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Entry version 256 (16 Oct 2019)
Sequence version 5 (16 Oct 2019)
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Protein

Fibronectin

Gene

FN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei663Important for superfibronectin formation1
Sitei666Important for superfibronectin formation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi907 – 1172Add BLAST266

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

SIGNOR Signaling Network Open Resource

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SIGNORi
P02751

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fibronectin
Short name:
FN
Alternative name(s):
Cold-insoluble globulin
Short name:
CIG
Cleaved into the following 4 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FN1
Synonyms:FN
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:3778 FN1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
135600 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P02751

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Glomerulopathy with fibronectin deposits 2 (GFND2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionGenetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant dbSNP:rs137854488EnsemblClinVar.1
Natural variantiVAR_0439191925W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854486EnsemblClinVar.1
Natural variantiVAR_0439201974L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854487EnsemblClinVar.1
Spondylometaphyseal dysplasia, corner fracture type (SMDCF)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDCF is characterized by flake-like, triangular, or curvilinear ossification centers at the edges of irregular metaphyses that simulate fractures. These corner fractures involve the distal tibia, the ulnar aspect of the distal radius, the proximal humerus, and the proximal femur. They represent irregular ossification at the growth plates and secondary ossification centers.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08052387C → F in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553669703EnsemblClinVar.1
Natural variantiVAR_080524123C → R in SMDCF. 1 PublicationCorresponds to variant dbSNP:rs1553667072EnsemblClinVar.1
Natural variantiVAR_080525225C → W in SMDCF. 1 Publication1
Natural variantiVAR_080526240Y → D in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553659131EnsemblClinVar.1
Natural variantiVAR_080527260C → G in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553658926EnsemblClinVar.1
Natural variantiVAR_080528809Missing in SMDCF; unknown pathological significance. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi641Y → A: Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683. 1 Publication1
Mutagenesisi642I → A: Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692. 1 Publication1
Mutagenesisi663L → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 K but abolishes polymerization activity; when associated with A-666. 2 Publications1
Mutagenesisi666Y → A: No effect on secondary structure nor on fibronectin binding nor on activation of p38 kinase but abolishes polymerization activity; when associated with A-663. 2 Publications1
Mutagenesisi681L → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683. 1 Publication1
Mutagenesisi682I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692. 1 Publication1
Mutagenesisi683S → A: Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681. 1 Publication1
Mutagenesisi684I → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692. 1 Publication1
Mutagenesisi691E → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696. 1 Publication1
Mutagenesisi692V → A: Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684. 1 Publication1
Mutagenesisi694R → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696. 1 Publication1
Mutagenesisi695F → A: Loss of ability to form fibronectin aggregates; when associated with A-697. 1 Publication1
Mutagenesisi696D → A: Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694. 1 Publication1
Mutagenesisi697F → A: Loss of ability to form fibronectin aggregates; when associated with A-695. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNET

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DisGeNETi
2335

MalaCards human disease database

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MalaCardsi
FN1
MIMi184255 phenotype
601894 phenotype

Open Targets

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OpenTargetsi
ENSG00000115414

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
84090 Fibronectin glomerulopathy
93315 Spondylometaphyseal dysplasia, 'corner fracture' type

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28194

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P02751

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3810

Drug and drug target database

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DrugBanki
DB06245 Lanoteplase
DB08888 Ocriplasmin
DB01593 Zinc
DB14487 Zinc acetate
DB14533 Zinc chloride

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FN1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
300669710

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 311 PublicationAdd BLAST31
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001923532 – 2477FibronectinAdd BLAST2446
ChainiPRO_0000390479627 – 702AnastellinAdd BLAST76
ChainiPRO_0000300249723 – 911Ugl-Y1Add BLAST189
ChainiPRO_0000300250723 – 903Ugl-Y2Add BLAST181
ChainiPRO_0000300251723 – ?Ugl-Y3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei32Pyrrolidone carboxylic acid1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki34Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
Cross-linki47Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi52 ↔ 78
Disulfide bondi76 ↔ 87
Disulfide bondi97 ↔ 125
Disulfide bondi123 ↔ 135
Disulfide bondi141 ↔ 169
Disulfide bondi167 ↔ 179
Disulfide bondi186 ↔ 215
Disulfide bondi213 ↔ 225
Disulfide bondi231 ↔ 260
Disulfide bondi258 ↔ 270
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi279O-linked (GalNAc...) threonine1 Publication1
Disulfide bondi308 ↔ 335
Disulfide bondi333 ↔ 342
Disulfide bondi360 ↔ 386
Disulfide bondi374 ↔ 401
Disulfide bondi420 ↔ 446
Glycosylationi430N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi434 ↔ 461
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...) (complex) asparagine5 Publications1
Glycosylationi542N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei876SulfotyrosineSequence analysis1
Glycosylationi877N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei881SulfotyrosineSequence analysis1
Glycosylationi1007N-linked (GlcNAc...) (complex) asparagine4 Publications1
Glycosylationi1244N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi2199N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2297 ↔ 2326By similarity
Disulfide bondi2324 ↔ 2336By similarity
Disulfide bondi2342 ↔ 2369By similarity
Disulfide bondi2367 ↔ 2379By similarity
Disulfide bondi2386 ↔ 2410By similarity
Disulfide bondi2408 ↔ 2424By similarity
Modified residuei2454PhosphothreonineCombined sources1
Disulfide bondi2458Interchain (with C-2462)
Disulfide bondi2462Interchain (with C-2458)
Modified residuei2475Phosphoserine; by FAM20CCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sulfated.1 Publication
It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated.9 Publications
Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
Phosphorylated by FAM20C in the extracellular medium.1 Publication
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.By similarity

