Skip Header

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

UniProtKB - P09055 (ITB1_MOUSE)

Entry version 212 (16 Oct 2019)
Sequence version 1 (01 Nov 1988)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Integrin beta-1

Gene

Itgb1

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

Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition (PubMed:12941630). Involved in promoting endothelial cell motility and angiogenesis (PubMed:15181153). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules (PubMed:21768292). May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (PubMed:18804435). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity).By similarity6 Publications
Isoform 2: Isoform 2 displaces isoform 1 in striated muscles.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi152MagnesiumBy similarity1
Metal bindingi154Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 1By similarity1
Metal bindingi157Calcium 1By similarity1
Metal bindingi189Calcium 2By similarity1
Metal bindingi244Calcium 2By similarity1
Metal bindingi246Calcium 2By similarity1
Metal bindingi248Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi249Calcium 2By similarity1
Metal bindingi249MagnesiumBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionIntegrin, Receptor
Biological processCell adhesion
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1566948 Elastic fibre formation
R-MMU-1566977 Fibronectin matrix formation
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-210991 Basigin interactions
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000157 Laminin interactions
R-MMU-3000170 Syndecan interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-445144 Signal transduction by L1
R-MMU-446343 Localization of the PINCH-ILK-PARVIN complex to focal adhesions
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8875513 MET interacts with TNS proteins

<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:
Integrin beta-1
Alternative name(s):
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen: CD29
<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:Itgb1
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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 8

Organism-specific databases

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

More...MGIi		MGI:96610 Itgb1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini21 – 728ExtracellularSequence analysisAdd BLAST708
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei729 – 751HelicalSequence analysisAdd BLAST23
Topological domaini752 – 798CytoplasmicSequence analysisAdd BLAST47

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endosome, Membrane

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Isoform 2 knockout mice are viable and fertile, but male mice display a mild abnormality of cardiac function reflected by an increased expression of atrial natriuretic peptide and beta myosin heavy chain. Muscles do not show any histological or ultrastructural alterations. Replacement of isoform 1 by isoform 2 results in embryonic lethality before 16.5 dpc with a plethora of developmental defects including open neural tube, which is abnormally waved both rostrally and caudally. Some embryos lack part of the hindbrain and in most embryos the first branchial arch is shortened, which in some of the embryos leaves the tongue exposed. Abnormally strong fibronectin staining is seen in the mesenchyme under the open neural tube. Extravasation of red blood cells is evident in various tissues and they are also found in the pericardial cavity. Choroid plexus is virtually absent correlating with the presence of an abnormally smooth head and small brain cavities. At later developmental stages, a striking feature is the lack of a lower jaw and a dysmorphic lower face. These defects are in part caused by the abnormal migration of neuroepithelial cells.1 Publication

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>Mutagenesisi783Y → F: Reduced endocytosis; when associated with F-795. 1 Publication1
Mutagenesisi795Y → F: Reduced endocytosis; when associated with F-783. 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 – 20Add BLAST20
<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_000001633521 – 798Integrin beta-1Add BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi27 ↔ 45By similarity
Disulfide bondi35 ↔ 464By similarity
Disulfide bondi38 ↔ 75By similarity
Disulfide bondi48 ↔ 64By 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>Glycosylationi50N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi207 ↔ 213By similarity
Glycosylationi212N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi261 ↔ 301By similarity
Glycosylationi269N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi363N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi401 ↔ 415By similarity
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi466 ↔ 691By similarity
Disulfide bondi477 ↔ 489By similarity
Glycosylationi481N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi486 ↔ 525By similarity
Disulfide bondi491 ↔ 500By similarity
Disulfide bondi502 ↔ 516By similarity
Glycosylationi520N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi531 ↔ 536By similarity
Disulfide bondi533 ↔ 568By similarity
Disulfide bondi538 ↔ 553By similarity
Disulfide bondi555 ↔ 560By similarity
Disulfide bondi574 ↔ 579By similarity
Disulfide bondi576 ↔ 607By similarity
Disulfide bondi581 ↔ 590By similarity
Glycosylationi584N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi592 ↔ 599By similarity
Disulfide bondi613 ↔ 618By similarity
Disulfide bondi615 ↔ 661By similarity
Disulfide bondi620 ↔ 630By similarity
Disulfide bondi633 ↔ 636By similarity
Disulfide bondi640 ↔ 649By similarity
Disulfide bondi646 ↔ 723By similarity
Disulfide bondi665 ↔ 699By similarity
Glycosylationi669N-linked (GlcNAc...) asparagine1 Publication1
<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 residuei777PhosphothreonineCombined sources1
Modified residuei783PhosphotyrosineCombined sources1
Modified residuei785PhosphoserineBy similarity1
Modified residuei789PhosphothreonineBy similarity1
Modified residuei794N6-acetyllysine; alternateBy 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-linki794Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity

