SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02751

- FINC_HUMAN

UniProt

P02751 - FINC_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Fibronectin
Gene
FN1, FN
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.4 Publications
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.4 Publications

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 – 1172266
Add
BLAST

GO - Molecular functioni

  1. collagen binding Source: UniProtKB
  2. heparin binding Source: UniProtKB
  3. integrin binding Source: UniProt
  4. peptidase activator activity Source: Ensembl
  5. protease binding Source: BHF-UCL
  6. protein binding Source: IntAct
Complete GO annotation...

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. extracellular matrix disassembly Source: Reactome
  8. extracellular matrix organization Source: Reactome
  9. leukocyte migration Source: Reactome
  10. peptide cross-linking Source: BHF-UCL
  11. platelet activation Source: Reactome
  12. platelet degranulation Source: Reactome
  13. regulation of cell shape Source: UniProtKB-KW
  14. response to wounding Source: UniProtKB
  15. substrate adhesion-dependent cell spreading Source: BHF-UCL
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. basement membrane Source: Ensembl
  3. blood microparticle Source: UniProt
  4. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  5. extracellular matrix Source: BHF-UCL
  6. extracellular region Source: InterPro
  7. extracellular space Source: BHF-UCL
  8. extracellular vesicular exosome Source: UniProt
  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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 Publication
Add
BLAST
Chaini32 – 23862355Fibronectin
PRO_0000019235Add
BLAST
Chaini627 – 70276Anastellin
PRO_0000390479Add
BLAST
Chaini723 – 911189Ugl-Y1
PRO_0000300249Add
BLAST
Chaini723 – 903181Ugl-Y2
PRO_0000300250Add
BLAST
Chaini723 – ?Ugl-Y3PRO_0000300251

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Pyrrolidone carboxylic acid
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 ↔ 782 Publications
Disulfide bondi76 ↔ 872 Publications
Disulfide bondi97 ↔ 1252 Publications
Disulfide bondi123 ↔ 1352 Publications
Disulfide bondi141 ↔ 1692 Publications
Disulfide bondi167 ↔ 1792 Publications
Disulfide bondi186 ↔ 2152 Publications
Disulfide bondi213 ↔ 2252 Publications
Disulfide bondi231 ↔ 2602 Publications
Disulfide bondi258 ↔ 2702 Publications
Glycosylationi279 – 2791O-linked (GalNAc...)1 Publication
Disulfide bondi308 ↔ 3352 Publications
Disulfide bondi333 ↔ 3422 Publications
Disulfide bondi360 ↔ 3862 Publications
Disulfide bondi374 ↔ 4012 Publications
Disulfide bondi420 ↔ 4462 Publications
Glycosylationi430 – 4301N-linked (GlcNAc...)3 Publications
Disulfide bondi434 ↔ 4612 Publications
Disulfide bondi470 ↔ 498 By similarity
Disulfide bondi496 ↔ 508 By similarity
Disulfide bondi518 ↔ 545 By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...) (complex)5 Publications
Glycosylationi542 – 5421N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi543 ↔ 555 By similarity
Disulfide bondi561 ↔ 589 By similarity
Disulfide bondi587 ↔ 599 By similarity
Modified residuei876 – 8761Sulfotyrosine Reviewed prediction
Glycosylationi877 – 8771N-linked (GlcNAc...)2 Publications
Modified residuei881 – 8811Sulfotyrosine Reviewed prediction
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...)2 Publications
Disulfide bondi2206 ↔ 2235 By similarity
Disulfide bondi2233 ↔ 2245 By similarity
Disulfide bondi2251 ↔ 2278 By similarity
Disulfide bondi2276 ↔ 2288 By similarity
Disulfide bondi2295 ↔ 2319 By similarity
Disulfide bondi2317 ↔ 2333 By similarity
Disulfide bondi2367 – 2367Interchain (with C-2371)2 Publications
Disulfide bondi2371 – 2371Interchain (with C-2367)2 Publications
Modified residuei2384 – 23841Phosphoserine2 Publications

Post-translational modificationi

Sulfated.
It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated.6 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.
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-2DPAGEiP02751.