Keywords - PTMi

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

Proteomic databases

The CPTAC Assay portal

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CPTACi
non-CPTAC-1122
non-CPTAC-2666

Encyclopedia of Proteome Dynamics

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EPDi
P02751

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P02751

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P02751

MaxQB - The MaxQuant DataBase

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MaxQBi
P02751

PeptideAtlas

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PeptideAtlasi
P02751

PRoteomics IDEntifications database

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PRIDEi
P02751

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
19829
20230
51567 [P02751-1]
51568 [P02751-10]
51569 [P02751-11]
51570 [P02751-12]
51571 [P02751-13]
51572 [P02751-14]
51573 [P02751-15]
51574 [P02751-2]
51575 [P02751-3]
51576 [P02751-4]
51577 [P02751-5]
51578 [P02751-6]
51579 [P02751-7]
51580 [P02751-8]
51581 [P02751-9]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P02751

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P02751

GlyConnect protein glycosylation platform

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GlyConnecti
161

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02751

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P02751

SwissPalm database of S-palmitoylation events

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SwissPalmi
P02751

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P02751

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). 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 (PubMed:17614963).3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed between 12 and 19 weeks post-conception (WPC) in Bruch's membrane, with expression in the choroid evident from 14 WPC onwards (at protein level) (PubMed:29777959). Expressed in the inner limiting membrane at 17 WPC (at protein level) (PubMed:29777959). Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age (PubMed:17614963, PubMed:3584091).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000115414 Expressed in 242 organ(s), highest expression level in tendon

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02751 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02751 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB000126
HPA027066

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers.

Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1.

Interacts with FBLN7 (By similarity).

Interacts with COMP (PubMed:12225811).

Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity).

Interacts with FST3 and MYOC.

By similarity9 Publications

(Microbial infection) Interacts with S.aureus FnbA.

1 Publication

(Microbial infection) Interacts with M.bovis FbpB via the collagen-binding region.

1 Publication

(Microbial infection) Interacts with recombinant S.pneumoniae PavA (rqcH).

1 Publication

(Microbial infection) Interacts with recombinant S.suis FbpS (rqcH) via fibronectin's N-terminal 30 kDa region.

1 Publication

(Microbial infection) Interacts with fibronectin-binding proteins from other Mycobacteria.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108621, 752 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02751

Database of interacting proteins

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DIPi
DIP-29547N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P02751

Protein interaction database and analysis system

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IntActi
P02751, 525 interactors

Molecular INTeraction database

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MINTi
P02751

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P02751

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P02751

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P02751

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini50 – 90Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST41
Domaini95 – 138Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST44
Domaini139 – 182Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST44
Domaini184 – 228Fibronectin type-I 4PROSITE-ProRule annotationAdd BLAST45
Domaini229 – 273Fibronectin type-I 5PROSITE-ProRule annotationAdd BLAST45
Domaini306 – 345Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST40
Domaini355 – 403Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini415 – 463Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini468 – 511Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST44
Domaini516 – 558Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST43
Domaini559 – 602Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST44
Domaini610 – 702Fibronectin type-III 1Add BLAST93
Domaini722 – 812Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST91
Domaini813 – 904Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini909 – 998Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST90
Domaini999 – 1088Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST90
Domaini1089 – 1175Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST87
Domaini1176 – 1270Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST95
Domaini1271 – 1359Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST89
Domaini1360 – 1452Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST93
Domaini1453 – 1540Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST88
Domaini1541 – 1634Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST94
Domaini1635 – 1726Fibronectin type-III 12; extra domainPROSITE-ProRule annotationAdd BLAST92
Domaini1727 – 1814Fibronectin type-III 13PROSITE-ProRule annotationAdd BLAST88
Domaini1815 – 1908Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST94
Domaini1909 – 1995Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST87
Domaini1996 – 2086Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST91
Domaini2194 – 2288Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST95
Domaini2295 – 2339Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST45
Domaini2340 – 2382Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST43
Domaini2384 – 2427Fibronectin type-I 12PROSITE-ProRule annotationAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni52 – 272Fibrin- and heparin-binding 1Add BLAST221
Regioni308 – 608Collagen-bindingAdd BLAST301
Regioni464 – 477Critical for collagen bindingAdd BLAST14
Regioni1358 – 1631Cell-attachmentAdd BLAST274
Regioni1812 – 2082Heparin-binding 2Add BLAST271
Regioni1904 – 2082Binds to FBLN1Add BLAST179
Regioni2083 – 2193Connecting strand 3 (CS-3) (V region)Add BLAST111
Regioni2297 – 2428Fibrin-binding 2Add BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1615 – 1617Cell attachment site3

