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P02751 (FINC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 193. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibronectin
Short name=FN
Alternative name(s):
Cold-insoluble globulin
Short name=CIG

Cleaved into the following 4 chains:

  1. Anastellin
  2. Ugl-Y1
  3. Ugl-Y2
  4. Ugl-Y3
Gene names
Name:FN1
Synonyms:FN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

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. 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. Ref.38 Ref.40 Ref.44 Ref.52

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. Ref.38 Ref.40 Ref.44 Ref.52

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. Interacts with COMP. Interacts with S.aureus fnbA. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth By similarity. Interacts with FST3. Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.48

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.16 Ref.35

Developmental stage

Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age. Ref.16 Ref.35

Post-translational modification

Sulfated.

It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated. Ref.16 Ref.26 Ref.35 Ref.45 Ref.51 Ref.60

Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).

Phosphorylation sites are present in the extracellular medium.

Proteolytic processing produces the C-terminal NC1 peptide, anastellin.

Involvement in disease

Glomerulopathy with fibronectin deposits 2 (GFND2) [MIM:601894]: Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.74

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.

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 CAH18136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAcute phase
Angiogenesis
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
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-independent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

cell-substrate junction assembly

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

peptide cross-linking

Inferred from direct assay PubMed 3997886. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 16236823. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basement membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 15308636. Source: UniProtKB

fibrinogen complex

Inferred from direct assay PubMed 3997886. Source: BHF-UCL

platelet alpha granule lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Non-traceable author statement. Source: UniProtKB

   Molecular_functioncollagen binding

Non-traceable author statement Ref.14. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement. Source: UniProtKB

heparin binding

Non-traceable author statement Ref.66. Source: UniProtKB

peptidase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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
SCGB1A1P116843EBI-1220319,EBI-7797649
TGM2P219803EBI-1220319,EBI-727668
VHLP403372EBI-1220319,EBI-301246

Alternative products

This entry describes 17 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.
Isoform 16 (identifier: P02751-16)

Also known as: Migration stimulation factor; MSF;

The sequence of this isoform differs from the canonical sequence as follows:
     658-2386: Missing.
Note: Expressed by fetal and tumor-associated cells.
Isoform 17 (identifier: P02751-17)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Ref.12
Chain32 – 23862355Fibronectin
PRO_0000019235
Chain627 – 70276Anastellin
PRO_0000390479
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
Domain610 – 70293Fibronectin type-III 1
Domain722 – 81291Fibronectin type-III 2
Domain813 – 90492Fibronectin type-III 3
Domain909 – 99890Fibronectin type-III 4
Domain999 – 108890Fibronectin type-III 5
Domain1089 – 117587Fibronectin type-III 6
Domain1176 – 126691Fibronectin type-III 7
Domain1269 – 136193Fibronectin type-III 8
Domain1362 – 144988Fibronectin type-III 9
Domain1450 – 154394Fibronectin type-III 10
Domain1544 – 163592Fibronectin type-III 11
Domain1636 – 172388Fibronectin type-III 12; extra domain
Domain1724 – 181794Fibronectin type-III 13
Domain1818 – 190487Fibronectin type-III 14
Domain1905 – 199591Fibronectin type-III 15
Domain2103 – 219795Fibronectin 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

Site6631Important for superfibronectin formation
Site6661Important for superfibronectin formation
Site21081Not glycosylated

