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Protein

Fibronectin

Gene

FN1

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

Functioni

Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.
Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei663Important for superfibronectin formation1
Sitei666Important for superfibronectin formation1

Regions

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding
Biological processAcute phase, Angiogenesis, Cell adhesion, Cell shape

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1474244 Extracellular matrix organization
R-HSA-1566977 Fibronectin matrix formation
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2129379 Molecules associated with elastic fibres
R-HSA-216083 Integrin cell surface interactions
R-HSA-3000170 Syndecan interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-HSA-372708 p130Cas linkage to MAPK signaling for integrins
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8957275 Post-translational protein phosphorylation
SIGNORiP02751

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Alternative name(s):
Cold-insoluble globulin
Short name:
CIG
Cleaved into the following 4 chains:
Gene namesi
Name:FN1
Synonyms:FN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000115414.18
HGNCiHGNC:3778 FN1
MIMi135600 gene
neXtProtiNX_P02751

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Glomerulopathy with fibronectin deposits 2 (GFND2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionGenetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.
See also OMIM:601894
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant dbSNP:rs137854488EnsemblClinVar.1
Natural variantiVAR_0439191834W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854486Ensembl.1
Natural variantiVAR_0439201883L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854487Ensembl.1
Spondylometaphyseal dysplasia, corner fracture type (SMDCF)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDCF is characterized by flake-like, triangular, or curvilinear ossification centers at the edges of irregular metaphyses that simulate fractures. These corner fractures involve the distal tibia, the ulnar aspect of the distal radius, the proximal humerus, and the proximal femur. They represent irregular ossification at the growth plates and secondary ossification centers.
See also OMIM:184255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08052387C → F in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080524123C → R in SMDCF. 1 Publication1
Natural variantiVAR_080525225C → W in SMDCF. 1 Publication1
Natural variantiVAR_080526240Y → D in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080527260C → G in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080528809Missing in SMDCF; unknown pathological significance. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi641Y → A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683. 1 Publication1
Mutagenesisi642I → A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692. 1 Publication1
Mutagenesisi663L → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 K but abolishes polymerization activity; when associated with A-666. 2 Publications1
Mutagenesisi666Y → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 kinase but abolishes polymerization activity; when associated with A-663. 2 Publications1
Mutagenesisi681L → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683. 1 Publication1
Mutagenesisi682I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692. 1 Publication1
Mutagenesisi683S → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681. 1 Publication1
Mutagenesisi684I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692. 1 Publication1
Mutagenesisi691E → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696. 1 Publication1
Mutagenesisi692V → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684. 1 Publication1
Mutagenesisi694R → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696. 1 Publication1
Mutagenesisi695F → A: Loss of ability to form fibronectin aggregates; when associated with A-697. 1 Publication1
Mutagenesisi696D → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694. 1 Publication1
Mutagenesisi697F → A: Loss of ability to form fibronectin aggregates; when associated with A-695. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi2335
MalaCardsiFN1
MIMi184255 phenotype
601894 phenotype
OpenTargetsiENSG00000115414
Orphaneti84090 Fibronectin glomerulopathy
93315 Spondylometaphyseal dysplasia, 'corner fracture' type
PharmGKBiPA28194