<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

The cysteine residues are involved in intrachain disulfide bonds.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P09055

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09055

MaxQB - The MaxQuant DataBase

More...MaxQBi		P09055

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

More...PaxDbi		P09055

PeptideAtlas

More...PeptideAtlasi		P09055

PRoteomics IDEntifications database

More...PRIDEi		P09055

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2403

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P09055

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

More...PhosphoSitePlusi		P09055

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P09055

<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

Isoform 2 is expressed in skeletal and cardiac muscles only (at protein level). Isoform 1 is very weakly expressed in striated muscles and not detected in adult skeletal muscle fibers and cardiomyocytes.1 Publication

<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

Isoform 2 is not detected in proliferating myoblasts, but it appears immediately after myoblast fusion and its amount continues to rise during myotube growth and maturation reaching its highest level at day 9 through day 10, when mature differentiated myotubes appear in cell culture. Isoform 1 expression is down-regulated during myodifferentiation in culture and it is completely displaced by isoform 2 in mature differentiated myotubes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000025809 Expressed in 327 organ(s), highest expression level in trachea

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P09055 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P09055 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

Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner (By similarity). Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5.

Interacts with FLNA, FLNB, FLNC and RANBP9.

Interacts with KRT1 in the presence of RACK1 and SRC.

Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization.

Interacts with RAB21.

Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region).

Interacts with MYO10.

Interacts with ITGB1BP1 (via C-terminal region); the interaction is a prerequisite for focal adhesion disassembly.

Interacts with TLN1; the interaction is prevented by competitive binding of ITGB1BP1.

Interacts with ACAP1; required for ITGB1 recycling.

Interacts with ASAP3.

Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1.

Interacts with DAB2.

Interacts with FGR and HCK.

Isoform 2 interacts with alpha-7A and alpha-7B in adult skeletal muscle.

Isoform 2 interacts with alpha-7B in cardiomyocytes of adult heart.

Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has a heterodimer form (PubMed:12189152). ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1 interacts with IL1B.

Interacts with MDK (PubMed:15466886). ITGA4:ITGB1 interacts with MDK; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation (PubMed:15466886). ITGA6:ITGB1 interacts with MDK; this interaction mediates MDK-inducedneurite-outgrowth (PubMed:15466886).

By similarity9 Publications

<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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		200826, 52 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3027 Integrin alpha5-beta1 complex
CPX-3114 Integrin alpha1-beta1 complex
CPX-3115 Integrin alpha2-beta1 complex
CPX-3117 Integrin alpha3-beta1 complex
CPX-3118 integrin alpha4-beta1 complex
CPX-3119 Integrin alpha6-beta1 complex
CPX-3121 Integrin alpha7-beta1 complex
CPX-3122 Integrin alpha8-beta1 complex
CPX-3123 Integrin alpha9-beta1 complex
CPX-3124 Integrin alpha10-beta1 complex
CPX-3125 Integrin alpha11-beta1 complex
CPX-3130 Integrin alphav-beta1 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P09055

