Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P02751 (FINC_HUMAN)

Last modified June 16, 2009. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Fibronectin
      Short name=FN
Alternative name(s):
    Cold-insoluble globulin
      Short name=CIG
Cleaved into the following 3 chains:
    1- Recommended name:
            Ugl-Y1
    2- Recommended name:
            Ugl-Y2
    3- Recommended name:
            Ugl-Y3
Gene names
Name: FN1
Synonyms: FN
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length2386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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. Interaction with TNR mediates inhibition of cell adhesion and neurite outgrowth By similarity.

Subunit structure

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.

Subcellular location

Secreted › extracellular space › extracellular matrix.

Tissue specificity

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. Ref.14 Ref.33

Developmental stage

Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. Ref.14 Ref.33

Post-translational modification

Sulfated.

It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated. Ref.14 Ref.33 Ref.24 Ref.38 Ref.39 Ref.51

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).

Involvement in disease

Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a 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. Ref.60

Sequence similarities

Contains 12 fibronectin type-I domains.

Contains 2 fibronectin type-II domains.

Contains 16 fibronectin type-III domains.

Sequence caution

The sequence AAX76513.1 differs from that shown. Reason: Erroneous gene model prediction.

Hide | Top

Ontologies

Keywords
   Biological processAcute phase
Cell adhesion
Cell shape
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Phosphoprotein
Pyrrolidone carboxylic acid
Sulfation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Non-traceable author statement. Source: UniProtKB

peptide cross-linking

Inferred from direct assay. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

substrate adhesion-dependent cell spreading

Inferred from direct assay. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Non-traceable author statement. Source: UniProtKB

   Cellular componentER-Golgi intermediate compartment

Inferred from direct assay. Source: UniProtKB

fibrinogen complex

Inferred from direct assay. Source: UniProtKB

platelet alpha granule lumen

Inferred from Experiment. Source: Reactome

proteinaceous extracellular matrix

Non-traceable author statement. Source: UniProtKB

   Molecular functioncollagen binding Ref.12

Non-traceable author statement. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement. Source: UniProtKB

heparin binding Ref.56

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Hide | Top

Alternative products

This entry describes 15 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P02751-1)

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.
Isoform 2 (identifier: P02751-2)

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.
Isoform 3 (identifier: P02751-3)

Also known as: V89;

The sequence of this isoform differs from the canonical sequence as follows:
     2081-2111: Missing.
Isoform 4 (identifier: P02751-4)

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.
Isoform 5 (identifier: P02751-5)

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.
Isoform 6 (identifier: P02751-6)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1992-2193: Missing.
Isoform 7 (identifier: P02751-7)

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.
Isoform 8 (identifier: P02751-8)

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
Isoform 9 (identifier: P02751-9)

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.
Isoform 10 (identifier: P02751-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     1991-2110: Missing.
Isoform 11 (identifier: P02751-11)

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
Isoform 12 (identifier: P02751-12)

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.
Isoform 13 (identifier: P02751-13)

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.
Isoform 14 (identifier: P02751-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1631-1721: NIDRPKGLAF...QPLIGTQSTA → T
     2081-2111: Missing.
Isoform 15 (identifier: P02751-15)

The sequence of this isoform differs from the canonical sequence as follows:
     1265-1265: P → PEVPQLTDLS...SAPTTLTQQT
Note: No experimental confirmation available.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.10
Chain32 – 23862355Fibronectin
PRO_0000019235
Chain723 – 911189Ugl-Y1
PRO_0000300249
Chain723 – 903181Ugl-Y2
PRO_0000300250
Chain723 – ?Ugl-Y3PRO_0000300251