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155126

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234344

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02751

KEGG Orthology (KO)

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KOi
K05717

Identification of Orthologs from Complete Genome Data

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OMAi
YVIKIVA

Database of Orthologous Groups

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OrthoDBi
6580at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P02751

TreeFam database of animal gene trees

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TreeFami
TF329915

Family and domain databases

Conserved Domains Database

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CDDi
cd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 16 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.10.10.10, 2 hits
2.60.40.10, 16 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000083 Fibronectin_type1
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR013783 Ig-like_fold
IPR013806 Kringle-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00039 fn1, 12 hits
PF00040 fn2, 2 hits
PF00041 fn3, 16 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 16 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 10 hits
SSF57440 SSF57440, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00022 EGF_1, 2 hits
PS01253 FN1_1, 12 hits
PS51091 FN1_2, 12 hits
PS00023 FN2_1, 2 hits
PS51092 FN2_2, 2 hits
PS50853 FN3, 16 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (17+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 17 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 15 (identifier: P02751-15) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLRGPGPGLL LLAVQCLGTA VPSTGASKSK RQAQQMVQPQ SPVAVSQSKP
60 70 80 90 100
GCYDNGKHYQ INQQWERTYL GNALVCTCYG GSRGFNCESK PEAEETCFDK
110 120 130 140 150
YTGNTYRVGD TYERPKDSMI WDCTCIGAGR GRISCTIANR CHEGGQSYKI
160 170 180 190 200
GDTWRRPHET GGYMLECVCL GNGKGEWTCK PIAEKCFDHA AGTSYVVGET
210 220 230 240 250
WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY RIGDTWSKKD
260 270 280 290 300
NRGNLLQCIC TGNGRGEWKC ERHTSVQTTS SGSGPFTDVR AAVYQPQPHP
310 320 330 340 350
QPPPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHTVLVQT RGGNSNGALC HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDM GHMMRCTCVG
510 520 530 540 550
NGRGEWTCIA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPVDQ CQDSETGTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPSSSG PVEVFITETP SQPNSHPIQW NAPQPSHISK YILRWRPKNS
660 670 680 690 700
VGRWKEATIP GHLNSYTIKG LKPGVVYEGQ LISIQQYGHQ EVTRFDFTTT
710 720 730 740 750
STSTPVTSNT VTGETTPFSP LVATSESVTE ITASSFVVSW VSASDTVSGF
760 770 780 790 800
RVEYELSEEG DEPQYLDLPS TATSVNIPDL LPGRKYIVNV YQISEDGEQS
810 820 830 840 850
LILSTSQTTA PDAPPDTTVD QVDDTSIVVR WSRPQAPITG YRIVYSPSVE
860 870 880 890 900
GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVVIQQETTG
910 920 930 940 950
TPRSDTVPSP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH
960 970 980 990 1000
GQRLPISRNT FAEVTGLSPG VTYYFKVFAV SHGRESKPLT AQQTTKLDAP
1010 1020 1030 1040 1050
TNLQFVNETD STVLVRWTPP RAQITGYRLT VGLTRRGQPR QYNVGPSVSK
1060 1070 1080 1090 1100
YPLRNLQPAS EYTVSLVAIK GNQESPKATG VFTTLQPGSS IPPYNTEVTE
1110 1120 1130 1140 1150
TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV SGLTPGVEYV
1160 1170 1180 1190 1200
YTIQVLRDGQ ERDAPIVNKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
1210 1220 1230 1240 1250
PDITGYRITT TPTNGQQGNS LEEVVHADQS SCTFDNLSPG LEYNVSVYTV
1260 1270 1280 1290 1300
KDDKESVPIS DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI
1310 1320 1330 1340 1350
TVVAAGEGIP IFEDFVDSSV GYYTVTGLEP GIDYDISVIT LINGGESAPT
1360 1370 1380 1390 1400
TLTQQTAVPP PTDLRFTNIG PDTMRVTWAP PPSIDLTNFL VRYSPVKNEE
1410 1420 1430 1440 1450
DVAELSISPS DNAVVLTNLL PGTEYVVSVS SVYEQHESTP LRGRQKTGLD
1460 1470 1480 1490 1500
SPTGIDFSDI TANSFTVHWI APRATITGYR IRHHPEHFSG RPREDRVPHS
1510 1520 1530 1540 1550
RNSITLTNLT PGTEYVVSIV ALNGREESPL LIGQQSTVSD VPRDLEVVAA
1560 1570 1580 1590 1600
TPTSLLISWD APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK
1610 1620 1630 1640 1650
PGVDYTITVY AVTGRGDSPA SSKPISINYR TEIDKPSQMQ VTDVQDNSIS
1660 1670 1680 1690 1700
VKWLPSSSPV TGYRVTTTPK NGPGPTKTKT AGPDQTEMTI EGLQPTVEYV
1710 1720 1730 1740 1750
VSVYAQNPSG ESQPLVQTAV TNIDRPKGLA FTDVDVDSIK IAWESPQGQV
1760 1770 1780 1790 1800
SRYRVTYSSP EDGIHELFPA PDGEEDTAEL QGLRPGSEYT VSVVALHDDM
1810 1820 1830 1840 1850
ESQPLIGTQS TAIPAPTDLK FTQVTPTSLS AQWTPPNVQL TGYRVRVTPK
1860 1870 1880 1890 1900
EKTGPMKEIN LAPDSSSVVV SGLMVATKYE VSVYALKDTL TSRPAQGVVT
1910 1920 1930 1940 1950
TLENVSPPRR ARVTDATETT ITISWRTKTE TITGFQVDAV PANGQTPIQR
1960 1970 1980 1990 2000
TIKPDVRSYT ITGLQPGTDY KIYLYTLNDN ARSSPVVIDA STAIDAPSNL
2010 2020 2030 2040 2050
RFLATTPNSL LVSWQPPRAR ITGYIIKYEK PGSPPREVVP RPRPGVTEAT
2060 2070 2080 2090 2100
ITGLEPGTEY TIYVIALKNN QKSEPLIGRK KTDELPQLVT LPHPNLHGPE
2110 2120 2130 2140 2150
ILDVPSTVQK TPFVTHPGYD TGNGIQLPGT SGQQPSVGQQ MIFEEHGFRR
2160 2170 2180 2190 2200
TTPPTTATPI RHRPRPYPPN VGEEIQIGHI PREDVDYHLY PHGPGLNPNA
2210 2220 2230 2240 2250
STGQEALSQT TISWAPFQDT SEYIISCHPV GTDEEPLQFR VPGTSTSATL
2260 2270 2280 2290 2300
TGLTRGATYN VIVEALKDQQ RHKVREEVVT VGNSVNEGLN QPTDDSCFDP
2310 2320 2330 2340 2350
YTVSHYAVGD EWERMSESGF KLLCQCLGFG SGHFRCDSSR WCHDNGVNYK
2360 2370 2380 2390 2400
IGEKWDRQGE NGQMMSCTCL GNGKGEFKCD PHEATCYDDG KTYHVGEQWQ
2410 2420 2430 2440 2450
KEYLGAICSC TCFGGQRGWR CDNCRRPGGE PSPEGTTGQS YNQYSQRYHQ
2460 2470
RTNTNVNCPI ECFMPLDVQA DREDSRE
Note: No experimental confirmation available.
Length:2,477
Mass (Da):272,320
Last modified:October 16, 2019 - v5
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6C436A7A5FEE6DEB
GO
Isoform 1 (identifier: P02751-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.