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

ArrayExpressiP02751.
BgeeiP02751.
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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-1220319,EBI-6927928From a different organism.
CTGFP292795EBI-1220319,EBI-2835375
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. 718 interactions.
DIPiDIP-29547N.
IntActiP02751. 445 interactions.
MINTiMINT-1779779.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi52 – 543
Beta strandi57 – 593
Beta strandi64 – 696
Beta strandi72 – 787
Turni81 – 833
Beta strandi85 – 895
Beta strandi96 – 983
Turni100 – 1023
Beta strandi105 – 1073
Beta strandi111 – 1166
Beta strandi119 – 1279
Turni128 – 1314
Beta strandi132 – 1365
Beta strandi140 – 1434
Beta strandi146 – 1494
Beta strandi153 – 1575
Beta strandi161 – 17111
Turni172 – 1754
Beta strandi176 – 1816
Beta strandi185 – 1884
Turni189 – 1924
Beta strandi193 – 1964
Beta strandi200 – 2056
Turni206 – 2083
Beta strandi209 – 2179
Turni218 – 2214
Beta strandi222 – 2265
Beta strandi230 – 2334
Turni234 – 2374
Beta strandi238 – 2414
Beta strandi245 – 2495
Beta strandi251 – 2533
Beta strandi255 – 2628
Turni263 – 2664
Beta strandi267 – 2715
Beta strandi302 – 3043
Beta strandi307 – 3093
Turni311 – 3133
Beta strandi315 – 3173
Beta strandi321 – 3266
Beta strandi329 – 3368
Beta strandi339 – 3446
Turni353 – 3564
Beta strandi360 – 3667
Beta strandi369 – 3735
Beta strandi381 – 3833
Beta strandi385 – 3917
Helixi392 – 3954
Beta strandi398 – 4014
Helixi403 – 4053
Turni413 – 4175
Beta strandi422 – 4265
Beta strandi429 – 4335
Beta strandi440 – 4423
Beta strandi445 – 4517
Helixi452 – 4554
Beta strandi458 – 4603
Helixi465 – 4673
Beta strandi469 – 4713
Beta strandi477 – 4793
Beta strandi483 – 4853
Beta strandi490 – 4923
Beta strandi495 – 5006
Turni501 – 5044
Beta strandi505 – 5139
Beta strandi517 – 5204
Beta strandi523 – 5264
Beta strandi529 – 5346
Beta strandi540 – 5478
Turni548 – 5514
Beta strandi552 – 5576
Beta strandi559 – 5624
Turni564 – 5663
Beta strandi569 – 5713
Beta strandi575 – 5784
Beta strandi585 – 5917
Turni592 – 5954
Beta strandi596 – 6016
Beta strandi613 – 6153
Beta strandi626 – 6316
Beta strandi634 – 6363
Beta strandi638 – 64710
Turni648 – 6514
Beta strandi655 – 6595
Beta strandi661 – 6644
Beta strandi665 – 6684
Beta strandi673 – 68816
Beta strandi690 – 69910
Helixi732 – 7343
Beta strandi736 – 7394
Beta strandi747 – 75610
Turni757 – 7593
Beta strandi764 – 7696
Beta strandi774 – 7774
Beta strandi785 – 79410
Beta strandi799 – 80810
Beta strandi1178 – 11847
Beta strandi1186 – 11894
Beta strandi1191 – 11966
Beta strandi1205 – 12128
Turni1213 – 12153
Beta strandi1221 – 12255
Beta strandi1231 – 12333
Beta strandi1243 – 12519
Beta strandi1259 – 12635
Beta strandi1271 – 12777
Beta strandi1283 – 12886
Beta strandi1296 – 13049
Helixi1308 – 13103
Beta strandi1312 – 13165
Beta strandi1322 – 13254
Beta strandi1333 – 134210
Beta strandi1350 – 13556
Beta strandi1362 – 13687
Beta strandi1371 – 13799
Beta strandi1386 – 13938
Beta strandi1402 – 14076
Beta strandi1412 – 14176
Beta strandi1423 – 143210
Beta strandi1440 – 14456
Beta strandi1455 – 14595
Beta strandi1461 – 14633
Beta strandi1464 – 14674
Beta strandi1476 – 14849
Turni1485 – 14906
Beta strandi1492 – 14976
Beta strandi1502 – 15054
Beta strandi1513 – 15219
Beta strandi1525 – 15273
Beta strandi1534 – 15396
Beta strandi1639 – 16446
Beta strandi1647 – 16515
Beta strandi1662 – 16687
Turni1669 – 16713
Beta strandi1672 – 16765
Beta strandi1686 – 16894
Beta strandi1696 – 17049
Beta strandi1706 – 17083
Beta strandi1714 – 17196
Beta strandi1726 – 17338
Beta strandi1738 – 17436
Beta strandi1751 – 176313
Beta strandi1766 – 17705
Beta strandi1776 – 17794
Beta strandi1787 – 179610
Beta strandi1804 – 18096
Beta strandi1818 – 18258
Beta strandi1830 – 18356
Beta strandi1843 – 185311
Beta strandi1857 – 18615
Beta strandi1866 – 18705
Beta strandi1878 – 188710
Beta strandi1895 – 19006
Beta strandi1907 – 19159
Beta strandi1918 – 19247
Beta strandi1932 – 19387
Beta strandi1957 – 19604
Beta strandi1968 – 197710
Beta strandi1985 – 19906
Beta strandi2253 – 22553
Beta strandi2263 – 22675
Beta strandi2269 – 228012
Turni2281 – 22844
Beta strandi2285 – 22906

