Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fibronectin

Gene

Fn1

Organism
Mus musculus (Mouse)
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 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.1 Publication
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 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi906 – 1171Add 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-MMU-114608 Platelet degranulation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1474244 Extracellular matrix organization
R-MMU-1566977 Fibronectin matrix formation
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000170 Syndecan interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-MMU-372708 p130Cas linkage to MAPK signaling for integrins
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8957275 Post-translational protein phosphorylation

<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
Cleaved into the following chain:
<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95566 Fn1

<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; 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

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>Mutagenesisi35Q → A: 99% decrease in cross-linking efficiency; when associated with A-36 and A-48. 1 Publication1
Mutagenesisi35Q → L: 65% decrease in cross-linking efficiency; when associated with L-36. 1 Publication1
Mutagenesisi36Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-48. 1 Publication1
Mutagenesisi36Q → L: 65% decrease in cross-linking efficiency; when associated with L-35. 1 Publication1
Mutagenesisi48Q → A: 99% decrease in cross-linking efficiency; when associated with A-35 and A-36. 1 Publication1

<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 – 32By similarityAdd BLAST32
<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_000001923633 – 2477FibronectinAdd BLAST2445
ChainiPRO_0000390480627 – 701AnastellinBy similarityAdd BLAST75

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 residuei33Pyrrolidone carboxylic acidBy similarity1
<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-linki35Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)1 Publication
Cross-linki36Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)1 Publication
Cross-linki48Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)1 Publication
<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 bondi53 ↔ 79By similarity
Disulfide bondi77 ↔ 88By similarity
Disulfide bondi98 ↔ 126By similarity
Disulfide bondi124 ↔ 136By similarity
Disulfide bondi142 ↔ 170By similarity
Disulfide bondi168 ↔ 180By similarity
Disulfide bondi187 ↔ 216By similarity
Disulfide bondi214 ↔ 226By similarity
Disulfide bondi232 ↔ 261By similarity
Disulfide bondi259 ↔ 271By similarity
Modified residuei285PhosphoserineCombined sources1
Disulfide bondi308 ↔ 335By similarity
Disulfide bondi333 ↔ 342By similarity
Disulfide bondi360 ↔ 386By similarity
Disulfide bondi374 ↔ 401By similarity
Disulfide bondi420 ↔ 446By similarity
<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>Glycosylationi430N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi434 ↔ 461By similarity
Disulfide bondi470 ↔ 498By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi518 ↔ 545By similarity
Glycosylationi528N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi542N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi543 ↔ 555By similarity
Disulfide bondi561 ↔ 589By similarity
Disulfide bondi587 ↔ 599By similarity
Modified residuei875SulfotyrosineSequence analysis1
Glycosylationi876N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei880SulfotyrosineSequence analysis1
Glycosylationi1006N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi1243N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1290N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi2198N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2296 ↔ 2325By similarity
Disulfide bondi2323 ↔ 2335By similarity
Disulfide bondi2341 ↔ 2368By similarity
Disulfide bondi2366 ↔ 2378By similarity
Disulfide bondi2385 ↔ 2411By similarity
Modified residuei2392SulfotyrosineSequence analysis1
Disulfide bondi2409 ↔ 2420By similarity
Modified residuei2454PhosphothreonineBy similarity1
Disulfide bondi2458Interchain (with C-2462)
Disulfide bondi2462Interchain (with C-2458)
Modified residuei2475PhosphoserineCombined sources1

<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.By similarity
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).1 Publication
Phosphorylated by FAM20C in the extracellular medium.By similarity
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.By similarity
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.1 Publication

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P11276

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P11276

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P11276

PeptideAtlas

More...
PeptideAtlasi
P11276

PRoteomics IDEntifications database

More...
PRIDEi
P11276

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11276

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

More...
PhosphoSitePlusi
P11276

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P11276

<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

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.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Glucocorticoids suppressed mRNA expression and protein synthesis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026193 Expressed in 313 organ(s), highest expression level in vault of skull

CleanEx database of gene expression profiles

More...
CleanExi
MM_FN1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P11276 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P11276 MM

<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, LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR; interaction mediates inhibition of cell adhesion and neurite outgrowth. Interacts with FBLN7. Interacts with FST3 and MYOC (By similarity).By similarity

