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P02751

- FINC_HUMAN

UniProt

P02751 - FINC_HUMAN

Protein

Fibronectin

Gene

FN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 200 (01 Oct 2014)
      Sequence version 4 (13 Jul 2010)
      Previous versions | rss
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    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: UniProt
    4. peptidase activator activity Source: Ensembl
    5. protease binding Source: BHF-UCL
    6. protein binding Source: IntAct

    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

    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: 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

    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...)2 Publications
    Disulfide bondi308 ↔ 335
    Disulfide bondi333 ↔ 342
    Disulfide bondi360 ↔ 386
    Disulfide bondi374 ↔ 401
    Disulfide bondi420 ↔ 446
    Glycosylationi430 – 4301N-linked (GlcNAc...)4 Publications
    Disulfide bondi434 ↔ 461
    Disulfide bondi470 ↔ 498By similarity
    Disulfide bondi496 ↔ 508By similarity
    Disulfide bondi518 ↔ 545By similarity
    Glycosylationi528 – 5281N-linked (GlcNAc...) (complex)6 Publications
    Glycosylationi542 – 5421N-linked (GlcNAc...) (complex)4 Publications
    Disulfide bondi543 ↔ 555By similarity
    Disulfide bondi561 ↔ 589By similarity
    Disulfide bondi587 ↔ 599By similarity
    Modified residuei876 – 8761SulfotyrosineSequence Analysis
    Glycosylationi877 – 8771N-linked (GlcNAc...)3 Publications
    Modified residuei881 – 8811SulfotyrosineSequence Analysis
    Glycosylationi1007 – 10071N-linked (GlcNAc...) (complex)5 Publications
    Glycosylationi1244 – 12441N-linked (GlcNAc...)3 Publications
    Glycosylationi2064 – 20641O-linked (GalNAc...)2 Publications
    Glycosylationi2065 – 20651O-linked (GalNAc...)2 Publications
    Glycosylationi2108 – 21081N-linked (GlcNAc...)2 Publications
    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

    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.By similarity10 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. 450 interactions.
    MINTiMINT-1779779.

    Structurei

    Secondary structure

    1
    2386
    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.
    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.
    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.

    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
    Alternative sequencei1256 – 1487232Missing in isoform 12. 1 PublicationVSP_013681Add
    BLAST
    Alternative sequencei1265 – 12651P → PEVPQLTDLSFVDITDSSIG LRWTPLNSSTIIGYRITVVA AGEGIPIFEDFVDSSVGYYT VTGLEPGIDYDISVITLING GESAPTTLTQQT in isoform 7, isoform 13 and isoform 15. 1 PublicationVSP_008104
    Alternative sequencei1266 – 1365100AVPPP…PTGID → EVPQLTDLSFVDITDSSIGL RWTPLNSSTIIGYRITVVAA GEGIPIFEDFVDSSVGYYTV TGLEPGIDYDISVITLINGG ESAPTTLTQQTAVPPPTDLR in isoform 11. CuratedVSP_008105Add
    BLAST
    Alternative sequencei1631 – 172191NIDRP…TQSTA → T in isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14. 5 PublicationsVSP_008106Add
    BLAST
    Alternative sequencei1991 – 2110120Missing in isoform 4, isoform 5, isoform 10 and isoform 13. 3 PublicationsVSP_008107Add
    BLAST
    Alternative sequencei1991 – 201525Missing in isoform 9 and isoform 12. 2 PublicationsVSP_008108Add
    BLAST
    Alternative sequencei1992 – 2193202Missing in isoform 6. 1 PublicationVSP_008109Add
    BLAST
    Alternative sequencei1992 – 201625Missing in isoform 17. CuratedVSP_047310Add
    BLAST
    Alternative sequencei2081 – 211131Missing in isoform 3, isoform 7, isoform 9, isoform 12 and isoform 14. 6 PublicationsVSP_008110Add
    BLAST
    Alternative sequencei2082 – 211231Missing in isoform 17. CuratedVSP_047311Add
    BLAST
    Alternative sequencei2148 – 21514FRVP → STKA in isoform 4. 1 PublicationVSP_008111
    Alternative sequencei2152 – 2386235Missing in isoform 4. 1 PublicationVSP_008112Add
    BLAST
    Alternative sequencei2193 – 224755Missing in isoform 5. 1 PublicationVSP_008113Add
    BLAST