Regions

Domain50 – 9041Fibronectin type-I 1
Domain95 – 13844Fibronectin type-I 2
Domain139 – 18244Fibronectin type-I 3
Domain184 – 22845Fibronectin type-I 4
Domain229 – 27345Fibronectin type-I 5
Domain306 – 34540Fibronectin type-I 6
Domain355 – 40349Fibronectin type-II 1
Domain415 – 46349Fibronectin type-II 2
Domain468 – 51144Fibronectin type-I 7
Domain516 – 55843Fibronectin type-I 8
Domain559 – 60244Fibronectin type-I 9
Domain607 – 69993Fibronectin type-III 1
Domain720 – 80990Fibronectin type-III 2
Domain811 – 89888Fibronectin type-III 3
Domain908 – 99588Fibronectin type-III 4
Domain996 – 108489Fibronectin type-III 5
Domain1087 – 117286Fibronectin type-III 6
Domain1173 – 126593Fibronectin type-III 7
Domain1266 – 135691Fibronectin type-III 8
Domain1357 – 144690Fibronectin type-III 9
Domain1447 – 153690Fibronectin type-III 10
Domain1541 – 163090Fibronectin type-III 11
Domain1631 – 172090Fibronectin type-III 12; extra domain
Domain1723 – 181088Fibronectin type-III 13
Domain1813 – 190189Fibronectin type-III 14
Domain1902 – 199190Fibronectin type-III 15
Domain2100 – 219091Fibronectin type-III 16
Domain2204 – 224845Fibronectin type-I 10
Domain2249 – 229143Fibronectin type-I 11
Domain2293 – 233644Fibronectin type-I 12
DNA binding907 – 1172266
Region52 – 272221Fibrin- and heparin-binding 1
Region308 – 608301Collagen-binding
Region464 – 47714Critical for collagen binding
Region1267 – 1540274Cell-attachment
Region1721 – 1991271Heparin-binding 2
Region1813 – 1991179Binds to FBLN1
Region1992 – 2102111Connecting strand 3 (CS-3) (V region)
Region2206 – 2337132Fibrin-binding 2
Motif1524 – 15263Cell attachment site

Sites

Site21081Not glycosylated

Amino acid modifications

Modified residue321Pyrrolidone carboxylic acid
Modified residue8761Sulfotyrosine Potential
Modified residue8811Sulfotyrosine Potential
Modified residue9041Phosphoserine Ref.41
Modified residue23841Phosphoserine Ref.40 Ref.42
Glycosylation4301N-linked (GlcNAc...) Ref.39 Ref.51
Glycosylation5281N-linked (GlcNAc...) Ref.38 Ref.39
Glycosylation5421N-linked (GlcNAc...) Ref.39
Glycosylation8771N-linked (GlcNAc...) Ref.14
Glycosylation10071N-linked (GlcNAc...) Ref.39
Glycosylation12441N-linked (GlcNAc...) Ref.39
Glycosylation20641O-linked (GalNAc...) Ref.24
Glycosylation20651O-linked (GalNAc...) Ref.24
Disulfide bond52 ↔ 78 Ref.46 Ref.57
Disulfide bond76 ↔ 87 Ref.46 Ref.57
Disulfide bond97 ↔ 125 Ref.46 Ref.57
Disulfide bond123 ↔ 135 Ref.46 Ref.57
Disulfide bond141 ↔ 169 Ref.46 Ref.57
Disulfide bond167 ↔ 179 Ref.46 Ref.57
Disulfide bond186 ↔ 215 Ref.46 Ref.57
Disulfide bond213 ↔ 225 Ref.46 Ref.57
Disulfide bond231 ↔ 260 Ref.46 Ref.57
Disulfide bond258 ↔ 270 Ref.46 Ref.57
Disulfide bond308 ↔ 335 Ref.46 Ref.57
Disulfide bond333 ↔ 342 Ref.46 Ref.57
Disulfide bond360 ↔ 386 Ref.46 Ref.57
Disulfide bond374 ↔ 401 Ref.46 Ref.57
Disulfide bond420 ↔ 446 Ref.46 Ref.57
Disulfide bond434 ↔ 461 Ref.46 Ref.57
Disulfide bond470 ↔ 498 By similarity
Disulfide bond496 ↔ 508 By similarity
Disulfide bond518 ↔ 545 By similarity
Disulfide bond543 ↔ 555 By similarity
Disulfide bond561 ↔ 589 By similarity
Disulfide bond587 ↔ 599 By similarity
Disulfide bond2206 ↔ 2235 By similarity
Disulfide bond2233 ↔ 2245 By similarity
Disulfide bond2251 ↔ 2278 By similarity
Disulfide bond2276 ↔ 2288 By similarity
Disulfide bond2295 ↔ 2319 By similarity
Disulfide bond2317 ↔ 2333 By similarity
Disulfide bond2367Interchain (with C-2371) Ref.46 Ref.57
Disulfide bond2371Interchain (with C-2367) Ref.46 Ref.57
Cross-link34Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity
Cross-link35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity
Cross-link47Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?) By similarity