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
4MMXX-ray3.32C1448-1540[»]
4MMYX-ray3.18C1448-1540[»]
4MMZX-ray3.10C1448-1540[»]
ProteinModelPortaliP02751.
SMRiP02751. Positions 48-274, 297-606, 609-809, 1173-1540, 1631-1991, 2242-2299.

Miscellaneous databases

EvolutionaryTraceiP02751.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 272221Fibrin- and heparin-binding 1
Add
BLAST
Regioni308 – 608301Collagen-binding
Add
BLAST
Regioni464 – 47714Critical for collagen binding
Add
BLAST
Regioni1267 – 1540274Cell-attachment
Add
BLAST
Regioni1721 – 1991271Heparin-binding 2
Add
BLAST
Regioni1813 – 1991179Binds to FBLN1
Add
BLAST
Regioni1992 – 2102111Connecting strand 3 (CS-3) (V region)
Add
BLAST
Regioni2206 – 2337132Fibrin-binding 2
Add
BLAST

Motif

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG005731.
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

MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP     50
GCYDNGKHYQ INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK 100
YTGNTYRVGD TYERPKDSMI WDCTCIGAGR GRISCTIANR CHEGGQSYKI 150
GDTWRRPHET GGYMLECVCL GNGKGEWTCK PIAEKCFDHA AGTSYVVGET 200
WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY RIGDTWSKKD 250
NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP 300
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT 350
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF 400
CTDHTVLVQT RGGNSNGALC HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ 450
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDM GHMMRCTCVG 500
NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR 550
GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ 600
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS 650
VGRWKEATIP GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT 700
STSTPVTSNT VTGETTPFSP LVATSESVTE ITASSFVVSW VSASDTVSGF 750
RVEYELSEEG DEPQYLDLPS TATSVNIPDL LPGRKYIVNV YQISEDGEQS 800
LILSTSQTTA PDAPPDTTVD QVDDTSIVVR WSRPQAPITG YRIVYSPSVE 850
GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG 900
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH 950
GQRLPISRNT FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP 1000
TNLQFVNETD STVLVRWTPP RAQITGYRLT VGLTRRGQPR QYNVGPSVSK 1050
YPLRNLQPAS EYTVSLVAIK GNQESPKATG VFTTLQPGSS IPPYNTEVTE 1100
TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV SGLTPGVEYV 1150
YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT 1200
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV 1250
KDDKESVPIS DTIIPAVPPP TDLRFTNIGP DTMRVTWAPP PSIDLTNFLV 1300
RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYVVSVSS VYEQHESTPL 1350
RGRQKTGLDS PTGIDFSDIT ANSFTVHWIA PRATITGYRI RHHPEHFSGR 1400
PREDRVPHSR NSITLTNLTP GTEYVVSIVA LNGREESPLL IGQQSTVSDV 1450
PRDLEVVAAT PTSLLISWDA PAVTVRYYRI TYGETGGNSP VQEFTVPGSK 1500
STATISGLKP GVDYTITVYA VTGRGDSPAS SKPISINYRT EIDKPSQMQV 1550
TDVQDNSISV KWLPSSSPVT GYRVTTTPKN GPGPTKTKTA GPDQTEMTIE 1600
GLQPTVEYVV SVYAQNPSGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI 1650
AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGEEDTAELQ GLRPGSEYTV 1700
SVVALHDDME SQPLIGTQST AIPAPTDLKF TQVTPTSLSA QWTPPNVQLT 1750
GYRVRVTPKE KTGPMKEINL APDSSSVVVS GLMVATKYEV SVYALKDTLT 1800
SRPAQGVVTT LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAVP 1850
ANGQTPIQRT IKPDVRSYTI TGLQPGTDYK IYLYTLNDNA RSSPVVIDAS 1900
TAIDAPSNLR FLATTPNSLL VSWQPPRARI TGYIIKYEKP GSPPREVVPR 1950
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL 2000
PHPNLHGPEI LDVPSTVQKT PFVTHPGYDT GNGIQLPGTS GQQPSVGQQM 2050
IFEEHGFRRT TPPTTATPIR HRPRPYPPNV GEEIQIGHIP REDVDYHLYP 2100
HGPGLNPNAS TGQEALSQTT ISWAPFQDTS EYIISCHPVG TDEEPLQFRV 2150
PGTSTSATLT GLTRGATYNV IVEALKDQQR HKVREEVVTV GNSVNEGLNQ 2200
PTDDSCFDPY TVSHYAVGDE WERMSESGFK LLCQCLGFGS GHFRCDSSRW 2250
CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG NGKGEFKCDP HEATCYDDGK 2300
TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP SPEGTTGQSY 2350
NQYSQRYHQR TNTNVNCPIE CFMPLDVQAD REDSRE 2386
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 BAD93077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAD91166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAD97964.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAD97965.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAD97984.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAH18136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAX76513.1 differs from that shown. Reason: Erroneous gene model prediction.