Chemistry databases

ChEMBLiCHEMBL3810
DrugBankiDB08888 Ocriplasmin

Polymorphism and mutation databases

BioMutaiFN1
DMDMi300669710

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Pyrrolidone carboxylic acid1 Publication1
Cross-linki34Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki47Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Disulfide bondi52 ↔ 78
Disulfide bondi76 ↔ 87
Disulfide bondi97 ↔ 125
Disulfide bondi123 ↔ 135
Disulfide bondi141 ↔ 169
Disulfide bondi167 ↔ 179
Disulfide bondi186 ↔ 215
Disulfide bondi213 ↔ 225
Disulfide bondi231 ↔ 260
Disulfide bondi258 ↔ 270
Glycosylationi279O-linked (GalNAc...) threonine1 Publication1
Disulfide bondi308 ↔ 335
Disulfide bondi333 ↔ 342
Disulfide bondi360 ↔ 386
Disulfide bondi374 ↔ 401
Disulfide bondi420 ↔ 446
Glycosylationi430N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi434 ↔ 461
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...) (complex) asparagine5 Publications1
Glycosylationi542N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei876SulfotyrosineSequence analysis1
Glycosylationi877N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei881SulfotyrosineSequence analysis1
Glycosylationi1007N-linked (GlcNAc...) (complex) asparagine4 Publications1
Glycosylationi1244N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi2064O-linked (GalNAc...) threonine1 Publication1
Glycosylationi2065O-linked (GalNAc...) threonine1 Publication1
Glycosylationi2108N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2206 ↔ 2235By similarity
Disulfide bondi2233 ↔ 2245By similarity
Disulfide bondi2251 ↔ 2278By similarity
Disulfide bondi2276 ↔ 2288By similarity
Disulfide bondi2295 ↔ 2319By similarity
Disulfide bondi2317 ↔ 2333By similarity
Modified residuei2363PhosphothreonineCombined sources1
Disulfide bondi2367Interchain (with C-2371)
Disulfide bondi2371Interchain (with C-2367)
Modified residuei2384Phosphoserine; by FAM20CCombined sources1 Publication1

Post-translational modificationi

Sulfated.1 Publication
It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated.9 Publications
Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
Phosphorylated by FAM20C in the extracellular medium.1 Publication
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2108Not glycosylated1 Publication1

Keywords - PTMi

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

Proteomic databases

EPDiP02751
MaxQBiP02751
PeptideAtlasiP02751
PRIDEiP02751
ProteomicsDBi51567
51568 [P02751-10]
51569 [P02751-11]
51570 [P02751-12]
51571 [P02751-13]
51572 [P02751-14]
51573 [P02751-15]
51574 [P02751-2]
51575 [P02751-3]
51576 [P02751-4]
51577 [P02751-5]
51578 [P02751-6]
51579 [P02751-7]
51580 [P02751-8]
51581 [P02751-9]

2D gel databases

DOSAC-COBS-2DPAGEiP02751

PTM databases

CarbonylDBiP02751
GlyConnecti161
iPTMnetiP02751
PhosphoSitePlusiP02751
SwissPalmiP02751
UniCarbKBiP02751

Expressioni

Tissue specificityi

Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine.2 Publications

Developmental stagei

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

Gene expression databases

BgeeiENSG00000115414 Expressed in 242 organ(s), highest expression level in tendon
ExpressionAtlasiP02751 baseline and differential
GenevisibleiP02751 HS

Organism-specific databases

HPAiCAB000126
HPA027066

Interactioni

Subunit structurei

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP (PubMed:12225811). Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC.By similarity9 Publications
(Microbial infection) Interacts with S.aureus fnbA.1 Publication
(Microbial infection) Interacts with M.bovis fbpB via the collagen-binding region.1 Publication
(Microbial infection) Interacts with fibronectin-binding proteins from other Mycobacteria.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108621, 743 interactors
CORUMiP02751
DIPiDIP-29547N
ELMiP02751
IntActiP02751, 503 interactors
MINTiP02751

Chemistry databases

BindingDBiP02751

Structurei

Secondary structure

12386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02751
SMRiP02751
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02751

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

GeneTreeiENSGT00930000150813
HOGENOMiHOG000234344
HOVERGENiHBG053239
InParanoidiP02751
KOiK05717
OMAiYILRWKP
OrthoDBiEOG091G116D
PhylomeDBiP02751
TreeFamiTF329915

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 16 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 16 hits
InterProiView protein in InterPro
IPR000083 Fibronectin_type1
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR013783 Ig-like_fold
IPR013806 Kringle-like
PfamiView protein in Pfam
PF00039 fn1, 12 hits
PF00040 fn2, 2 hits
PF00041 fn3, 16 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 16 hits
SUPFAMiSSF49265 SSF49265, 10 hits
SSF57440 SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022 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

Sequences (17+)i

Sequence statusi: Complete.