Natural variations

Alternative sequence368 – 38821GRTFY…LWCST → DRTDST in isoform 2.
VSP_003255
Alternative sequence648 – 65710KNSVGRWKEA → VSIPPRNLGY in isoform 2.
VSP_003256
Alternative sequence658 – 23861729Missing in isoform 2.
VSP_003257
Alternative sequence1256 – 1487232Missing in isoform 12.
VSP_013681
Alternative sequence12651P → PEVPQLTDLSFVDITDSSIG LRWTPLNSSTIIGYRITVVA AGEGIPIFEDFVDSSVGYYT VTGLEPGIDYDISVITLING GESAPTTLTQQT in isoform 7, isoform 13 and isoform 15.
VSP_008104
Alternative sequence1266 – 1365100AVPPP…PTGID → EVPQLTDLSFVDITDSSIGL RWTPLNSSTIIGYRITVVAA GEGIPIFEDFVDSSVGYYTV TGLEPGIDYDISVITLINGG ESAPTTLTQQTAVPPPTDLR in isoform 11.
VSP_008105
Alternative sequence1631 – 172191NIDRP…TQSTA → T in isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14.
VSP_008106
Alternative sequence1991 – 2110120Missing in isoform 4, isoform 5, isoform 10 and isoform 13.
VSP_008107
Alternative sequence1991 – 201525Missing in isoform 9 and isoform 12.
VSP_008108
Alternative sequence1992 – 2193202Missing in isoform 6.
VSP_008109
Alternative sequence2081 – 211131Missing in isoform 3, isoform 7, isoform 9, isoform 12 and isoform 14.
VSP_008110
Alternative sequence2148 – 21514FRVP → STKA in isoform 4.
VSP_008111
Alternative sequence2152 – 2386235Missing in isoform 4.
VSP_008112
Alternative sequence2193 – 224755Missing in isoform 5.
VSP_008113
Natural variant151Q → L: dbSNP rs1250259. Ref.60 Ref.3 Ref.4 Ref.6 Ref.8
VAR_043917
Natural variant9401D → N in a breast cancer sample; somatic mutation. Ref.59
VAR_036018
Natural variant9731Y → C in GFND2. Ref.60
VAR_043918
Natural variant11201R → P in a breast cancer sample; somatic mutation. Ref.59
VAR_036019
Natural variant14671S → R: dbSNP rs11687611.
VAR_056576
Natural variant18341W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. Ref.60
VAR_043919
Natural variant18831L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. Ref.60
VAR_043920
Natural variant19601I → V: dbSNP rs1250209. Ref.60
VAR_043921
Natural variant21211I → V: dbSNP rs17449032.
VAR_056577
Natural variant23801D → N in a colorectal cancer sample; somatic mutation. Ref.59
VAR_036020