Show »
Length:2,386
Mass (Da):262,625
Checksum:i5F7EDB9700335098
GO
Isoform 2 (identifier: P02751-2) [UniParc]FASTAAdd to basket
Also known as: MSF-FN70, Migration stimulation factor FN70

The sequence of this isoform differs from the canonical sequence as follows:
     368-386: GRTFYSCTTEGRQDGHLWC → DRTD
     648-657: KNSVGRWKEA → VSIPPRNLGY
     658-2477: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     2173-2203: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     2081-2201: KTDELPQLVT...HGPGLNPNAS → K
     2239-2242: FRVP → STKA
     2243-2477: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     2081-2201: KTDELPQLVT...HGPGLNPNAS → K
     2285-2339: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     2081-2284: KTDELPQLVT...REEVVTVGNS → KT

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

The sequence of this isoform differs from the canonical sequence as follows:
     2173-2203: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI
     2081-2106: KTDELPQLVTLPHPNLHGPEILDVPS → K
     2173-2203: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI
     2081-2201: KTDELPQLVT...HGPGLNPNAS → K

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

The sequence of this isoform differs from the canonical sequence as follows:
     1367-1457: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1256-1578: Missing.
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI
     2081-2106: KTDELPQLVTLPHPNLHGPEILDVPS → K
     2173-2203: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI
     2081-2201: KTDELPQLVT...HGPGLNPNAS → K

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     1722-1813: NIDRPKGLAF...PLIGTQSTAI → TI
     2173-2203: Missing.