Database of interacting proteins

More...DIPi		DIP-46247N

Protein interaction database and analysis system

More...IntActi		P09055, 62 interactors

Molecular INTeraction database

More...MINTi		P09055

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000087457

<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

1798
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P09055

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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>Domaini140 – 378VWFAAdd BLAST239
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati466 – 515IAdd BLAST50
Repeati516 – 559IIAdd BLAST44
Repeati560 – 598IIIAdd BLAST39
Repeati599 – 635IVAdd BLAST37

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>Regioni207 – 213CX3CL1-bindingBy similarity7
Regioni295 – 314CX3CL1-bindingBy similarityAdd BLAST20
Regioni466 – 635Cysteine-rich tandem repeatsAdd BLAST170
Regioni762 – 767Signal for sorting from recycling endosomes; interaction with ACAP1By similarity6
Regioni785 – 792Interaction with ITGB1BP1By similarity8

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the integrin beta chain family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1226 Eukaryota
ENOG410XP60 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00960000186593

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000252936

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09055

KEGG Orthology (KO)

More...KOi		K05719

Identification of Orthologs from Complete Genome Data

More...OMAi		DEQMCTF

Database of Orthologous Groups

More...OrthoDBi		473040at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09055

TreeFam database of animal gene trees

More...TreeFami		TF105392

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.410, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013111 EGF_extracell
IPR040622 I-EGF_1
IPR027071 Integrin_beta-1
IPR033760 Integrin_beta_N
IPR015812 Integrin_bsu
IPR014836 Integrin_bsu_cyt_dom
IPR012896 Integrin_bsu_tail
IPR036349 Integrin_bsu_tail_dom_sf
IPR002369 Integrin_bsu_VWA
IPR032695 Integrin_dom_sf
IPR016201 PSI
IPR036465 vWFA_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR10082 PTHR10082, 1 hit
PTHR10082:SF28 PTHR10082:SF28, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07974 EGF_2, 1 hit
PF18372 I-EGF_1, 1 hit
PF08725 Integrin_b_cyt, 1 hit
PF07965 Integrin_B_tail, 1 hit
PF00362 Integrin_beta, 1 hit
PF17205 PSI_integrin, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002512 Integrin_B, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01186 INTEGRINB

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00187 INB, 1 hit
SM01241 Integrin_b_cyt, 1 hit
SM01242 Integrin_B_tail, 1 hit
SM00423 PSI, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53300 SSF53300, 1 hit
SSF69179 SSF69179, 1 hit
SSF69687 SSF69687, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00022 EGF_1, 2 hits
PS00243 INTEGRIN_BETA, 3 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 (2+)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 2 <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 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P09055-1) [UniParc]FASTAAdd to basket
Also known as: Beta-1A

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
MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN 
        60         70         80         90        100
TTFLQEGMPT SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK 
       110        120        130        140        150
GMAEKLRPED ITQIQPQQLL LKLRSGEPQK FTLKFKRAED YPIDLYYLMD 
       160        170        180        190        200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP 
       210        220        230        240        250
AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR ISGNLDSPEG 
       260        270        280        290        300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 
       310        320        330        340        350
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN 
       360        370        380        390        400
LIPKSAVGTL SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY 
       410        420        430        440        450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TANKCPNKES ETIKIKPLGF 
       460        470        480        490        500
TEEVEVVLQF ICKCNCQSHG IPASPKCHEG NGTFECGACR CNEGRVGRHC 
       510        520        530        540        550
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG 
       560        570        580        590        600
KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL 
       610        620        630        640        650
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR 
       660        670        680        690        700
AFNKGEKKDT CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW 
       710        720        730        740        750
FYFTYSVNGN NEAIVHVVET PDCPTGPDII PIVAGVVAGI VLIGLALLLI 
       760        770        780        790 
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
Length:798
Mass (Da):88,231
Last modified:November 1, 1988 - v1
<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:i26788F7F0A168B56
GO
Isoform 2 (identifier: P09055-2) [UniParc]FASTAAdd to basket
Also known as: Beta-1D