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.
VSP_003255Add
BLAST
Alternative sequencei648 – 65710KNSVGRWKEA → VSIPPRNLGY in isoform 2 and isoform 16.
VSP_003256
Alternative sequencei658 – 23861729Missing in isoform 2 and isoform 16.
VSP_003257Add
BLAST
Alternative sequencei1256 – 1487232Missing in isoform 12.
VSP_013681Add
BLAST
Alternative sequencei1265 – 12651P → PEVPQLTDLSFVDITDSSIG LRWTPLNSSTIIGYRITVVA AGEGIPIFEDFVDSSVGYYT VTGLEPGIDYDISVITLING GESAPTTLTQQT in isoform 7, isoform 13 and isoform 15.
VSP_008104
Alternative sequencei1266 – 1365100AVPPP…PTGID → EVPQLTDLSFVDITDSSIGL RWTPLNSSTIIGYRITVVAA GEGIPIFEDFVDSSVGYYTV TGLEPGIDYDISVITLINGG ESAPTTLTQQTAVPPPTDLR in isoform 11.
VSP_008105Add
BLAST
Alternative sequencei1631 – 172191NIDRP…TQSTA → T in isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14.
VSP_008106Add
BLAST
Alternative sequencei1991 – 2110120Missing in isoform 4, isoform 5, isoform 10 and isoform 13.
VSP_008107Add
BLAST
Alternative sequencei1991 – 201525Missing in isoform 9 and isoform 12.
VSP_008108Add
BLAST
Alternative sequencei1992 – 2193202Missing in isoform 6.
VSP_008109Add
BLAST
Alternative sequencei1992 – 201625Missing in isoform 17.
VSP_047310Add
BLAST
Alternative sequencei2081 – 211131Missing in isoform 3, isoform 7, isoform 9, isoform 12 and isoform 14.
VSP_008110Add
BLAST
Alternative sequencei2082 – 211231Missing in isoform 17.
VSP_047311Add
BLAST
Alternative sequencei2148 – 21514FRVP → STKA in isoform 4.
VSP_008111
Alternative sequencei2152 – 2386235Missing in isoform 4.
VSP_008112Add
BLAST
Alternative sequencei2193 – 224755Missing in isoform 5.
VSP_008113Add
BLAST

