Sequence conflicti69Y → N in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti73A → V in CAA26536 (PubMed:2992939).Curated1
Sequence conflicti126I → V in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti199E → G in CAD91166 (PubMed:17974005).Curated1
Sequence conflicti247S → R in CAD59389 (PubMed:11737888).Curated1
Sequence conflicti247S → R in CAH60958 (PubMed:16322219).Curated1
Sequence conflicti260C → R in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti289V → A in CAE45847 (PubMed:17974005).Curated1
Sequence conflicti355S → L in AAD00015 (Ref. 13) Curated1
Sequence conflicti357G → E in CAD97984 (PubMed:17974005).Curated1
Sequence conflicti375T → A in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti411R → Q in AAD00015 (Ref. 13) Curated1
Sequence conflicti518C → R in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti552R → K in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti552R → K in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti580V → A in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti678E → Q AA sequence (PubMed:3900070).Curated1
Sequence conflicti704 – 705TP → PT AA sequence (PubMed:3900070).Curated2
Sequence conflicti980V → L in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti1030T → A in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1048V → D in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1048V → D in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1134D → G in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1137S → N in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1137S → N in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1152T → I in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1222E → G in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti1226H → Q in CAE45932 (PubMed:17974005).Curated1
Sequence conflicti1555D → G in CAE45714 (PubMed:17974005).Curated1
Sequence conflicti1601G → S in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1601G → S in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1622Q → E AA sequence (PubMed:2012601).Curated1
Sequence conflicti1715 – 1721IGTQSTA → VQTAVTT in AAA52463 (PubMed:3021206).Curated7
Sequence conflicti1726T → A in CAE45847 (PubMed:17974005).Curated1
Sequence conflicti1755R → W in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1768I → V in CAB52436 (PubMed:3375063).Curated1
Sequence conflicti1783M → T in CAE45932 (PubMed:17974005).Curated1
Sequence conflicti1927R → C in AAD00014 (Ref. 13) Curated1
Sequence conflicti1934I → V in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti1992D → G in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1992D → G in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2023V → A in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2023V → A in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2027G → R in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2027G → R in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2251C → R in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti2312Y → N in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2312Y → N in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2341S → T in CAE45714 (PubMed:17974005).Curated1
Sequence conflicti2341S → T in CAH18171 (PubMed:17974005).Curated1
Sequence conflicti2341S → T in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti2341S → T in CAE45958 (PubMed:17974005).Curated1
Sequence conflicti2367C → Y in CAE45932 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04391715Q → L.5 PublicationsCorresponds to variant rs1250259dbSNPEnsembl.1
Natural variantiVAR_059529817T → P.7 PublicationsCorresponds to variant rs2577301dbSNPEnsembl.1
Natural variantiVAR_036018940D → N in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs752106647dbSNPEnsembl.1
Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant rs137854488dbSNPEnsembl.1
Natural variantiVAR_0360191120R → P in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0565761467S → R.Corresponds to variant rs11687611dbSNPEnsembl.1
Natural variantiVAR_0439191834W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant rs137854486dbSNPEnsembl.1
Natural variantiVAR_0439201883L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant rs137854487dbSNPEnsembl.1
Natural variantiVAR_0439211960I → V.1 PublicationCorresponds to variant rs1250209dbSNPEnsembl.1
Natural variantiVAR_0565772121I → V.Corresponds to variant rs17449032dbSNPEnsembl.1
Natural variantiVAR_0614862170V → I.Combined sources11 Publications