Experimental info

Sequence conflict321Q → R in CAH18171. Ref.4
Sequence conflict691Y → N in CAH18172. Ref.4
Sequence conflict731A → V in CAA26536. Ref.9
Sequence conflict1261I → V in CAH18136. Ref.4
Sequence conflict1991E → G in CAD91166. Ref.4
Sequence conflict2471S → R in CAD59389. Ref.1
Sequence conflict2601C → R in CAH18172. Ref.4
Sequence conflict2891V → A in CAE45847. Ref.4
Sequence conflict3551S → L in AAD00015. Ref.11
Sequence conflict3751T → A in CAH18136. Ref.4
Sequence conflict4111Q → R in CAC20427. Ref.1
Sequence conflict4111Q → R in CAD59389. Ref.1
Sequence conflict4111Q → R in BAD52437. Ref.2
Sequence conflict4111Q → R in CAD91166. Ref.4
Sequence conflict4111Q → R in CAD97791. Ref.4
Sequence conflict4111Q → R in CAD97964. Ref.4
Sequence conflict4111Q → R in CAD97965. Ref.4
Sequence conflict4111Q → R in CAE45714. Ref.4
Sequence conflict4111Q → R in CAE45847. Ref.4
Sequence conflict4111Q → R in CAE45932. Ref.4
Sequence conflict4111Q → R in CAH18136. Ref.4
Sequence conflict4111Q → R in CAH18171. Ref.4
Sequence conflict4111Q → R in CAH18172. Ref.4
Sequence conflict4111Q → R in BAD93077. Ref.3
Sequence conflict4111Q → R in AAX76513. Ref.5
Sequence conflict4111Q → R in AAI17177. Ref.6
Sequence conflict4111Q → R in AAG30571. Ref.9
Sequence conflict5181C → R in CAD97791. Ref.4
Sequence conflict5521R → K in CAD97965. Ref.4
Sequence conflict5521R → K in CAD97964. Ref.4
Sequence conflict5801V → A in CAH18172. Ref.4
Sequence conflict6781E → Q AA sequence Ref.13
Sequence conflict704 – 7052TP → PT AA sequence Ref.13
Sequence conflict8171P → T in AAX76513. Ref.5
Sequence conflict9801V → L in CAD97791. Ref.4
Sequence conflict10301T → A in CAH18136. Ref.4
Sequence conflict10481V → D in CAD97965. Ref.4
Sequence conflict10481V → D in CAD97964. Ref.4
Sequence conflict11341D → G in CAH18136. Ref.4
Sequence conflict11371S → N in CAD97965. Ref.4
Sequence conflict11371S → N in CAD97964. Ref.4
Sequence conflict11521T → I in CAH18136. Ref.4
Sequence conflict12221E → G in CAD97791. Ref.4
Sequence conflict12261H → Q in CAE45932. Ref.4
Sequence conflict15551D → G in CAE45714. Ref.4
Sequence conflict16011G → S in CAD97965. Ref.4
Sequence conflict16011G → S in CAD97964. Ref.4
Sequence conflict16221Q → E AA sequence Ref.24
Sequence conflict1715 – 17217IGTQSTA → VQTAVTT in AAA52463. Ref.26
Sequence conflict17261T → A in CAE45847. Ref.4
Sequence conflict17551R → W in CAH18136. Ref.4
Sequence conflict17681I → V in CAB52436. Ref.16
Sequence conflict17831M → T in CAE45932. Ref.4
Sequence conflict19271R → C in AAD00014. Ref.11
Sequence conflict19341I → V in CAH18172. Ref.4
Sequence conflict19921D → G in CAD97965. Ref.4
Sequence conflict19921D → G in CAD97964. Ref.4
Sequence conflict20231V → A in CAD97965. Ref.4
Sequence conflict20231V → A in CAD97964. Ref.4
Sequence conflict20271G → R in CAD97965. Ref.4
Sequence conflict20271G → R in CAD97964. Ref.4
Sequence conflict21701I → V in AAX76513. Ref.5
Sequence conflict22511C → R in CAH18172. Ref.4
Sequence conflict23121Y → N in CAD97965. Ref.4
Sequence conflict23121Y → N in CAD97964. Ref.4
Sequence conflict23411S → T in CAE45714. Ref.4
Sequence conflict23411S → T in CAH18171. Ref.4
Sequence conflict23411S → T in CAH18172. Ref.4
Sequence conflict23671C → Y in CAE45932. Ref.4