Amino acid modifications

Modified residue321Pyrrolidone carboxylic acid
Modified residue8761Sulfotyrosine Potential
Modified residue8811Sulfotyrosine Potential
Modified residue23841Phosphoserine Ref.47 Ref.49
Glycosylation2791O-linked (GalNAc...) Ref.45
Glycosylation4301N-linked (GlcNAc...) Ref.45 Ref.46 Ref.60
Glycosylation5281N-linked (GlcNAc...) (complex) Ref.43 Ref.45 Ref.46 Ref.50 Ref.51
Glycosylation5421N-linked (GlcNAc...) (complex) Ref.45 Ref.46 Ref.51
Glycosylation8771N-linked (GlcNAc...) Ref.16 Ref.45
Glycosylation10071N-linked (GlcNAc...) (complex) Ref.45 Ref.46 Ref.50 Ref.51
Glycosylation12441N-linked (GlcNAc...) Ref.45 Ref.46
Glycosylation20641O-linked (GalNAc...) Ref.26
Glycosylation20651O-linked (GalNAc...) Ref.26
Glycosylation21081N-linked (GlcNAc...) Ref.26 Ref.45
Disulfide bond52 ↔ 78 Ref.55 Ref.69
Disulfide bond76 ↔ 87 Ref.55 Ref.69
Disulfide bond97 ↔ 125 Ref.55 Ref.69
Disulfide bond123 ↔ 135 Ref.55 Ref.69
Disulfide bond141 ↔ 169 Ref.55 Ref.69
Disulfide bond167 ↔ 179 Ref.55 Ref.69
Disulfide bond186 ↔ 215 Ref.55 Ref.69
Disulfide bond213 ↔ 225 Ref.55 Ref.69
Disulfide bond231 ↔ 260 Ref.55 Ref.69
Disulfide bond258 ↔ 270 Ref.55 Ref.69
Disulfide bond308 ↔ 335 Ref.55 Ref.69
Disulfide bond333 ↔ 342 Ref.55 Ref.69
Disulfide bond360 ↔ 386 Ref.55 Ref.69
Disulfide bond374 ↔ 401 Ref.55 Ref.69
Disulfide bond420 ↔ 446 Ref.55 Ref.69
Disulfide bond434 ↔ 461 Ref.55 Ref.69
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.55 Ref.69
Disulfide bond2371Interchain (with C-2367) Ref.55 Ref.69
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 and isoform 16.
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 sequence1992 – 201625Missing in isoform 17.
VSP_047310
Alternative sequence2081 – 211131Missing in isoform 3, isoform 7, isoform 9, isoform 12 and isoform 14.
VSP_008110
Alternative sequence2082 – 211231Missing in isoform 17.
VSP_047311
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. Ref.4 Ref.5 Ref.8 Ref.10 Ref.74
Corresponds to variant rs1250259 [ dbSNP | Ensembl ].
VAR_043917
Natural variant8171T → P. Ref.1 Ref.3 Ref.4 Ref.5 Ref.8 Ref.11 Ref.16
Corresponds to variant rs2577301 [ dbSNP | Ensembl ].
VAR_059529
Natural variant9401D → N in a breast cancer sample; somatic mutation. Ref.73
VAR_036018
Natural variant9731Y → C in GFND2. Ref.74
VAR_043918
Natural variant11201R → P in a breast cancer sample; somatic mutation. Ref.73
VAR_036019
Natural variant14671S → R.
Corresponds to variant rs11687611 [ dbSNP | Ensembl ].
VAR_056576
Natural variant18341W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. Ref.74
VAR_043919
Natural variant18831L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. Ref.74
VAR_043920
Natural variant19601I → V. Ref.74
Corresponds to variant rs1250209 [ dbSNP | Ensembl ].
VAR_043921
Natural variant21211I → V.
Corresponds to variant rs17449032 [ dbSNP | Ensembl ].
VAR_056577
Natural variant21701V → I. Ref.1 Ref.3 Ref.4 Ref.5 Ref.8 Ref.11 Ref.17 Ref.25 Ref.26 Ref.29 Ref.32 Ref.75
Corresponds to variant rs1250209 [ dbSNP | Ensembl ].
VAR_061486
Natural variant23801D → N in a colorectal cancer sample; somatic mutation. Ref.73
VAR_036020