<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

WithEntry#Exp.IntActNotes
Plcg2Q8CIH56EBI-641955,EBI-617954

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199719, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P11276

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P11276

Protein interaction database and analysis system

More...
IntActi
P11276, 6 interactors

Molecular INTeraction database

More...
MINTi
P11276

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000054499

<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

Secondary structure

12477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P11276

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

More...
SMRi
P11276

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P11276

<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>Domaini51 – 91Fibronectin type-I 1PROSITE-ProRule annotationAdd BLAST41
Domaini96 – 139Fibronectin type-I 2PROSITE-ProRule annotationAdd BLAST44
Domaini140 – 183Fibronectin type-I 3PROSITE-ProRule annotationAdd BLAST44
Domaini185 – 229Fibronectin type-I 4PROSITE-ProRule annotationAdd BLAST45
Domaini230 – 274Fibronectin type-I 5PROSITE-ProRule annotationAdd BLAST45
Domaini306 – 343Fibronectin type-I 6PROSITE-ProRule annotationAdd BLAST38
Domaini355 – 403Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini415 – 463Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini468 – 516Fibronectin type-I 7PROSITE-ProRule annotationAdd BLAST49
Domaini516 – 558Fibronectin type-I 8PROSITE-ProRule annotationAdd BLAST43
Domaini559 – 602Fibronectin type-I 9PROSITE-ProRule annotationAdd BLAST44
Domaini610 – 717Fibronectin type-III 1Add BLAST108
Domaini721 – 811Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST91
Domaini812 – 903Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini908 – 997Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST90
Domaini998 – 1087Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST90
Domaini1088 – 1174Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST87
Domaini1175 – 1269Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST95
Domaini1270 – 1358Fibronectin type-III 8; extra domain 1PROSITE-ProRule annotationAdd BLAST89
Domaini1359 – 1451Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST93
Domaini1452 – 1539Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST88
Domaini1540 – 1633Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST94
Domaini1634 – 1725Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST92
Domaini1726 – 1813Fibronectin type-III 13; extra domain 2PROSITE-ProRule annotationAdd BLAST88
Domaini1814 – 1907Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST94
Domaini1908 – 1994Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST87
Domaini1995 – 2085Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST91
Domaini2193 – 2287Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST95
Domaini2294 – 2338Fibronectin type-I 10PROSITE-ProRule annotationAdd BLAST45
Domaini2339 – 2381Fibronectin type-I 11PROSITE-ProRule annotationAdd BLAST43
Domaini2383 – 2426Fibronectin 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>Regioni53 – 273Fibrin- and heparin-binding 1Add BLAST221
Regioni308 – 608Collagen-bindingAdd BLAST301
Regioni1357 – 1630Cell-attachmentAdd BLAST274
Regioni1811 – 2081Heparin-binding 2Add BLAST271
Regioni2082 – 2201Connecting strand 3 (CS-3) (V region)Add BLAST120
Regioni2296 – 2427Fibrin-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>Motifi1614 – 1616Cell attachment site3
Motifi2181 – 2183Cell attachment site3

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IF4N Eukaryota
ENOG410Y2NH LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155126

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234344

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005731

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P11276

KEGG Orthology (KO)

More...
KOi
K05717

Database of Orthologous Groups

More...
OrthoDBi
EOG091G116D

TreeFam database of animal gene trees

More...
TreeFami
TF329915

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 17 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.10.10, 2 hits
2.60.40.10, 17 hits

Integrated resource of protein families, domains and functional sites

More...
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, 17 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, 17 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 11 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, 17 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)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 1 <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> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. Each of the "extra domain" and the connecting strand 3 are present in some forms of fibronectin and absent in others.