Secondary structure

1 ......................................................................................................................................................................................................................................... 2386
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: F346FB6832210FA9

FASTA2,386262,607
        10         20         30         40         50         60 
MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP GCYDNGKHYQ 

        70         80         90        100        110        120 
INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK YTGNTYRVGD TYERPKDSMI 

       130        140        150        160        170        180 
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK 

       190        200        210        220        230        240 
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY 

       250        260        270        280        290        300 
RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP 

       310        320        330        340        350        360 
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC 

       370        380        390        400        410        420 
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHTVLVQT QGGNSNGALC 

       430        440        450        460        470        480 
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI 

       490        500        510        520        530        540 
GDQWDKQHDM GHMMRCTCVG NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM 

       550        560        570        580        590        600 
LNCTCFGQGR GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ 

       610        620        630        640        650        660 
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS VGRWKEATIP 

       670        680        690        700        710        720 
GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT STSTPVTSNT VTGETTPFSP 

       730        740        750        760        770        780 
LVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVNIPDL 

       790        800        810        820        830        840 
LPGRKYIVNV YQISEDGEQS LILSTSQTTA PDAPPDPTVD QVDDTSIVVR WSRPQAPITG 

       850        860        870        880        890        900 
YRIVYSPSVE GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG 

       910        920        930        940        950        960 
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH GQRLPISRNT 

       970        980        990       1000       1010       1020 
FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP TNLQFVNETD STVLVRWTPP 

      1030       1040       1050       1060       1070       1080 
RAQITGYRLT VGLTRRGQPR QYNVGPSVSK YPLRNLQPAS EYTVSLVAIK GNQESPKATG 

      1090       1100       1110       1120       1130       1140 
VFTTLQPGSS IPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV 

      1150       1160       1170       1180       1190       1200 
SGLTPGVEYV YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT 

      1210       1220       1230       1240       1250       1260 
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV KDDKESVPIS 

      1270       1280       1290       1300       1310       1320 
DTIIPAVPPP TDLRFTNIGP DTMRVTWAPP PSIDLTNFLV RYSPVKNEED VAELSISPSD 

      1330       1340       1350       1360       1370       1380 
NAVVLTNLLP GTEYVVSVSS VYEQHESTPL RGRQKTGLDS PTGIDFSDIT ANSFTVHWIA 

      1390       1400       1410       1420       1430       1440 
PRATITGYRI RHHPEHFSGR PREDRVPHSR NSITLTNLTP GTEYVVSIVA LNGREESPLL 

      1450       1460       1470       1480       1490       1500 
IGQQSTVSDV PRDLEVVAAT PTSLLISWDA PAVTVRYYRI TYGETGGNSP VQEFTVPGSK 

      1510       1520       1530       1540       1550       1560 
STATISGLKP GVDYTITVYA VTGRGDSPAS SKPISINYRT EIDKPSQMQV TDVQDNSISV 

      1570       1580       1590       1600       1610       1620 
KWLPSSSPVT GYRVTTTPKN GPGPTKTKTA GPDQTEMTIE GLQPTVEYVV SVYAQNPSGE 

      1630       1640       1650       1660       1670       1680 
SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS RYRVTYSSPE DGIHELFPAP 

      1690       1700       1710       1720       1730       1740 
DGEEDTAELQ GLRPGSEYTV SVVALHDDME SQPLIGTQST AIPAPTDLKF TQVTPTSLSA 