Show »
Length:2,265
Mass (Da):249,402
Checksum:iAC05A50EA66B26C5
GO
Isoform 16 (identifier: P02751-16) [UniParc]FASTAAdd to basket
Also known as: Migration stimulation factor, MSF

The sequence of this isoform differs from the canonical sequence as follows:
     648-657: KNSVGRWKEA → VSIPPRNLGY
     658-2477: Missing.

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

The sequence of this isoform differs from the canonical sequence as follows:
     1266-1356: Missing.
     2081-2106: KTDELPQLVTLPHPNLHGPEILDVPS → K
     2173-2203: Missing.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

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

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y4K8H0Y4K8_HUMAN
Fibronectin
FN1
241Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA52463 differs from that shown. Reason: Erroneous translation.Curated
The sequence AAX76513 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAD93077 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAD91166 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAD97964 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAD97965 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAD97984 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAE45847 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
The sequence CAH18136 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti32Q → R in CAH18171 (PubMed:17974005).Curated1
Sequence conflicti48S → C AA sequence (PubMed:6630202).Curated1
Sequence conflicti52C → S AA sequence (PubMed:6630202).Curated1
Sequence conflicti69Y → N in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti73A → V in CAA26536 (PubMed:2992939).Curated1
Sequence conflicti126I → V in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti199E → G in CAD91166 (PubMed:17974005).Curated1
Sequence conflicti247S → R in CAD59389 (PubMed:11737888).Curated1
Sequence conflicti247S → R in CAH60958 (PubMed:16322219).Curated1
Sequence conflicti260C → R in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti289V → A in CAE45847 (PubMed:17974005).Curated1
Sequence conflicti355S → L in CAA26536 (PubMed:2992939).Curated1
Sequence conflicti355S → L in AAD00015 (Ref. 13) Curated1
Sequence conflicti357G → E in CAD97984 (PubMed:17974005).Curated1
Sequence conflicti375T → A in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti411R → Q in CAA26536 (PubMed:2992939).Curated1
Sequence conflicti411R → Q in AAD00015 (Ref. 13) Curated1
Sequence conflicti518C → R in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti552R → K in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti552R → K in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti580V → A in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti678E → Q AA sequence (PubMed:3900070).Curated1
Sequence conflicti704 – 705TP → PT AA sequence (PubMed:3900070).Curated2
Sequence conflicti980V → L in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti1030T → A in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1048V → D in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1048V → D in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1134D → G in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1137S → N in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1137S → N in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1152T → I in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1222E → G in CAD97791 (PubMed:17974005).Curated1
Sequence conflicti1226H → Q in CAE45932 (PubMed:17974005).Curated1
Sequence conflicti1646D → G in CAE45714 (PubMed:17974005).Curated1
Sequence conflicti1692G → S in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti1692G → S in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti1713Q → E AA sequence (PubMed:2012601).Curated1
Sequence conflicti1806 – 1812IGTQSTA → VQTAVTT in AAA52463 (PubMed:3021206).Curated7
Sequence conflicti1817T → A in CAE45847 (PubMed:17974005).Curated1
Sequence conflicti1846R → W in CAH18136 (PubMed:17974005).Curated1
Sequence conflicti1859I → V in CAB52436 (PubMed:3375063).Curated1
Sequence conflicti1874M → T in CAE45932 (PubMed:17974005).Curated1
Sequence conflicti2018R → C in AAD00014 (Ref. 13) Curated1
Sequence conflicti2025I → V in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti2083D → G in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2083D → G in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2114V → A in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2114V → A in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2118G → R in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2118G → R in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2342C → R in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti2403Y → N in CAD97965 (PubMed:17974005).Curated1
Sequence conflicti2403Y → N in CAD97964 (PubMed:17974005).Curated1
Sequence conflicti2432S → T in CAE45714 (PubMed:17974005).Curated1
Sequence conflicti2432S → T in CAH18171 (PubMed:17974005).Curated1
Sequence conflicti2432S → T in CAH18172 (PubMed:17974005).Curated1
Sequence conflicti2432S → T in CAE45958 (PubMed:17974005).Curated1
Sequence conflicti2458C → Y in CAE45932 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04391715Q → L5 PublicationsCorresponds to variant dbSNP:rs1250259Ensembl.1
Natural variantiVAR_08052387C → F in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553669703EnsemblClinVar.1
Natural variantiVAR_080524123C → R in SMDCF. 1 PublicationCorresponds to variant dbSNP:rs1553667072EnsemblClinVar.1
Natural variantiVAR_080525225C → W in SMDCF. 1 Publication1
Natural variantiVAR_080526240Y → D in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553659131EnsemblClinVar.1
Natural variantiVAR_080527260C → G in SMDCF; the mutant is not secreted. 1 PublicationCorresponds to variant dbSNP:rs1553658926EnsemblClinVar.1
Natural variantiVAR_080528809Missing in SMDCF; unknown pathological significance. 1 Publication1
Natural variantiVAR_059529817T → P6 PublicationsCorresponds to variant dbSNP:rs2577301Ensembl.1
Natural variantiVAR_036018940D → N in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs752106647Ensembl.1
Natural variantiVAR_043918973Y → C in GFND2. 1 PublicationCorresponds to variant dbSNP:rs137854488EnsemblClinVar.1
Natural variantiVAR_0360191120R → P in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0565761558S → R. Corresponds to variant dbSNP:rs11687611Ensembl.1
Natural variantiVAR_0439191925W → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854486EnsemblClinVar.1
Natural variantiVAR_0439201974L → R in GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation. 1 PublicationCorresponds to variant dbSNP:rs137854487EnsemblClinVar.1
Natural variantiVAR_0439212051I → V1 PublicationCorresponds to variant dbSNP:rs1250209Ensembl.1
Natural variantiVAR_0565772212I → V. Corresponds to variant dbSNP:rs17449032Ensembl.1
Natural variantiVAR_0614862261V → ICombined sources10 PublicationsCorresponds to variant dbSNP:rs1250209Ensembl.1
Natural variantiVAR_0360202471D → N in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1373375768Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_060343368 – 386GRTFY…GHLWC → DRTD in isoform 2. Add BLAST19
Alternative sequenceiVSP_060344648 – 657KNSVGRWKEA → VSIPPRNLGY in isoform 2 and isoform 16. 10
Alternative sequenceiVSP_060345658 – 2477Missing in isoform 2 and isoform 16. Add BLAST1820
Alternative sequenceiVSP_0603461256 – 1578Missing in isoform 12. Add BLAST323
Alternative sequenceiVSP_0603471266 – 1356Missing in isoform 1, isoform 3, isoform 4, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10, isoform 14 and isoform 17. Add BLAST91
Alternative sequenceiVSP_0603481367 – 1457Missing in isoform 11. Add BLAST91
Alternative sequenceiVSP_0603491722 – 1813NIDRP…QSTAI → TI in isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14. Add BLAST92
Alternative sequenceiVSP_0603502081 – 2284KTDEL…TVGNS → KT in isoform 6. Add BLAST204
Alternative sequenceiVSP_0603512081 – 2201KTDEL…NPNAS → K in isoform 4, isoform 5, isoform 10 and isoform 13. Add BLAST121
Alternative sequenceiVSP_0603522081 – 2106KTDEL…LDVPS → K in isoform 9, isoform 12 and isoform 17. Add BLAST26
Alternative sequenceiVSP_0603532173 – 2203Missing in isoform 3, isoform 7, isoform 9, isoform 12, isoform 14 and isoform 17. Add BLAST31
Alternative sequenceiVSP_0603542239 – 2242FRVP → STKA in isoform 4. 4
Alternative sequenceiVSP_0603552243 – 2477Missing in isoform 4. Add BLAST235
Alternative sequenceiVSP_0603562285 – 2339Missing in isoform 5. Add BLAST55