Experimental info

Mutagenesis6411Y → A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683. Ref.62
Mutagenesis6421I → A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692. Ref.62
Mutagenesis6631L → 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. Ref.52 Ref.62
Mutagenesis6661Y → 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. Ref.52 Ref.62
Mutagenesis6811L → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683. Ref.62
Mutagenesis6821I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692. Ref.62
Mutagenesis6831S → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681. Ref.62
Mutagenesis6841I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692. Ref.62
Mutagenesis6911E → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696. Ref.62
Mutagenesis6921V → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684. Ref.62
Mutagenesis6941R → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696. Ref.62
Mutagenesis6951F → A: Loss of ability to form fibronectin aggregates; when associated with A-697. Ref.62
Mutagenesis6961D → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694. Ref.62
Mutagenesis6971F → A: Loss of ability to form fibronectin aggregates; when associated with A-695. Ref.62
Sequence conflict321Q → R in CAH18171. Ref.5
Sequence conflict691Y → N in CAH18172. Ref.5
Sequence conflict731A → V in CAA26536. Ref.11
Sequence conflict1261I → V in CAH18136. Ref.5
Sequence conflict1991E → G in CAD91166. Ref.5
Sequence conflict2471S → R in CAD59389. Ref.1
Sequence conflict2471S → R in CAH60958. Ref.2
Sequence conflict2601C → R in CAH18172. Ref.5
Sequence conflict2891V → A in CAE45847. Ref.5
Sequence conflict3551S → L in AAD00015. Ref.13
Sequence conflict3751T → A in CAH18136. Ref.5
Sequence conflict4111R → Q in AAD00015. Ref.13
Sequence conflict5181C → R in CAD97791. Ref.5
Sequence conflict5521R → K in CAD97965. Ref.5
Sequence conflict5521R → K in CAD97964. Ref.5
Sequence conflict5801V → A in CAH18172. Ref.5
Sequence conflict6781E → Q AA sequence Ref.15
Sequence conflict704 – 7052TP → PT AA sequence Ref.15
Sequence conflict9801V → L in CAD97791. Ref.5
Sequence conflict10301T → A in CAH18136. Ref.5
Sequence conflict10481V → D in CAD97965. Ref.5
Sequence conflict10481V → D in CAD97964. Ref.5
Sequence conflict11341D → G in CAH18136. Ref.5
Sequence conflict11371S → N in CAD97965. Ref.5
Sequence conflict11371S → N in CAD97964. Ref.5
Sequence conflict11521T → I in CAH18136. Ref.5
Sequence conflict12221E → G in CAD97791. Ref.5
Sequence conflict12261H → Q in CAE45932. Ref.5
Sequence conflict15551D → G in CAE45714. Ref.5
Sequence conflict16011G → S in CAD97965. Ref.5
Sequence conflict16011G → S in CAD97964. Ref.5
Sequence conflict16221Q → E AA sequence Ref.26
Sequence conflict1715 – 17217IGTQSTA → VQTAVTT in AAA52463. Ref.28
Sequence conflict17261T → A in CAE45847. Ref.5
Sequence conflict17551R → W in CAH18136. Ref.5
Sequence conflict17681I → V in CAB52436. Ref.18
Sequence conflict17831M → T in CAE45932. Ref.5
Sequence conflict19271R → C in AAD00014. Ref.13
Sequence conflict19341I → V in CAH18172. Ref.5
Sequence conflict19921D → G in CAD97965. Ref.5
Sequence conflict19921D → G in CAD97964. Ref.5
Sequence conflict20231V → A in CAD97965. Ref.5
Sequence conflict20231V → A in CAD97964. Ref.5
Sequence conflict20271G → R in CAD97965. Ref.5
Sequence conflict20271G → R in CAD97964. Ref.5
Sequence conflict22511C → R in CAH18172. Ref.5
Sequence conflict23121Y → N in CAD97965. Ref.5
Sequence conflict23121Y → N in CAD97964. Ref.5
Sequence conflict23411S → T in CAE45714. Ref.5
Sequence conflict23411S → T in CAH18171. Ref.5
Sequence conflict23411S → T in CAH18172. Ref.5
Sequence conflict23411S → T in CAE45958. Ref.5
Sequence conflict23671C → Y in CAE45932. Ref.5

Secondary structure

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

Details...

Sequences

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

Last modified July 13, 2010. Version 4.
Checksum: 5F7EDB9700335098

FASTA2,386262,625
        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 RGGNSNGALC 

       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 PDAPPDTTVD 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 
GLTRGATYNV 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) [UniParc].

Checksum: C66606885E3FA200
Show »

FASTA64271,971
Isoform 3 (V89) [UniParc].

Checksum: 6AAF44283F1E04C6
Show »

FASTA2,355259,216
Isoform 4 (Fibronectin III-15X) [UniParc].

Checksum: 92B5303A584A0FB1
Show »

FASTA2,031222,976
Isoform 5 (Fibronectin (V+I-10)-) [UniParc].