      1750       1760       1770       1780       1790       1800 
QWTPPNVQLT GYRVRVTPKE KTGPMKEINL APDSSSVVVS GLMVATKYEV SVYALKDTLT 

      1810       1820       1830       1840       1850       1860 
SRPAQGVVTT LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAVP ANGQTPIQRT 

      1870       1880       1890       1900       1910       1920 
IKPDVRSYTI TGLQPGTDYK IYLYTLNDNA RSSPVVIDAS TAIDAPSNLR FLATTPNSLL 

      1930       1940       1950       1960       1970       1980 
VSWQPPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI TGLEPGTEYT IYVIALKNNQ 

      1990       2000       2010       2020       2030       2040 
KSEPLIGRKK TDELPQLVTL PHPNLHGPEI LDVPSTVQKT PFVTHPGYDT GNGIQLPGTS 

      2050       2060       2070       2080       2090       2100 
GQQPSVGQQM IFEEHGFRRT TPPTTATPIR HRPRPYPPNV GEEIQIGHIP REDVDYHLYP 

      2110       2120       2130       2140       2150       2160 
HGPGLNPNAS TGQEALSQTT ISWAPFQDTS EYIISCHPVG TDEEPLQFRV PGTSTSATLT 

      2170       2180       2190       2200       2210       2220 
GLTRGATYNI IVEALKDQQR HKVREEVVTV GNSVNEGLNQ PTDDSCFDPY TVSHYAVGDE 

      2230       2240       2250       2260       2270       2280 
WERMSESGFK LLCQCLGFGS GHFRCDSSRW CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG 

      2290       2300       2310       2320       2330       2340 
NGKGEFKCDP HEATCYDDGK TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP 

      2350       2360       2370       2380 
SPEGTTGQSY NQYSQRYHQR TNTNVNCPIE CFMPLDVQAD REDSRE

« Hide

Isoform 2 (MSF-FN70) (Migration stimulation factor FN70).

Checksum: F66607585E3FA299
Show »

FASTA64271,943
Isoform 3 (V89).

Checksum: 4F340858663A6775
Show »

FASTA2,355259,198
Isoform 4 (Fibronectin III-15X).

Checksum: EAFF51E6C4E34B9B
Show »

FASTA2,031222,944
Isoform 5 (Fibronectin (V+I-10)-).

Checksum: 1FE1225A5BB45B88
Show »

FASTA2,211243,316
Isoform 6 (Fibronectin (V+III-15)-).

Checksum: 4E878AABBE265F5E
Show »

FASTA2,184240,477
Isoform 7 (Fibronectin containing extra ED-B domain).

Checksum: C2114B00795CA0D6
Show »

FASTA2,446268,894
Isoform 8 (Fibronectin not containing EIIIA domain).

Checksum: 136ED3895D3F20C8
Show »

FASTA2,296252,793
Isoform 9 (Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region).

Checksum: AD7A0163A3FA6FD3
Show »

FASTA2,240246,670
Isoform 10.

Checksum: 340133CA851947CC
Show »

FASTA2,176239,608
Isoform 11 (Fibronectin containing extra type III repeat (EDII)) (exon x+2).

Checksum: 94364A40CAB83C50
Show »

FASTA2,386262,388
Isoform 12.

Checksum: A190321D611D015A
Show »

FASTA2,008221,274
Isoform 13.

Checksum: 7191EBFBEFD903F1
Show »

FASTA2,267249,304
Isoform 14.

Checksum: 9CEDA4F9F80E4638
Show »

FASTA2,265249,384
Isoform 15.