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ276395 mRNA Translation: CAC20427.1
AJ535086 mRNA Translation: CAD59389.1
AJ849445 mRNA Translation: CAH60958.1
AB191261 mRNA Translation: BAD52437.1
AB209840 mRNA Translation: BAD93077.1 Different initiation.
AL832202 mRNA Translation: CAD91166.1 Different initiation.
BX537590 mRNA Translation: CAD97791.1
BX538017 mRNA Translation: CAD97964.1 Different initiation.
BX538018 mRNA Translation: CAD97965.1 Different initiation.
BX538045 mRNA Translation: CAD97984.1 Different initiation.
BX640608 mRNA Translation: CAE45714.1
BX640731 mRNA Translation: CAE45847.1 Different initiation.
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 Translation: AAY24063.1
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
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 Sequence problems.
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.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2399.1 [P02751-3]
CCDS2400.1 [P02751-10]
CCDS42813.1 [P02751-8]
CCDS42814.1 [P02751-15]
CCDS46510.1 [P02751-17]
CCDS46512.1 [P02751-16]
CCDS77522.1 [P02751-9]
CCDS77523.1 [P02751-14]
CCDS77525.1 [P02751-13]
CCDS77526.1 [P02751-7]

Protein sequence database of the Protein Information Resource

More...
PIRi
A26460 FNHU
I52394
S00848

NCBI Reference Sequences

More...
RefSeqi
NP_001293058.1, NM_001306129.1
NP_001293059.1, NM_001306130.1
NP_001293060.1, NM_001306131.1
NP_001293061.1, NM_001306132.1
NP_002017.1, NM_002026.3
NP_473375.2, NM_054034.2 [P02751-16]
NP_997639.1, NM_212474.2
NP_997641.1, NM_212476.2
NP_997643.1, NM_212478.2
NP_997647.1, NM_212482.2
XP_005246463.1, XM_005246406.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2335