Checksum: A2F5D57DDD663FA0
Show »

FASTA2,211243,334
Isoform 6 (Fibronectin (V+III-15)-) [UniParc].

Checksum: 72C662DC4C18DA2B
Show »

FASTA2,184240,509
Isoform 7 (Fibronectin containing extra ED-B domain) [UniParc].

Checksum: 630CB516DE884514
Show »

FASTA2,446268,912
Isoform 8 (Fibronectin not containing EIIIA domain) [UniParc].

Checksum: 2C4DEB94AD4D5435
Show »

FASTA2,296252,811
Isoform 9 (Fibronectin not containing EIIIA and EIIIB and uses V64 variant of IIICS region) [UniParc].

Checksum: 5C46F0CECC71F96F
Show »

FASTA2,240246,688
Isoform 10 [UniParc].

Checksum: 1CABF440AE6185E2
Show »

FASTA2,176239,626
Isoform 11 (Fibronectin containing extra type III repeat (EDII)) (exon x+2) [UniParc].

Checksum: 380E6ABFF8AA6361
Show »

FASTA2,386262,406
Isoform 12 [UniParc].

Checksum: 697C36C79E89EB78
Show »

FASTA2,008221,292
Isoform 13 [UniParc].

Checksum: 4C45B65A37F78909
Show »

FASTA2,267249,322
Isoform 14 [UniParc].

Checksum: AC05A50EA66B26C5
Show »

FASTA2,265249,402
Isoform 15 [UniParc].

Checksum: 6C436A7A5FEE6DEB
Show »

FASTA2,477272,320
Isoform 16 (Migration stimulation factor) (MSF) [UniParc].

Checksum: 735BED369D07D294
Show »

FASTA65773,742
Isoform 17 [UniParc].

Checksum: FAACAE02C878443E
Show »