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

This entry describes 17 isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 17 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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

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

« Hide
        10         20         30         40         50
MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP
60 70 80 90 100
GCYDNGKHYQ INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK
110 120 130 140 150
YTGNTYRVGD TYERPKDSMI WDCTCIGAGR GRISCTIANR CHEGGQSYKI
160 170 180 190 200
GDTWRRPHET GGYMLECVCL GNGKGEWTCK PIAEKCFDHA AGTSYVVGET
210 220 230 240 250
WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY RIGDTWSKKD
260 270 280 290 300
NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP
310 320 330 340 350
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHTVLVQT RGGNSNGALC HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDM GHMMRCTCVG
510 520 530 540 550
NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS
660 670 680 690 700
VGRWKEATIP GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT
710 720 730 740 750
STSTPVTSNT VTGETTPFSP LVATSESVTE ITASSFVVSW VSASDTVSGF
760 770 780 790 800
RVEYELSEEG DEPQYLDLPS TATSVNIPDL LPGRKYIVNV YQISEDGEQS
810 820 830 840 850
LILSTSQTTA PDAPPDTTVD QVDDTSIVVR WSRPQAPITG YRIVYSPSVE
860 870 880 890 900
GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG
910 920 930 940 950
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH
960 970 980 990 1000
GQRLPISRNT FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP
1010 1020 1030 1040 1050
TNLQFVNETD STVLVRWTPP RAQITGYRLT VGLTRRGQPR QYNVGPSVSK
1060 1070 1080 1090 1100
YPLRNLQPAS EYTVSLVAIK GNQESPKATG VFTTLQPGSS IPPYNTEVTE
1110 1120 1130 1140 1150
TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV SGLTPGVEYV
1160 1170 1180 1190 1200
YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
1210 1220 1230 1240 1250
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV
1260 1270 1280 1290 1300
KDDKESVPIS DTIIPAVPPP TDLRFTNIGP DTMRVTWAPP PSIDLTNFLV
1310 1320 1330 1340 1350
RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYVVSVSS VYEQHESTPL
1360 1370 1380 1390 1400
RGRQKTGLDS PTGIDFSDIT ANSFTVHWIA PRATITGYRI RHHPEHFSGR
1410 1420 1430 1440 1450
PREDRVPHSR NSITLTNLTP GTEYVVSIVA LNGREESPLL IGQQSTVSDV
1460 1470 1480 1490 1500
PRDLEVVAAT PTSLLISWDA PAVTVRYYRI TYGETGGNSP VQEFTVPGSK
1510 1520 1530 1540 1550
STATISGLKP GVDYTITVYA VTGRGDSPAS SKPISINYRT EIDKPSQMQV
1560 1570 1580 1590 1600
TDVQDNSISV KWLPSSSPVT GYRVTTTPKN GPGPTKTKTA GPDQTEMTIE
1610 1620 1630 1640 1650
GLQPTVEYVV SVYAQNPSGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
1660 1670 1680 1690 1700
AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGEEDTAELQ GLRPGSEYTV
1710 1720 1730 1740 1750
SVVALHDDME SQPLIGTQST AIPAPTDLKF TQVTPTSLSA QWTPPNVQLT
1760 1770 1780 1790 1800
GYRVRVTPKE KTGPMKEINL APDSSSVVVS GLMVATKYEV SVYALKDTLT
1810 1820 1830 1840 1850
SRPAQGVVTT LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAVP
1860 1870 1880 1890 1900
ANGQTPIQRT IKPDVRSYTI TGLQPGTDYK IYLYTLNDNA RSSPVVIDAS
1910 1920 1930 1940 1950
TAIDAPSNLR FLATTPNSLL VSWQPPRARI TGYIIKYEKP GSPPREVVPR
1960 1970 1980 1990 2000
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL
2010 2020 2030 2040 2050
PHPNLHGPEI LDVPSTVQKT PFVTHPGYDT GNGIQLPGTS GQQPSVGQQM
2060 2070 2080 2090 2100
IFEEHGFRRT TPPTTATPIR HRPRPYPPNV GEEIQIGHIP REDVDYHLYP
2110 2120 2130 2140 2150
HGPGLNPNAS TGQEALSQTT ISWAPFQDTS EYIISCHPVG TDEEPLQFRV
2160 2170 2180 2190 2200
PGTSTSATLT GLTRGATYNV IVEALKDQQR HKVREEVVTV GNSVNEGLNQ
2210 2220 2230 2240 2250
PTDDSCFDPY TVSHYAVGDE WERMSESGFK LLCQCLGFGS GHFRCDSSRW
2260 2270 2280 2290 2300
CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG NGKGEFKCDP HEATCYDDGK
2310 2320 2330 2340 2350
TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP SPEGTTGQSY
2360 2370 2380
NQYSQRYHQR TNTNVNCPIE CFMPLDVQAD REDSRE
Length:2,386
Mass (Da):262,625
Last modified:July 13, 2010 - v4
Checksum:i5F7EDB9700335098
GO
Isoform 2 (identifier: P02751-2) [UniParc]FASTAAdd to basket
Also known as: MSF-FN70, Migration stimulation factor FN70