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ276395 mRNA. Translation: CAC20427.1.
AJ535086 mRNA. Translation: CAD59389.1.
AJ849445 mRNA. Translation: CAH60958.1.
AB191261 mRNA. Translation: BAD52437.1.
AB209840 mRNA. Translation: BAD93077.1. Different initiation.
AL832202 mRNA. Translation: CAD91166.1. Different initiation.
BX537590 mRNA. Translation: CAD97791.1.
BX538017 mRNA. Translation: CAD97964.1. Different initiation.
BX538018 mRNA. Translation: CAD97965.1. Different initiation.
BX538045 mRNA. Translation: CAD97984.1. Different initiation.
BX640608 mRNA. Translation: CAE45714.1.
BX640731 mRNA. Translation: CAE45847.1.
BX640875 mRNA. Translation: CAE45932.1.
BX640920 mRNA. Translation: CAE45958.1.
CR749281 mRNA. Translation: CAH18136.1. Different initiation.
CR749316 mRNA. Translation: CAH18171.1.
CR749317 mRNA. Translation: CAH18172.1.
AC012462 Genomic DNA. Translation: AAX76513.1. Sequence problems.
AC073284 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70536.1.
BC117176 mRNA. Translation: AAI17177.1.
BC143763 mRNA. Translation: AAI43764.1.
M15801 Genomic DNA. Translation: AAA53376.1.
AF312399 mRNA. Translation: AAG30571.1.
X02761 mRNA. Translation: CAA26536.1.
U41850 mRNA. Translation: AAD00014.1.
U42404 mRNA. Translation: AAD00015.1.
U42592 mRNA. Translation: AAD00017.1.
U42593 mRNA. Translation: AAD00018.1.
U42594 mRNA. Translation: AAD00019.1.
U42455 mRNA. Translation: AAD09448.1.
U42456 mRNA. Translation: AAD09449.1.
U42458 mRNA. Translation: AAD09450.1.
U42457 mRNA. Translation: AAD04751.1.
X07718 Genomic DNA. Translation: CAB52436.1. Different termination.
X07717 Genomic DNA. Translation: CAB52437.1.
M18179, M18177, M18178 Genomic DNA. Translation: AAA52461.1.
M12549 Genomic DNA. Translation: AAA58483.1.
M10905 mRNA. Translation: AAA52462.1.
M14059 mRNA. Translation: AAA52463.1.
AJ320525 mRNA. Translation: CAC86914.1.
AJ320526 mRNA. Translation: CAC86915.1.
AJ320527 mRNA. Translation: CAC86916.1.
M27589 mRNA. Translation: AAA52465.1.
X04530 Genomic DNA. No translation available.
CCDSiCCDS2399.1. [P02751-3]
CCDS2400.1. [P02751-10]
CCDS42813.1. [P02751-8]
CCDS42814.1. [P02751-15]
CCDS46510.1. [P02751-17]
PIRiA26460. FNHU.
I52394.
S00848.
RefSeqiNP_002017.1. NM_002026.2.
NP_473375.2. NM_054034.2.
NP_997639.1. NM_212474.1.
NP_997641.1. NM_212476.1.
NP_997643.1. NM_212478.1.
NP_997647.1. NM_212482.1.
XP_005246457.1. XM_005246400.1. [P02751-7]
XP_005246463.1. XM_005246406.1. [P02751-1]
XP_005246470.1. XM_005246413.1. [P02751-13]
XP_005246472.1. XM_005246415.1. [P02751-14]
XP_005246474.1. XM_005246417.1. [P02751-9]
UniGeneiHs.203717.

Genome annotation databases

EnsembliENST00000323926; ENSP00000323534; ENSG00000115414. [P02751-7]
ENST00000336916; ENSP00000338200; ENSG00000115414. [P02751-3]
ENST00000345488; ENSP00000273049; ENSG00000115414. [P02751-6]
ENST00000354785; ENSP00000346839; ENSG00000115414. [P02751-15]
ENST00000356005; ENSP00000348285; ENSG00000115414. [P02751-8]
ENST00000357009; ENSP00000349509; ENSG00000115414. [P02751-4]
ENST00000357867; ENSP00000350534; ENSG00000115414. [P02751-10]
ENST00000359671; ENSP00000352696; ENSG00000115414. [P02751-1]
ENST00000421182; ENSP00000394423; ENSG00000115414. [P02751-9]
ENST00000432072; ENSP00000399538; ENSG00000115414. [P02751-13]
ENST00000443816; ENSP00000415018; ENSG00000115414. [P02751-14]
ENST00000446046; ENSP00000410422; ENSG00000115414. [P02751-17]
GeneIDi2335.
KEGGihsa:2335.
UCSCiuc002vfa.3. human. [P02751-15]
uc002vfb.3. human. [P02751-14]
uc002vfc.3. human. [P02751-9]
uc002vfe.3. human. [P02751-3]
uc002vfg.3. human. [P02751-8]
uc002vfh.3. human.
uc002vfi.3. human. [P02751-7]
uc002vfj.3. human. [P02751-13]