FASTA2,330256,502

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS PRO-817 AND ILE-2170.
[2]"The expression of migration stimulating factor, a potent oncofetal cytokine, is uniquely controlled by 3'-untranslated region-dependent nuclear sequestration of its precursor messenger RNA."
Kay R.A., Ellis I.R., Jones S.J., Perrier S., Florence M.M., Schor A.M., Schor S.L.
Cancer Res. 65:10742-10749(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), VARIANTS PRO-817 AND ILE-2170.
Tissue: Retinal pigment epithelium.
[4]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), VARIANTS LEU-15; PRO-817 AND ILE-2170.
Tissue: Aortic endothelium.
[5]"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 7; 8; 9; 10; 13; 14 AND 15), VARIANTS LEU-15; PRO-817 AND ILE-2170.
Tissue: Amygdala, Cervix, Endometrial tumor and Uterine endothelium.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), VARIANTS LEU-15; PRO-817 AND ILE-2170.
Tissue: Cerebellum.
[9]"Human fibronectin is synthesized as a pre-propolypeptide."
Gutman A., Yamada K.M., Kornblihtt A.R.
FEBS Lett. 207:145-148(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-38.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49, VARIANT LEU-15.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-2386 (ISOFORM 3), VARIANTS PRO-817 AND ILE-2170.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-290.
[13]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.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 309-608, COLLAGEN-BINDING.
[15]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 616-705.
[16]"Identification of novel fibronectin fragments detected specifically in juvenile urine."
Iida R., Yasuda T., Kishi K.
FEBS J. 274:3939-3947(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 723-911, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION AT ASN-877, VARIANT PRO-817.
Tissue: Urine.
[17]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 973-2386 (ISOFORM 3), VARIANT ILE-2170.
[18]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1232-1782 (ISOFORMS 7/15).
[19]"Transformed human cells produce a new fibronectin isoform by preferential alternative splicing of a previously unobserved exon."
Zardi L., Carnemolla B., Siri A., Petersen T.E., Paolella G., Sebastio G., Baralle F.E.
EMBO J. 6:2337-2342(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1234-1286 (ISOFORM 7).
[20]"Identification of a third region of cell-specific alternative splicing in human fibronectin mRNA."
Gutman A., Kornblihtt A.R.
Proc. Natl. Acad. Sci. U.S.A. 84:7179-7182(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1257-1365 (ISOFORM 11).
[21]"The cell attachment domain of fibronectin. Determination of the primary structure."
Pierschbacher M.D., Ruoslahti E., Sundelin J., Lind P., Peterson P.A.
J. Biol. Chem. 257:9593-9597(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1441-1548.
[22]"Molecular cloning and nucleotide sequence of a cDNA clone coding for the cell attachment domain in human fibronectin."
Oldberg A., Linney E., Ruoslahti E.
J. Biol. Chem. 258:10193-10196(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1448-1540.
[23]"Evolution of the fibronectin gene. Exon structure of cell attachment domain."
Oldberg A., Ruoslahti E.
J. Biol. Chem. 261:2113-2116(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1448-1540.
[24]"Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity."
Garcia-Pardo A., Rostagno A., Frangione B.
Biochem. J. 241:923-928(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1589-2058.
[25]"Human cellular fibronectin: comparison of the carboxyl-terminal portion with rat identifies primary structural domains separated by hypervariable regions."
Bernard M.P., Kolbe M., Weil D., Chu M.-L.
Biochemistry 24:2698-2704(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1594-2386 (ISOFORMS 1/11/15), VARIANT ILE-2170.
[26]"Human plasma fibronectin. Demonstration of structural differences between the A- and B-chains in the III CS region."
Tressel T., McCarthy J.B., Calaycay J., Lee T.D., Legesse K., Shively J.E., Pande H.
Biochem. J. 274:731-738(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1614-1623; 1730-1748; 1756-1759; 1803-1811; 1860-1923; 1930-1945; 1949-1972; 1982-1989; 1991-2003; 2020-2038; 2060-2131; 2150-2180; 2185-2205 AND 2231-2242, GLYCOSYLATION AT THR-2064 AND THR-2065, LACK OF GLYCOSYLATION AT ASN-2108, MASS SPECTROMETRY, VARIANT ILE-2170.
[27]"Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain."
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.
EMBO J. 3:221-226(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1624-1727 (ISOFORMS 8/9/10/12/13/14).
[28]"Human liver fibronectin complementary DNAs: identification of two different messenger RNAs possibly encoding the alpha and beta subunits of plasma fibronectin."
Sekiguchi K., Klos A.M., Kurachi K., Yoshitake S., Hakomori S.
Biochemistry 25:4936-4941(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1712-1739 (ISOFORMS 1/3/4/5/6/7/11/15).
[29]"Novel cartilage-specific splice variants of fibronectin."
Parker A.E., Boutell J., Carr A., Maciewicz R.A.
Osteoarthritis Cartilage 10:528-534(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1788-2386 (ISOFORMS 4; 5 AND 6), VARIANT ILE-2170.
Tissue: Cartilage.