The sequence of this isoform differs from the canonical sequence as follows:
     778-778: G → Q
     786-798: AVTTVVNPKYEGK → PINNFKNPNYGRKAGL

Show »
Length:801
Mass (Da):88,700
Checksum:i7559450B2812F5A2
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
D6RJL5D6RJL5_MOUSE
Integrin beta-1
Itgb1
58Annotation 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>
A0A0A0MQJ3A0A0A0MQJ3_MOUSE
Integrin beta-1
Itgb1
112Annotation 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 BAC36379 differs from that shown. Reason: Erroneous initiation. Truncated 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 conflicti5L → Q in BAC40532 (PubMed:16141072).Curated1
Sequence conflicti72K → E in BAE35290 (PubMed:16141072).Curated1
Sequence conflicti385E → D in BAC36379 (PubMed:16141072).Curated1
Sequence conflicti385E → P in CAA33272 (PubMed:2523953).Curated1
Sequence conflicti392G → A in CAA33272 (PubMed:2523953).Curated1
Sequence conflicti407G → E in BAC36379 (PubMed:16141072).Curated1
Sequence conflicti443 – 445IKI → HSKL in CAA33272 (PubMed:2523953).Curated3

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_053581778G → Q in isoform 2. 1 Publication1
Alternative sequenceiVSP_053582786 – 798AVTTV…KYEGK → PINNFKNPNYGRKAGL in isoform 2. 1 PublicationAdd BLAST13

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
Y00769 mRNA Translation: CAA68738.1
AK076526 mRNA Translation: BAC36379.1 Different initiation.
AK088729 mRNA Translation: BAC40532.1
AK159689 mRNA Translation: BAE35290.1
AK167682 mRNA Translation: BAE39731.1
AC156608 Genomic DNA No translation available.
CH466525 Genomic DNA Translation: EDL11832.1
BC050906 mRNA Translation: AAH50906.1
X15202 mRNA Translation: CAA33272.1
U37029 mRNA Translation: AAA80243.1
U47283 Genomic DNA Translation: AAA88821.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS22791.1 [P09055-1]

Protein sequence database of the Protein Information Resource

More...PIRi		PL0104 IJMSFB
S01659

NCBI Reference Sequences

More...RefSeqi		NP_034708.1, NM_010578.2 [P09055-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809 [P09055-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		16412

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:16412

UCSC genome browser

More...UCSCi		uc009nzv.2 mouse [P09055-1]

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
Y00769 mRNA Translation: CAA68738.1
AK076526 mRNA Translation: BAC36379.1 Different initiation.
AK088729 mRNA Translation: BAC40532.1
AK159689 mRNA Translation: BAE35290.1
AK167682 mRNA Translation: BAE39731.1
AC156608 Genomic DNA No translation available.
CH466525 Genomic DNA Translation: EDL11832.1
BC050906 mRNA Translation: AAH50906.1
X15202 mRNA Translation: CAA33272.1
U37029 mRNA Translation: AAA80243.1
U47283 Genomic DNA Translation: AAA88821.1
CCDSiCCDS22791.1 [P09055-1]
PIRiPL0104 IJMSFB
S01659
RefSeqiNP_034708.1, NM_010578.2 [P09055-1]

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
5XQ0X-ray2.75A/B784-798[»]
SMRiP09055
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi200826, 52 interactors
ComplexPortaliCPX-3027 Integrin alpha5-beta1 complex
CPX-3114 Integrin alpha1-beta1 complex
CPX-3115 Integrin alpha2-beta1 complex
CPX-3117 Integrin alpha3-beta1 complex
CPX-3118 integrin alpha4-beta1 complex
CPX-3119 Integrin alpha6-beta1 complex
CPX-3121 Integrin alpha7-beta1 complex
CPX-3122 Integrin alpha8-beta1 complex
CPX-3123 Integrin alpha9-beta1 complex
CPX-3124 Integrin alpha10-beta1 complex
CPX-3125 Integrin alpha11-beta1 complex
CPX-3130 Integrin alphav-beta1 complex
CORUMiP09055
DIPiDIP-46247N
IntActiP09055, 62 interactors
MINTiP09055
STRINGi10090.ENSMUSP00000087457