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

Show »
Length:642
Mass (Da):71,971
Checksum:iC66606885E3FA200
GO
Isoform 3 (identifier: P02751-3) [UniParc]FASTAAdd to basket
Also known as: V89

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

Show »
Length:2,355
Mass (Da):259,216
Checksum:i6AAF44283F1E04C6
GO
Isoform 4 (identifier: P02751-4) [UniParc]FASTAAdd to basket
Also known as: Fibronectin III-15X

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

Show »
Length:2,031
Mass (Da):222,976
Checksum:i92B5303A584A0FB1
GO
Isoform 5 (identifier: P02751-5) [UniParc]FASTAAdd to basket
Also known as: Fibronectin (V+I-10)-

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

Show »
Length:2,211
Mass (Da):243,334
Checksum:iA2F5D57DDD663FA0
GO
Isoform 6 (identifier: P02751-6) [UniParc]FASTAAdd to basket
Also known as: Fibronectin (V+III-15)-

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

Show »
Length:2,184
Mass (Da):240,509
Checksum:i72C662DC4C18DA2B
GO
Isoform 7 (identifier: P02751-7) [UniParc]FASTAAdd to basket
Also known as: Fibronectin containing extra ED-B domain

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

Show »
Length:2,446
Mass (Da):268,912
Checksum:i630CB516DE884514
GO
Isoform 8 (identifier: P02751-8) [UniParc]FASTAAdd to basket
Also known as: Fibronectin not containing EIIIA domain

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

Show »
Length:2,296
Mass (Da):252,811
Checksum:i2C4DEB94AD4D5435
GO
Isoform 9 (identifier: P02751-9) [UniParc]FASTAAdd to basket
Also known as: Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region

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

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

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

Show »
Length:2,176
Mass (Da):239,626
Checksum:i1CABF440AE6185E2
GO
Isoform 11 (identifier: P02751-11) [UniParc]FASTAAdd to basket
Also known as: Fibronectin containing extra type III repeat (EDII), exon x+2

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

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

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

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

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

Note: No experimental confirmation available.
Show »
Length:2,267
Mass (Da):249,322
Checksum:i4C45B65A37F78909
GO
Isoform 14 (identifier: P02751-14) [UniParc]FASTAAdd to basket