[30]"Isolation and characterization of cDNA clones for human liver fibronectin."
Umezawa K., Kornblihtt A.R., Baralle F.E.
FEBS Lett. 186:31-34(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1948-2067 (ISOFORMS 1/8/10/11/15).
[31]"Donor and acceptor splice signals within an exon of the human fibronectin gene: a new type of differential splicing."
Vibe-Pedersen K., Magnusson S., Baralle F.E.
FEBS Lett. 207:287-291(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1992-2147.
[32]"Primary structure of human plasma fibronectin. Characterization of a 31,000-dalton fragment from the COOH-terminal region containing a free sulfhydryl group and a fibrin-binding site."
Garcia-Pardo A., Pearlstein E., Frangione B.
J. Biol. Chem. 260:10320-10325(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2071-2356 (ISOFORM 3), VARIANT ILE-2170.
[33]"Isolation and characterization of cDNA clones for human and bovine fibronectins."
Kornblihtt A.R., Vibe-Pedersen K., Baralle F.E.
Proc. Natl. Acad. Sci. U.S.A. 80:3218-3222(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2291-2386.
[34]"Tyrosine sulfation of proteins from the human hepatoma cell line HepG2."
Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.
Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[35]"Purification of a young age-related glycoprotein (Ugl-Y) from normal human urine."
Iida R., Yasuda T., Kishi K.
J. Biochem. 101:357-363(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF UGL-Y1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
[36]"Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin."
Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K., Argraves W.S.
J. Biol. Chem. 267:20120-20125(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBLN1.
[37]"Further characterization of the NH2-terminal fibrin-binding site on fibronectin."
Rostagno A., Williams M.J., Baron M., Campbell I.D., Gold L.I.
J. Biol. Chem. 269:31938-31945(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF FIBRIN-BINDING SITE 1.
[38]"Superfibronectin is a functionally distinct form of fibronectin."
Morla A., Zhang Z., Ruoslahti E.
Nature 367:193-196(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION OF ANASTELLIN.
[39]"Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin."
Sasaki T., Brakebusch C., Engel J., Timpl R.
EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LGALS3BP.
[40]"A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis."
Yi M., Ruoslahti E.
Proc. Natl. Acad. Sci. U.S.A. 98:620-624(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ANASTELLIN.
[41]"The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin."
Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R., Pihlajaniemi T.
J. Biol. Chem. 277:23092-23099(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COL13A1.
[42]"Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin."
Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.
Matrix Biol. 21:461-470(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COMP.
[43]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528, MASS SPECTROMETRY.
Tissue: Plasma.
[44]"Anastellin, a fragment of the first type III repeat of fibronectin, inhibits extracellular signal-regulated kinase and causes G(1) arrest in human microvessel endothelial cells."
Ambesi A., Klein R.M., Pumiglia K.M., McKeown-Longo P.J.
Cancer Res. 65:148-156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ANASTELLIN.
[45]"Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment."
Tajiri M., Yoshida S., Wada Y.
Glycobiology 15:1332-1340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-279; ASN-430; ASN-528; ASN-542; ASN-877; ASN-1007; ASN-1244 AND ASN-2108.
[46]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430; ASN-528; ASN-542; ASN-1007 AND ASN-1244, MASS SPECTROMETRY.
Tissue: Plasma.
[47]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[48]"A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG and follistatin."
Maguer-Satta V., Forissier S., Bartholin L., Martel S., Jeanpierre S., Bachelard E., Rimokh R.
Exp. Cell Res. 312:434-442(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FST3.
[49]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, MASS SPECTROMETRY.
Tissue: Liver.
[50]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-1007, MASS SPECTROMETRY.
Tissue: Liver.
[51]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-528; ASN-542 AND ASN-1007.
[52]"Regulation of p38 MAP kinase by anastellin is independent of anastellin's effect on matrix fibronectin."
You R., Klein R.M., Zheng M., McKeown-Longo P.J.
Matrix Biol. 28:101-109(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ANASTELLIN, MUTAGENESIS OF LEU-663 AND TYR-666.
[53]"1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin."
Baron M., Main A.L., Driscoll P.C., Mardon H.J., Boyd J., Campbell I.D.
Biochemistry 31:2068-2073(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1447-1540.
[54]"The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions."
Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D.
Cell 71:671-678(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1447-1540.
[55]"Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity."
Williams M.J., Phan I., Harvey T.S., Rostagno A., Gold L.I., Campbell I.D.