PTM databases

GlyConnecti2403
iPTMnetiP09055
PhosphoSitePlusiP09055
SwissPalmiP09055

Proteomic databases

EPDiP09055
jPOSTiP09055
MaxQBiP09055
PaxDbiP09055
PeptideAtlasiP09055
PRIDEiP09055

Genome annotation databases

EnsembliENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809 [P09055-1]
GeneIDi16412
KEGGimmu:16412
UCSCiuc009nzv.2 mouse [P09055-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3688
MGIiMGI:96610 Itgb1

Phylogenomic databases

eggNOGiKOG1226 Eukaryota
ENOG410XP60 LUCA
GeneTreeiENSGT00960000186593
HOGENOMiHOG000252936
InParanoidiP09055
KOiK05719
OMAiDEQMCTF
OrthoDBi473040at2759
PhylomeDBiP09055
TreeFamiTF105392

Enzyme and pathway databases

ReactomeiR-MMU-1566948 Elastic fibre formation
R-MMU-1566977 Fibronectin matrix formation
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-210991 Basigin interactions
R-MMU-2129379 Molecules associated with elastic fibres
R-MMU-216083 Integrin cell surface interactions
R-MMU-3000157 Laminin interactions
R-MMU-3000170 Syndecan interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-445144 Signal transduction by L1
R-MMU-446343 Localization of the PINCH-ILK-PARVIN complex to focal adhesions
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8875513 MET interacts with TNS proteins

Miscellaneous databases

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

More...ChiTaRSi		Itgb1 mouse

Protein Ontology

More...PROi		PR:P09055

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000025809 Expressed in 327 organ(s), highest expression level in trachea
ExpressionAtlasiP09055 baseline and differential
GenevisibleiP09055 MM

Family and domain databases

Gene3Di3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR013111 EGF_extracell
IPR040622 I-EGF_1
IPR027071 Integrin_beta-1
IPR033760 Integrin_beta_N
IPR015812 Integrin_bsu
IPR014836 Integrin_bsu_cyt_dom
IPR012896 Integrin_bsu_tail
IPR036349 Integrin_bsu_tail_dom_sf
IPR002369 Integrin_bsu_VWA
IPR032695 Integrin_dom_sf
IPR016201 PSI
IPR036465 vWFA_dom_sf
PANTHERiPTHR10082 PTHR10082, 1 hit
PTHR10082:SF28 PTHR10082:SF28, 1 hit
PfamiView protein in Pfam
PF07974 EGF_2, 1 hit
PF18372 I-EGF_1, 1 hit
PF08725 Integrin_b_cyt, 1 hit
PF07965 Integrin_B_tail, 1 hit
PF00362 Integrin_beta, 1 hit
PF17205 PSI_integrin, 1 hit
PIRSFiPIRSF002512 Integrin_B, 1 hit
PRINTSiPR01186 INTEGRINB
SMARTiView protein in SMART
SM00187 INB, 1 hit
SM01241 Integrin_b_cyt, 1 hit
SM01242 Integrin_B_tail, 1 hit
SM00423 PSI, 1 hit
SUPFAMiSSF53300 SSF53300, 1 hit
SSF69179 SSF69179, 1 hit
SSF69687 SSF69687, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 2 hits
PS00243 INTEGRIN_BETA, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiITB1_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: P09055
Secondary accession number(s): F6R105
, Q3TIW5, Q3TWH6, Q60993, Q61126, Q8BTU0, Q8BVU1
<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: November 1, 1988
Last sequence update: November 1, 1988
Last modified: October 16, 2019
This is version 212 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
  3. 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