This entry has 1 described isoform and 11 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11276-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK
60 70 80 90 100
PGCFDNGKHY QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD
110 120 130 140 150
KYTGNTYKVG DTYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK
160 170 180 190 200
IGDKWRRPHE TGGYMLECLC LGNGKGEWTC KPIAEKCFDH AAGTSYVVGE
210 220 230 240 250
TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS YRIGDTWSKK
260 270 280 290 300
DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP
310 320 330 340 350
QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT
360 370 380 390 400
YGGNSNGEPC VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF
410 420 430 440 450
CTDHAVLVQT RGGNSNGALC HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ
460 470 480 490 500
NYDADQKFGF CPMAAHEEIC TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG
510 520 530 540 550
NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM LNCTCFGQGR
560 570 580 590 600
GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
610 620 630 640 650
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS
660 670 680 690 700
TGRWKEATIP GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS
710 720 730 740 750
ASTPVTSNTV TGETAPYSPV VATSESVTEI TASSFVVSWV SASDTVSGFR
760 770 780 790 800
VEYELSEEGD EPQYLDLPST ATSVNIPDLL PGRKYIVNVY QISEEGKQSL
810 820 830 840 850
ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY RIVYSPSVEG
860 870 880 890 900
SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT
910 920 930 940 950
PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG
960 970 980 990 1000
QRLPVNRNTF AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT
1010 1020 1030 1040 1050
NLQFVNETDR TVLVTWTPPR ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY
1060 1070 1080 1090 1100
PLRNLQPGSE YTVTLVAVKG NQQSPKATGV FTTLQPLRSI PPYNTEVTET
1110 1120 1130 1140 1150
TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS GLTPGVEYTY
1160 1170 1180 1190 1200
TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
1210 1220 1230 1240 1250
DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK
1260 1270 1280 1290 1300
DDKESAPISD TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT
1310 1320 1330 1340 1350
VVAAGEGIPI FEDFVDSSVG YYTVTGLEPG IDYDISVITL INGGESAPTT
1360 1370 1380 1390 1400
LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP PSIELTNLLV RYSPVKNEED
1410 1420 1430 1440 1450
VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL RGRQKTGLDS
1460 1470 1480 1490 1500
PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR
1510 1520 1530 1540 1550
NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST
1560 1570 1580 1590 1600
PTSLLISWEP PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP
1610 1620 1630 1640 1650
GADYTITLYA VTGRGDSPAS SKPVSINYKT EIDKPSQMQV TDVQDNSISV
1660 1670 1680 1690 1700
RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA SPDQTEMTIE GLQPTVEYVV
1710 1720 1730 1740 1750
SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI AWESPQGQVS
1760 1770 1780 1790 1800
RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME
1810 1820 1830 1840 1850
SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE
1860 1870 1880 1890 1900
KTGPMKEINL SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT
1910 1920 1930 1940 1950
LENVSPPRRA RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQTPVQRS
1960 1970 1980 1990 2000
ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA RSSPVIIDAS TAIDAPSNLR
2010 2020 2030 2040 2050
FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR PRPGVTEATI
2060 2070 2080 2090 2100
TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
2110 2120 2130 2140 2150
LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT
2160 2170 2180 2190 2200
TPPTAATPVR LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS
2210 2220 2230 2240 2250
TGQEALSQTT ISWTPFQESS EYIISCQPVG TDEEPLQFQV PGTSTSATLT
2260 2270 2280 2290 2300
GLTRGVTYNI IVEALQNQRR HKVREEVVTV GNAVSEGLNQ PTDDSCFDPY
2310 2320 2330 2340 2350
TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW CHDNGVNYKI
2360 2370 2380 2390 2400
GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
2410 2420 2430 2440 2450
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ
2460 2470
RTNTNVNCPI ECFMPLDVQA DRDDSRE
Length:2,477
Mass (Da):272,538
Last modified:October 3, 2012 - v4
<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:i24A207BE67F85585
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 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WS56A0A087WS56_MOUSE
Fibronectin
Fn1
2,266Annotation 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>
B7ZNJ1B7ZNJ1_MOUSE
Fibronectin
Fn1
2,176Annotation 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>
Q3UHL6Q3UHL6_MOUSE
Fibronectin
Fn1
2,361Annotation 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>
B9EHT6B9EHT6_MOUSE
Fibronectin
Fn1
2,271Annotation 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>
A0A087WSN6A0A087WSN6_MOUSE
Fibronectin
Fn1 mCG_121782
2,296Annotation 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>
A0A087WR50A0A087WR50_MOUSE
Fibronectin
Fn1 mCG_121782
2,386Annotation 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>
Q4KL80Q4KL80_MOUSE
Fibronectin
Fn1
383Annotation 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>
A0A087WQW8A0A087WQW8_MOUSE
Fibronectin
Fn1
160Annotation 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>
A0A087WQE0A0A087WQE0_MOUSE
Fibronectin
Fn1
71Annotation 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>
A0A087WS99A0A087WS99_MOUSE
Fibronectin
Fn1
200Annotation 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>
There is more potential isoformShow all