J. Mol. Biol. 235:1302-1311(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 183-275, DISULFIDE BONDS.
[56]"High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin."
Potts J.R., Phan I., Williams M.J., Campbell I.D.
Nat. Struct. Biol. 2:946-950(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 32-92.
[57]"Solution structure of the glycosylated second type 2 module of fibronectin."
Sticht H., Pickford A.R., Potts J.R., Campbell I.D.
J. Mol. Biol. 276:177-187(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 406-464.
[58]"NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis."
Fattorusso R., Pellecchia M., Viti F., Neri P., Neri D., Wuethrich K.
Structure 7:381-390(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF EXTRA ED-B DOMAIN FROM ISOFORM 7.
[59]"Solution structure of a pair of modules from the gelatin-binding domain of fibronectin."
Bocquier A.A., Potts J.R., Pickford A.R., Campbell I.D.
Structure 7:1451-1460(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 305-405.
[60]"The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding."
Pickford A.R., Smith S.P., Staunton D., Boyd J., Campbell I.D.
EMBO J. 20:1519-1529(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 305-464, GLYCOSYLATION AT ASN-430.
[61]"NMR structure of human fibronectin EDA."
Niimi T., Osawa M., Yamaji N., Yasunaga K., Sakashita H., Mase T., Tanaka A., Fujita S.
J. Biomol. NMR 21:281-284(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1631-1724.
[62]"Anastellin, an FN3 fragment with fibronectin polymerization activity, resembles amyloid fibril precursors."
Briknarova K., Aakerman M.E., Hoyt D.W., Ruoslahti E., Ely K.R.
J. Mol. Biol. 332:205-215(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 631-705, MUTAGENESIS OF TYR-641; ILE-642; LEU-663; TYR-666; LEU-681; ILE-682; SER-683; ILE-684; GLU-691; VAL-692; ARG-694; PHE-695; ASP-696 AND PHE-697.
[63]"Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper."
Schwarz-Linek U., Werner J.M., Pickford A.R., Gurusiddappa S., Kim J.H., Pilka E.S., Briggs J.A., Gough T.S., Hoeoek M., Campbell I.D., Potts J.R.
Nature 423:177-181(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 48-140 IN COMPLEX WITH A BACTERIAL FIBRONECTIN-BINDING PROTEIN.
[64]"Crystal structure of the tenth type III cell adhesion module of human fibronectin."
Dickinson C.D., Veerapandian B., Dai X.-P., Hamlin R.C., Xuong N.-H., Ruoslahti E., Ely K.R.
J. Mol. Biol. 236:1079-1092(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1447-1535.
[65]"2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region."
Leahy D.J., Aukhil I., Erickson H.P.
Cell 84:155-164(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1173-1540.
[66]"Crystal structure of a heparin- and integrin-binding segment of human fibronectin."
Sharma A., Askari J.A., Humphries M.J., Jones E.Y., Stuart D.I.
EMBO J. 18:1468-1479(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1721-1991.
[67]"Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates."
Gao M., Craig D., Lequin O., Campbell I.D., Vogel V., Schulten K.
Proc. Natl. Acad. Sci. U.S.A. 100:14784-14789(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 608-701.
[68]"Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis."
Vakonakis I., Staunton D., Rooney L.M., Campbell I.D.
EMBO J. 26:2575-2583(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 609-809.
[69]"The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin -- a tale with a twist."
Rudino-Pinera E., Ravelli R.B., Sheldrick G.M., Nanao M.H., Korostelev V.V., Werner J.M., Schwarz-Linek U., Potts J.R., Garman E.F.
J. Mol. Biol. 368:833-844(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 93-182, X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 93-182, DISULFIDE BONDS.
[70]"Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains."
Bingham R.J., Rudino-Pinera E., Meenan N.A.G., Schwarz-Linek U., Turkenburg J.P., Hoeoek M., Garman E.F., Potts J.R.
Proc. Natl. Acad. Sci. U.S.A. 105:12254-12258(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 93-275 IN COMPLEX WITH STAPHYLOCOCCUS AUREUS FNBA.
[71]"Solution structure of the 11th FN1 domain from human fibronectin 1."
RIKEN structural genomics initiative (RSGI)
Submitted (MAR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 2239-2299.
[72]"Identification and structural analysis of type I collagen sites in complex with fibronectin fragments."
Erat M.C., Slatter D.A., Lowe E.D., Millard C.J., Farndale R.W., Campbell I.D., Vakonakis I.
Proc. Natl. Acad. Sci. U.S.A. 106:4195-4200(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 516-608 IN COMPLEX WITH TYPE I COLLAGEN.
[73]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-940; PRO-1120 AND ASN-2380.
[74]"Mutations in FN1 cause glomerulopathy with fibronectin deposits."
Castelletti F., Donadelli R., Banterla F., Hildebrandt F., Zipfel P.F., Bresin E., Otto E., Skerka C., Renieri A., Todeschini M., Caprioli J., Caruso R.M., Artuso R., Remuzzi G., Noris M.
Proc. Natl. Acad. Sci. U.S.A. 105:2538-2543(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GFND2 CYS-973; ARG-1834 AND ARG-1883, VARIANTS LEU-15 AND VAL-1960, CHARACTERIZATION OF VARIANTS GFND2 ARG-1834 AND ARG-1883.
[75]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-2170, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Wikipedia