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2335

UCSC genome browser

More...
UCSCi
uc002vfa.4 human [P02751-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Fibronectin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276395 mRNA Translation: CAC20427.1
AJ535086 mRNA Translation: CAD59389.1
AJ849445 mRNA Translation: CAH60958.1
AB191261 mRNA Translation: BAD52437.1
AB209840 mRNA Translation: BAD93077.1 Different initiation.
AL832202 mRNA Translation: CAD91166.1 Different initiation.
BX537590 mRNA Translation: CAD97791.1
BX538017 mRNA Translation: CAD97964.1 Different initiation.
BX538018 mRNA Translation: CAD97965.1 Different initiation.
BX538045 mRNA Translation: CAD97984.1 Different initiation.
BX640608 mRNA Translation: CAE45714.1
BX640731 mRNA Translation: CAE45847.1 Different initiation.
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 Translation: AAY24063.1
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
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 Sequence problems.
AJ320525 mRNA Translation: CAC86914.1
AJ320526 mRNA Translation: CAC86915.1
AJ320527 mRNA Translation: CAC86916.1
M27589 mRNA Translation: AAA52465.1
X04530 Genomic DNA No translation available.
CCDSiCCDS2399.1 [P02751-3]
CCDS2400.1 [P02751-10]
CCDS42813.1 [P02751-8]
CCDS42814.1 [P02751-15]
CCDS46510.1 [P02751-17]
CCDS46512.1 [P02751-16]
CCDS77522.1 [P02751-9]
CCDS77523.1 [P02751-14]
CCDS77525.1 [P02751-13]
CCDS77526.1 [P02751-7]
PIRiA26460 FNHU
I52394
S00848
RefSeqiNP_001293058.1, NM_001306129.1
NP_001293059.1, NM_001306130.1
NP_001293060.1, NM_001306131.1
NP_001293061.1, NM_001306132.1
NP_002017.1, NM_002026.3
NP_473375.2, NM_054034.2 [P02751-16]
NP_997639.1, NM_212474.2
NP_997641.1, NM_212476.2
NP_997643.1, NM_212478.2
NP_997647.1, NM_212482.2
XP_005246463.1, XM_005246406.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E88NMR-A305-464[»]
1E8BNMR-A305-464[»]
1FBRNMR-A183-275[»]
1FNAX-ray1.80A1543-1633[»]
1FNFX-ray2.00A1173-1265[»]
A1357-1631[»]
1FNHX-ray2.80A1812-2082[»]
1J8KNMR-A1722-1815[»]
1O9ANMR-A48-140[»]
1OWWNMR-A608-701[»]
1Q38NMR-A631-705[»]
1QGBNMR-A48-140[»]
1QO6NMR-A305-405[»]
1TTFNMR-A1538-1631[»]
1TTGNMR-A1538-1631[»]
2CG6X-ray1.55A93-182[»]
2CG7X-ray1.20A93-182[»]
2CK2X-ray2.00A/B1538-1633[»]
2CKUNMR-A93-182[»]
2EC3NMR-A2330-2390[»]
2FN2NMR-A406-464[»]
2FNBNMR-A1266-1356[»]
2GEEX-ray2.01A1266-1447[»]
2H41NMR-A721-809[»]
2H45NMR-A721-809[»]
2HA1NMR-A609-809[»]
2MNUNMR-A907-995[»]
2N1KNMR-A808-905[»]
2OCFX-ray2.95D1539-1631[»]
2RKYX-ray1.80A/C183-275[»]
2RKZX-ray2.00A/B/C/D/E/F93-182[»]
2RL0X-ray2.00A/B/D/F/I/K184-272[»]
3CALX-ray1.70A/C93-182[»]
3EJHX-ray2.10A/B516-608[»]
3GXEX-ray2.60A/B516-608[»]
3M7PX-ray2.50A297-604[»]
3MQLX-ray3.00A308-515[»]
3R8QX-ray2.40A1812-2082[»]
3T1WX-ray2.40A1173-1539[»]
3ZRZX-ray1.70A/B93-182[»]
4GH7X-ray2.60B/D1173-1447[»]
4JE4X-ray2.31B1539-1631[»]
4JEGX-ray2.30B1539-1631[»]
4LXOX-ray1.42A/B1448-1631[»]
4MMXX-ray3.32C1539-1631[»]
4MMYX-ray3.18C1539-1631[»]
4MMZX-ray3.10C1539-1629[»]
4PZ5X-ray1.96A93-182[»]
5DC0X-ray2.23A1540-1631[»]
5DC4X-ray1.48B1539-1631[»]
5DC9X-ray1.56B1537-1631[»]
5DFTX-ray2.50A/B/C/D/E/F/G/H/I/J1638-1726[»]
5J6ZNMR-A806-834[»]
B631-705[»]
5J7CX-ray2.54C/D1540-1631[»]
5M0ANMR-A2199-2284[»]
5N47X-ray3.00B1267-1448[»]
D/F1173-1448[»]
5N48X-ray1.60B/D907-995[»]
6HNFNMR-A1995-2082[»]
SMRiP02751
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108621, 752 interactors
CORUMiP02751
DIPiDIP-29547N
ELMiP02751
IntActiP02751, 525 interactors
MINTiP02751