    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]
    CCDS46512.1. [P02751-16]
    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]
    ENST00000354785; ENSP00000346839; ENSG00000115414. [P02751-15]
    ENST00000356005; ENSP00000348285; ENSG00000115414. [P02751-8]
    ENST00000357867; ENSP00000350534; ENSG00000115414. [P02751-10]
    ENST00000359671; ENSP00000352696; ENSG00000115414. [P02751-1]
    ENST00000421182; ENSP00000394423; ENSG00000115414. [P02751-9]
    ENST00000426059; ENSP00000398907; ENSG00000115414. [P02751-16]
    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 ]
    CCDS46512.1. [P02751-16 ]
    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 [» ]
    1TTG NMR - A 1447-1540 [» ]
    2CG6 X-ray 1.55 A 93-182 [» ]
    2CG7 X-ray 1.20 A 93-182 [» ]
    2CK2 X-ray 2.00 A/B 1447-1542 [» ]
    2CKU NMR - A 93-182 [» ]
    2EC3 NMR - A 2239-2299 [» ]
    2FN2 NMR - A 406-464 [» ]
    2FNB NMR - A 1265-1355 [» ]
    2GEE X-ray 2.01 A 1205-1356 [» ]
    2H41 NMR - A 721-809 [» ]
    2H45 NMR - A 721-809 [» ]
    2HA1 NMR - A 609-809 [» ]
    2OCF X-ray 2.95 D 1447-1540 [» ]
    2RKY X-ray 1.80 A/C 183-275 [» ]
    2RKZ X-ray 2.00 A/B/C/D/E/F 93-182 [» ]
    2RL0 X-ray 2.00 A/B/D/F/I/K 184-272 [» ]
    3CAL X-ray 1.70 A/C 93-182 [» ]
    3EJH X-ray 2.10 A/B 516-608 [» ]
    3GXE X-ray 2.60 A/B 516-608 [» ]
    3M7P X-ray 2.50 A 297-604 [» ]
    3MQL X-ray 3.00 A 308-515 [» ]
    3R8Q X-ray 2.40 A 1721-1991 [» ]
    3T1W X-ray 2.40 A 1173-1448 [» ]
    3ZRZ X-ray 1.70 A/B 93-182 [» ]
    4GH7 X-ray 2.60 B/D 1173-1427 [» ]
    4JE4 X-ray 2.31 B 1450-1540 [» ]
    4JEG X-ray 2.30 B 1450-1540 [» ]
    4MMX X-ray 3.32 C 1448-1540 [» ]
    4MMY X-ray 3.18 C 1448-1540 [» ]
    4MMZ X-ray 3.10 C 1448-1540 [» ]
    ProteinModelPortali P02751.
    SMRi P02751. Positions 48-274, 297-606, 609-809, 1173-1540, 1631-1991, 2242-2299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108621. 718 interactions.
    DIPi DIP-29547N.
    IntActi P02751. 450 interactions.
    MINTi MINT-1779779.

    Chemistry

    BindingDBi P02751.
    ChEMBLi CHEMBL3810.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P02751.
    UniCarbKBi P02751.

    Polymorphism databases

    DMDMi 300669710.

    2D gel databases

    DOSAC-COBS-2DPAGE P02751.

    Proteomic databases

    MaxQBi P02751.
    PaxDbi P02751.
    PRIDEi P02751.

    Protocols and materials databases

    DNASUi 2335.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323926 ; ENSP00000323534 ; ENSG00000115414 . [P02751-7 ]
    ENST00000336916 ; ENSP00000338200 ; ENSG00000115414 . [P02751-3 ]
    ENST00000354785 ; ENSP00000346839 ; ENSG00000115414 . [P02751-15 ]
    ENST00000356005 ; ENSP00000348285 ; ENSG00000115414 . [P02751-8 ]
    ENST00000357867 ; ENSP00000350534 ; ENSG00000115414 . [P02751-10 ]
    ENST00000359671 ; ENSP00000352696 ; ENSG00000115414 . [P02751-1 ]
    ENST00000421182 ; ENSP00000394423 ; ENSG00000115414 . [P02751-9 ]
    ENST00000426059 ; ENSP00000398907 ; ENSG00000115414 . [P02751-16 ]
    ENST00000432072 ; ENSP00000399538 ; ENSG00000115414 . [P02751-13 ]
    ENST00000443816 ; ENSP00000415018 ; ENSG00000115414 . [P02751-14 ]
    ENST00000446046 ; ENSP00000410422 ; ENSG00000115414 . [P02751-17 ]
    GeneIDi 2335.
    KEGGi hsa:2335.
    UCSCi uc002vfa.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 ]

    Organism-specific databases

    CTDi 2335.
    GeneCardsi GC02M216225.
    <