Fibronectin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
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.
PIRFNHU. A26460.
I52394.
S00848.
RefSeqNP_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.
XP_005246463.1. XM_005246406.1.
XP_005246470.1. XM_005246413.1.
XP_005246472.1. XM_005246415.1.
XP_005246474.1. XM_005246417.1.
UniGeneHs.203717.

3D structure databases

PDBe
RCSB PDB
PDBj
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-A1961-1966[»]
2GEEX-ray2.01A1266-1356[»]
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-ray3.00A305-515[»]
3R8QX-ray2.40A1721-1991[»]
3T1WX-ray2.40A1173-1448[»]
3ZRZX-ray1.70A/B93-182[»]
4GH7X-ray2.60B/D1173-1357[»]
4JE4X-ray2.31B1450-1486[»]
4JEGX-ray2.30B1450-1486[»]
ProteinModelPortalP02751.
SMRP02751. Positions 48-274, 297-606, 609-809, 1173-1540, 1631-1991, 2242-2299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108621. 718 interactions.
DIPDIP-29547N.
IntActP02751. 442 interactions.
MINTMINT-1779779.

Chemistry

BindingDBP02751.
ChEMBLCHEMBL3810.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP02751.
UniCarbKBP02751.

Polymorphism databases

DMDM300669710.

2D gel databases

DOSAC-COBS-2DPAGEP02751.

Proteomic databases

PaxDbP02751.
PRIDEP02751.

Protocols and materials databases

DNASU2335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323926; ENSP00000323534; ENSG00000115414.
ENST00000336916; ENSP00000338200; ENSG00000115414.
ENST00000345488; ENSP00000273049; ENSG00000115414.
ENST00000354785; ENSP00000346839; ENSG00000115414.
ENST00000356005; ENSP00000348285; ENSG00000115414.
ENST00000357009; ENSP00000349509; ENSG00000115414.
ENST00000357867; ENSP00000350534; ENSG00000115414.
ENST00000359671; ENSP00000352696; ENSG00000115414.
ENST00000421182; ENSP00000394423; ENSG00000115414.
ENST00000432072; ENSP00000399538; ENSG00000115414.
ENST00000443816; ENSP00000415018; ENSG00000115414.
ENST00000446046; ENSP00000410422; ENSG00000115414.
GeneID2335.
KEGGhsa:2335.
UCSCuc002vfh.3. human.

Organism-specific databases

CTD2335.
GeneCardsGC02M216225.
HGNCHGNC:3778. FN1.
HPACAB000126.
HPA027066.
MIM135600. gene.
601894. phenotype.
neXtProtNX_P02751.
Orphanet84090. Fibronectin glomerulopathy.
PharmGKBPA28194.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG005731.
KOK05717.
OMAIPGHLNS.
OrthoDBEOG7X9G60.
TreeFamTF329915.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02751.
BgeeP02751.
GenevestigatorP02751.

Family and domain databases

Gene3D2.10.10.10. 2 hits.
2.60.40.10. 16 hits.
InterProIPR000083. Fibronectin_type1.
IPR003961. Fibronectin_type3.
IPR000562. FN_type2_col-bd.
IPR013783. Ig-like_fold.
IPR013806. Kringle-like.
[Graphical view]
PfamPF00039. fn1. 12 hits.
PF00040. fn2. 2 hits.
PF00041. fn3. 16 hits.
[Graphical view]
SMARTSM00058. FN1. 12 hits.
SM00059. FN2. 2 hits.
SM00060. FN3. 16 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 10 hits.
SSF57440. SSF57440. 2 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSFN1. human.
EvolutionaryTraceP02751.
GeneWikiFibronectin.
GenomeRNAi2335.
NextBio35481280.
PROP02751.
SOURCESearch...

Entry information

Entry nameFINC_HUMAN
AccessionPrimary (citable) accession number: P02751
Secondary accession number(s): B7ZLF0 expand/collapse secondary AC list , E9PE77, E9PG29, O95609, O95610, Q14312, Q14325, Q14326, Q17RV7, Q564H7, Q585T2, Q59EH1, Q60FE4, Q68DP8, Q68DP9, Q68DT4, Q6LDP6, Q6MZS0, Q6MZU5, Q6N025, Q6N0A6, Q86T27, Q8IVI8, Q96KP7, Q96KP8, Q96KP9, Q9H1B8, Q9HAP3, Q9UMK2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 13, 2010
Last modified: February 19, 2014
This is version 193 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

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