Chemistry databases

BindingDBiP02751
ChEMBLiCHEMBL3810
DrugBankiDB06245 Lanoteplase
DB08888 Ocriplasmin
DB01593 Zinc
DB14487 Zinc acetate
DB14533 Zinc chloride

PTM databases

CarbonylDBiP02751
GlyConnecti161
iPTMnetiP02751
PhosphoSitePlusiP02751
SwissPalmiP02751
UniCarbKBiP02751

Polymorphism and mutation databases

BioMutaiFN1
DMDMi300669710

2D gel databases

DOSAC-COBS-2DPAGEiP02751

Proteomic databases

CPTACinon-CPTAC-1122
non-CPTAC-2666
EPDiP02751
jPOSTiP02751
MassIVEiP02751
MaxQBiP02751
PeptideAtlasiP02751
PRIDEiP02751
ProteomicsDBi19829
20230
51567 [P02751-1]
51568 [P02751-10]
51569 [P02751-11]
51570 [P02751-12]
51571 [P02751-13]
51572 [P02751-14]
51573 [P02751-15]
51574 [P02751-2]
51575 [P02751-3]
51576 [P02751-4]
51577 [P02751-5]
51578 [P02751-6]
51579 [P02751-7]
51580 [P02751-8]
51581 [P02751-9]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P02751

The DNASU plasmid repository

More...
DNASUi
2335

Genome annotation databases

EnsembliENST00000323926; ENSP00000323534; ENSG00000115414 [P02751-7]
ENST00000336916; ENSP00000338200; ENSG00000115414 [P02751-3]
ENST00000354785; ENSP00000346839; ENSG00000115414 [P02751-15]
ENST00000356005; ENSP00000348285; ENSG00000115414 [P02751-8]
ENST00000357867; ENSP00000350534; ENSG00000115414 [P02751-10]
ENST00000359671; ENSP00000352696; ENSG00000115414 [P02751-1]
ENST00000421182; ENSP00000394423; ENSG00000115414 [P02751-9]
ENST00000426059; ENSP00000398907; ENSG00000115414 [P02751-16]
ENST00000432072; ENSP00000399538; ENSG00000115414 [P02751-13]
ENST00000443816; ENSP00000415018; ENSG00000115414 [P02751-14]
ENST00000446046; ENSP00000410422; ENSG00000115414 [P02751-17]
GeneIDi2335
KEGGihsa:2335
UCSCiuc002vfa.4 human [P02751-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2335
DisGeNETi2335

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FN1
HGNCiHGNC:3778 FN1
HPAiCAB000126
HPA027066
MalaCardsiFN1
MIMi135600 gene
184255 phenotype
601894 phenotype
neXtProtiNX_P02751
OpenTargetsiENSG00000115414
Orphaneti84090 Fibronectin glomerulopathy
93315 Spondylometaphyseal dysplasia, 'corner fracture' type
PharmGKBiPA28194

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

GeneTreeiENSGT00940000155126
HOGENOMiHOG000234344
InParanoidiP02751
KOiK05717
OMAiYVIKIVA
OrthoDBi6580at2759
PhylomeDBiP02751
TreeFamiTF329915

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
FN1 human
EvolutionaryTraceiP02751

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Fibronectin

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2335
PharosiP02751

Protein Ontology

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PROi
PR:P02751

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

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

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 16 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 16 hits
InterProiView protein in InterPro
IPR000083 Fibronectin_type1
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR013783 Ig-like_fold
IPR013806 Kringle-like
PfamiView protein in Pfam
PF00039 fn1, 12 hits
PF00040 fn2, 2 hits
PF00041 fn3, 16 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 16 hits
SUPFAMiSSF49265 SSF49265, 10 hits
SSF57440 SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS01253 FN1_1, 12 hits
PS51091 FN1_2, 12 hits
PS00023 FN2_1, 2 hits
PS51092 FN2_2, 2 hits
PS50853 FN3, 16 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFINC_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02751
Secondary accession number(s): B7ZLF0
, E9PE77, E9PG29, O95609, O95610, Q14312, Q14325, Q14326, Q17RV7, Q53S27, Q564H7, Q585T2, Q59EH1, Q60FE4, Q68DP8, Q68DP9, Q68DT4, Q6LDP6, Q6MZS0, Q6MZU5, Q6N025, Q6N0A6, Q7Z391, Q86T27, Q8IVI8, Q96KP7, Q96KP8, Q96KP9, Q9H1B8, Q9HAP3, Q9UMK2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 16, 2019
Last modified: October 16, 2019
This is version 256 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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