Checksum: BDDEE7807B63DCC1
Show »

FASTA2,477272,302

Hide | Top

References

« Hide 'large scale' references
[1]"Phenotypic and genetic alterations in mammary stroma: implications for tumour progression."
Schor S.L., Schor A.M.
Breast Cancer Res. 3:373-379(2001) [PubMed: 11737888] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Vector-capping: a simple method for preparing a high-quality full-length cDNA library."
Kato S., Ohtoko K., Ohtake H., Kimura T.
DNA Res. 12:53-62(2005) [PubMed: 16106752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
Tissue: Retinal pigment epithelium.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 14), VARIANT LEU-15.
Tissue: Aortic endothelium.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 7; 8; 9; 10; 13; 14 AND 15), VARIANT LEU-15.
Tissue: Amygdala, Cervix, Endometrial tumor and Uterine endothelium.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), VARIANT LEU-15.
Tissue: Cerebellum.
[7]"Human fibronectin is synthesized as a pre-propolypeptide."
Gutman A., Yamada K.M., Kornblihtt A.R.
FEBS Lett. 207:145-148(1986) [PubMed: 3770189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-38.
[8]"Cloning and analysis of the promotor region of the human fibronectin gene."
Dean D.C., Bowlus C.L., Bourgeois S.
Proc. Natl. Acad. Sci. U.S.A. 84:1876-1880(1987) [PubMed: 3031656] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, VARIANT LEU-15.
[9]"Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene."
Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E.
EMBO J. 4:1755-1759(1985) [PubMed: 2992939] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-2386 (ISOFORM 3).
[10]"Primary structure of human plasma fibronectin. The 29,000-dalton NH2-terminal domain."
Garcia-Pardo A., Pearlstein E., Frangione B.
J. Biol. Chem. 258:12670-12674(1983) [PubMed: 6630202] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-290.
[11]Godfrey H.P., Ebrahim A.A.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-481 (ISOFORMS 1/3/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [MRNA] OF 1116-1422 (ISOFORMS 1/3/4/5/6/8/9/10/14), NUCLEOTIDE SEQUENCE [MRNA] OF 1238-2160 (ISOFORMS 9 AND 12), NUCLEOTIDE SEQUENCE [MRNA] OF 1449-1825 (ISOFORMS 8/9/10/13/14), NUCLEOTIDE SEQUENCE [MRNA] OF 1919-2161 (ISOFORMS 3/7/14), NUCLEOTIDE SEQUENCE [MRNA] OF 2228-2386 (ISOFORMS 1/3/6/7/8/9/10/11/12/13/14/15).
Tissue: Peripheral blood T-cell and Umbilical vein endothelial cell.
[12]"Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli."
Owens R.J., Baralle F.E.
EMBO J. 5:2825-2830(1986) [PubMed: 3024962] [Abstract]
Cited for: PROTEIN SEQUENCE OF 309-608, COLLAGEN-BINDING.
[13]"Primary structure of a DNA- and heparin-binding domain (Domain III) in human plasma fibronectin."
Calaycay J., Pande H., Lee T., Borsi L., Siri A., Shively J.E., Zardi L.
J. Biol. Chem. 260:12136-12141(1985) [PubMed: 3900070] [Abstract]
Cited for: PROTEIN SEQUENCE OF 616-705.
[14]"Identification of novel fibronectin fragments detected specifically in juvenile urine."
Iida R., Yasuda T., Kishi K.
FEBS J. 274:3939-3947(2007) [PubMed: 17614963] [Abstract]
Cited for: PROTEIN SEQUENCE OF 723-911, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION AT ASN-877.
Tissue: Urine.
[15]"Human fibronectin: cell specific alternative mRNA splicing generates polypeptide chains differing in the number of internal repeats."
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.
Nucleic Acids Res. 12:5853-5868(1984) [PubMed: 6462919] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-2386 (ISOFORM 3).
[16]"Sequence analysis and in vivo expression show that alternative splicing of ED-B and ED-A regions of the human fibronectin gene are independent events."
Paolella G., Henchcliffe C., Sebastio G., Baralle F.E.
Nucleic Acids Res. 16:3545-3557(1988) [PubMed: 3375063] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1232-1782 (ISOFORMS 7/15).
[17]"Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon."
Zardi L., Carnemolla B., Siri A.,