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 conflicti1063V → A in CAA63654 (Ref. 6) Curated1
Sequence conflicti1820F → L in CAA63654 (Ref. 6) Curated1
Sequence conflicti2440T → N in AAA37636 (PubMed:3124113).Curated1

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
AC124821 Genomic DNA No translation available.
CH466548 Genomic DNA Translation: EDL00265.1
BC051082 mRNA No translation available.
Z22729 Genomic DNA Translation: CAA80422.1
X82402 mRNA Translation: CAA57796.1
X93167 mRNA Translation: CAA63654.1
M18194 mRNA Translation: AAA37636.1
S45680 mRNA Translation: AAB23491.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS15031.1 [P11276-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A49173
I48349

NCBI Reference Sequences

More...
RefSeqi
NP_034363.1, NM_010233.2 [P11276-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.193099

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193 [P11276-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
14268

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:14268

UCSC genome browser

More...
UCSCi
uc007bju.2 mouse [P11276-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC124821 Genomic DNA No translation available.
CH466548 Genomic DNA Translation: EDL00265.1
BC051082 mRNA No translation available.
Z22729 Genomic DNA Translation: CAA80422.1
X82402 mRNA Translation: CAA57796.1
X93167 mRNA Translation: CAA63654.1
M18194 mRNA Translation: AAA37636.1
S45680 mRNA Translation: AAB23491.1
CCDSiCCDS15031.1 [P11276-1]
PIRiA49173
I48349
RefSeqiNP_034363.1, NM_010233.2 [P11276-1]
UniGeneiMm.193099

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
1MFNNMR-A1447-1630[»]
2MFNNMR-A1447-1630[»]
ProteinModelPortaliP11276
SMRiP11276
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199719, 2 interactors
CORUMiP11276
ELMiP11276
IntActiP11276, 6 interactors
MINTiP11276
STRINGi10090.ENSMUSP00000054499

PTM databases

iPTMnetiP11276
PhosphoSitePlusiP11276
SwissPalmiP11276

Proteomic databases

EPDiP11276
MaxQBiP11276
PaxDbiP11276
PeptideAtlasiP11276
PRIDEiP11276

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193 [P11276-1]
GeneIDi14268
KEGGimmu:14268
UCSCiuc007bju.2 mouse [P11276-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2335
MGIiMGI:95566 Fn1

Phylogenomic databases

eggNOGiENOG410IF4N Eukaryota
ENOG410Y2NH LUCA
GeneTreeiENSGT00940000155126
HOGENOMiHOG000234344
HOVERGENiHBG005731
InParanoidiP11276
KOiK05717
OrthoDBiEOG091G116D
TreeFamiTF329915

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1474244 Extracellular matrix organization
R-MMU-1566977 Fibronectin matrix formation
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000170 Syndecan interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-354192 Integrin alphaIIb beta3 signaling
R-MMU-354194 GRB2:SOS provides linkage to MAPK signaling for Integrins
R-MMU-372708 p130Cas linkage to MAPK signaling for integrins
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8957275 Post-translational protein phosphorylation

Miscellaneous databases

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

More...
ChiTaRSi
Fn1 mouse
EvolutionaryTraceiP11276

Protein Ontology

More...
PROi
PR:P11276

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026193 Expressed in 313 organ(s), highest expression level in vault of skull
CleanExiMM_FN1
ExpressionAtlasiP11276 baseline and differential
GenevisibleiP11276 MM

Family and domain databases

CDDicd00061 FN1, 12 hits
cd00062 FN2, 2 hits
cd00063 FN3, 17 hits
Gene3Di2.10.10.10, 2 hits
2.60.40.10, 17 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, 17 hits
SMARTiView protein in SMART
SM00058 FN1, 12 hits
SM00059 FN2, 2 hits
SM00060 FN3, 17 hits
SUPFAMiSSF49265 SSF49265, 11 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, 17 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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_MOUSE
<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: P11276
Secondary accession number(s): G5E8B8
, Q61567, Q61568, Q61569, Q64233, Q80UI4
<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 1, 1989
Last sequence update: October 3, 2012
Last modified: December 5, 2018
This is version 204 of the entry and version 4 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

<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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again