Polymorphism databases

DMDMi300669710.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Fibronectin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ276395 mRNA. Translation: CAC20427.1 .
AJ535086 mRNA. Translation: CAD59389.1 .
AJ849445 mRNA. Translation: CAH60958.1 .
AB191261 mRNA. Translation: BAD52437.1 .
AB209840 mRNA. Translation: BAD93077.1 . Different initiation.
AL832202 mRNA. Translation: CAD91166.1 . Different initiation.
BX537590 mRNA. Translation: CAD97791.1 .
BX538017 mRNA. Translation: CAD97964.1 . Different initiation.
BX538018 mRNA. Translation: CAD97965.1 . Different initiation.
BX538045 mRNA. Translation: CAD97984.1 . Different initiation.
BX640608 mRNA. Translation: CAE45714.1 .
BX640731 mRNA. Translation: CAE45847.1 .
BX640875 mRNA. Translation: CAE45932.1 .
BX640920 mRNA. Translation: CAE45958.1 .
CR749281 mRNA. Translation: CAH18136.1 . Different initiation.
CR749316 mRNA. Translation: CAH18171.1 .
CR749317 mRNA. Translation: CAH18172.1 .
AC012462 Genomic DNA. Translation: AAX76513.1 . Sequence problems.
AC073284 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70536.1 .
BC117176 mRNA. Translation: AAI17177.1 .
BC143763 mRNA. Translation: AAI43764.1 .
M15801 Genomic DNA. Translation: AAA53376.1 .
AF312399 mRNA. Translation: AAG30571.1 .
X02761 mRNA. Translation: CAA26536.1 .
U41850 mRNA. Translation: AAD00014.1 .
U42404 mRNA. Translation: AAD00015.1 .
U42592 mRNA. Translation: AAD00017.1 .
U42593 mRNA. Translation: AAD00018.1 .
U42594 mRNA. Translation: AAD00019.1 .
U42455 mRNA. Translation: AAD09448.1 .
U42456 mRNA. Translation: AAD09449.1 .
U42458 mRNA. Translation: AAD09450.1 .
U42457 mRNA. Translation: AAD04751.1 .
X07718 Genomic DNA. Translation: CAB52436.1 . Different termination.
X07717 Genomic DNA. Translation: CAB52437.1 .
M18179 , M18177 , M18178 Genomic DNA. Translation: AAA52461.1 .
M12549 Genomic DNA. Translation: AAA58483.1 .
M10905 mRNA. Translation: AAA52462.1 .
M14059 mRNA. Translation: AAA52463.1 .
AJ320525 mRNA. Translation: CAC86914.1 .
AJ320526 mRNA. Translation: CAC86915.1 .
AJ320527 mRNA. Translation: CAC86916.1 .
M27589 mRNA. Translation: AAA52465.1 .
X04530 Genomic DNA. No translation available.
CCDSi CCDS2399.1. [P02751-3 ]
CCDS2400.1. [P02751-10 ]
CCDS42813.1. [P02751-8 ]
CCDS42814.1. [P02751-15 ]
CCDS46510.1. [P02751-17 ]
PIRi A26460. FNHU.
I52394.
S00848.
RefSeqi NP_002017.1. NM_002026.2.
NP_473375.2. NM_054034.2.
NP_997639.1. NM_212474.1.
NP_997641.1. NM_212476.1.
NP_997643.1. NM_212478.1.
NP_997647.1. NM_212482.1.
XP_005246457.1. XM_005246400.1. [P02751-7 ]
XP_005246463.1. XM_005246406.1. [P02751-1 ]
XP_005246470.1. XM_005246413.1. [P02751-13 ]
XP_005246472.1. XM_005246415.1. [P02751-14 ]
XP_005246474.1. XM_005246417.1. [P02751-9 ]
UniGenei Hs.203717.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E88 NMR - A 305-464 [» ]
1E8B NMR - A 305-464 [» ]
1FBR NMR - A 183-275 [» ]
1FNA X-ray 1.80 A 1452-1542 [» ]
1FNF X-ray 2.00 A 1173-1540 [» ]
1FNH X-ray 2.80 A 1721-1991 [» ]
1J8K NMR - A 1631-1724 [» ]
1O9A NMR - A 48-140 [» ]
1OWW NMR - A 608-701 [» ]
1Q38 NMR - A 631-705 [» ]
1QGB NMR - A 48-140 [» ]
1QO6 NMR - A 305-405 [» ]
1TTF NMR - A 1447-1540 [» ]