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

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

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

Note: No experimental confirmation available.
Show »
Length:2,477
Mass (Da):272,320
Checksum:i6C436A7A5FEE6DEB
GO
Isoform 16 (identifier: P02751-16) [UniParc]FASTAAdd to basket
Also known as: Migration stimulation factor, MSF

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

Note: Expressed by fetal and tumor-associated cells.
Show »
Length:657
Mass (Da):73,683
Checksum:iFDEBA031AD18C721
GO
Isoform 17 (identifier: P02751-17) [UniParc]FASTAAdd to basket

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

Note: Gene prediction based on EST data.
Show »
Length:2,330
Mass (Da):256,502
Checksum:iFAACAE02C878443E
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y7Z1H0Y7Z1_HUMAN
Fibronectin
FN1
1,103Annotation score:
H0Y4K8H0Y4K8_HUMAN
Fibronectin
FN1
241Annotation score:

Sequence cautioni

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

Experimental Info

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04391715Q → L5 PublicationsCorresponds to variant dbSNP:rs1250259Ensembl.1
Natural variantiVAR_08052387C → F in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080524123C → R in SMDCF. 1 Publication1
Natural variantiVAR_080525225C → W in SMDCF. 1 Publication1
Natural variantiVAR_080526240Y → D in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080527260C → G in SMDCF; the mutant is not secreted. 1 Publication1
Natural variantiVAR_080528809Missing in SMDCF; unknown pathological significance. 1 Publication1
Natural variantiVAR_059529817T → P7 PublicationsCorresponds to variant dbSNP:rs2577301Ensembl.1
Natural variantiVAR_036018940D → N in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs752106647Ensembl.1
Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant dbSNP:rs137854488EnsemblClinVar.1
Natural variantiVAR_0360191120R → P in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0565761467S → R. Corresponds to variant dbSNP:rs11687611Ensembl.1
Natural variantiVAR_0439191834W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854486Ensembl.1
Natural variantiVAR_0439201883L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854487Ensembl.1
Natural variantiVAR_0439211960I → V1 PublicationCorresponds to variant dbSNP:rs1250209Ensembl.1
Natural variantiVAR_0565772121I → V. Corresponds to variant dbSNP:rs17449032Ensembl.1
Natural variantiVAR_0614862170V → ICombined sources11 PublicationsCorresponds to variant dbSNP:rs1250209Ensembl.1
Natural variantiVAR_0360202380D → N in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1373375768Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003255368 – 388GRTFY…LWCST → DRTDST in isoform 2. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_003256648 – 657KNSVGRWKEA → VSIPPRNLGY in isoform 2 and isoform 16. 3 Publications10
Alternative sequenceiVSP_003257658 – 2386Missing in isoform 2 and isoform 16. 3 PublicationsAdd BLAST1729
Alternative sequenceiVSP_0136811256 – 1487Missing in isoform 12. 1 PublicationAdd BLAST232
Alternative sequenceiVSP_0081041265P → PEVPQLTDLSFVDITDSSIG LRWTPLNSSTIIGYRITVVA AGEGIPIFEDFVDSSVGYYT VTGLEPGIDYDISVITLING GESAPTTLTQQT in isoform 7, isoform 13 and isoform 15. 1 Publication1
Alternative sequenceiVSP_0081051266 – 1365AVPPP…PTGID → EVPQLTDLSFVDITDSSIGL RWTPLNSSTIIGYRITVVAA GEGIPIFEDFVDSSVGYYTV TGLEPGIDYDISVITLINGG ESAPTTLTQQTAVPPPTDLR in isoform 11. CuratedAdd BLAST100
Alternative sequenceiVSP_0081061631 – 1721NIDRP…TQSTA → T in isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14. 5 PublicationsAdd BLAST91
Alternative sequenceiVSP_0081071991 – 2110Missing in isoform 4, isoform 5, isoform 10 and isoform 13. 3 Publications