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Entry version 184 (12 Aug 2020)
Sequence version 1 (01 Feb 1996)
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Protein

Integrin beta-1

Gene

Itgb1

Organism
Rattus norvegicus (Rat)
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 transcript 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. 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. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. 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 (By similarity). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. 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. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

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 functionIntegrin, Receptor
Biological processCell adhesion
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1566948, Elastic fibre formation
R-RNO-1566977, Fibronectin matrix formation
R-RNO-198933, Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-RNO-202733, Cell surface interactions at the vascular wall
R-RNO-210991, Basigin interactions
R-RNO-2129379, Molecules associated with elastic fibres
R-RNO-216083, Integrin cell surface interactions
R-RNO-3000157, Laminin interactions
R-RNO-3000170, Syndecan interactions
R-RNO-3000178, ECM proteoglycans
R-RNO-445144, Signal transduction by L1
R-RNO-446343, Localization of the PINCH-ILK-PARVIN complex to focal adhesions
R-RNO-8874081, MET activates PTK2 signaling
R-RNO-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%5Fand%5Ftaxonomy%5Fsection">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):
Beta oligodendroglia
Short name:
Beta OL
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen: CD29
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2927, 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%5Flocation%5Fsection">'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 – 729ExtracellularSequence analysisAdd BLAST709
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei730 – 752HelicalSequence analysisAdd BLAST23
Topological domaini753 – 799CytoplasmicSequence analysisAdd BLAST47

Keywords - Cellular componenti

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

<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 – 20By similarityAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001633621 – 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 ↔ 465By similarity
Disulfide bondi38 ↔ 75By similarity
Disulfide bondi48 ↔ 64By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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...) asparagineSequence analysis1
Disulfide bondi401 ↔ 415By similarity
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 463By similarity
Disulfide bondi467 ↔ 692By similarity
Disulfide bondi478 ↔ 490By similarity
Glycosylationi482N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi487 ↔ 526By similarity
Disulfide bondi492 ↔ 501By similarity
Disulfide bondi503 ↔ 517By similarity
Glycosylationi521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi532 ↔ 537By similarity
Disulfide bondi534 ↔ 569By similarity
Disulfide bondi539 ↔ 554By similarity
Disulfide bondi556 ↔ 561By similarity
Disulfide bondi575 ↔ 580By similarity
Disulfide bondi577 ↔ 608By similarity
Disulfide bondi582 ↔ 591By similarity
Glycosylationi585N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi593 ↔ 600By similarity
Disulfide bondi614 ↔ 619By similarity
Disulfide bondi616 ↔ 662By similarity
Disulfide bondi621 ↔ 631By similarity
Disulfide bondi634 ↔ 637By similarity
Disulfide bondi641 ↔ 650By similarity
Disulfide bondi647 ↔ 724By similarity
Disulfide bondi666 ↔ 700By similarity
Glycosylationi670N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei778PhosphothreonineBy similarity1
Modified residuei784PhosphotyrosineBy similarity1
Modified residuei786PhosphoserineBy similarity1
Modified residuei790PhosphothreonineBy similarity1
Modified residuei795N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki795Glycyl 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%5Fprocessing%5Fsection">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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P49134

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

More...
PaxDbi
P49134

PRoteomics IDEntifications database

More...
PRIDEi
P49134

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P49134, 12 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P49134

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

More...
PhosphoSitePlusi
P49134

<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%5Fsection">'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%5Fsection">'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 (By similarity). ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (By similarity). 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 (By similarity). 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 (By similarity).

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

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
246668, 7 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P49134

Protein interaction database and analysis system

More...
IntActi
P49134, 4 interactors

Molecular INTeraction database

More...
MINTi
P49134

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000014785

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

3D structure databases

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

More...
SMRi
P49134

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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>Repeati467 – 516IAdd BLAST50
Repeati517 – 560IIAdd BLAST44
Repeati561 – 599IIIAdd BLAST39
Repeati600 – 636IVAdd 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
Regioni467 – 636Cysteine-rich tandem repeatsAdd BLAST170
Regioni763 – 768Signal for sorting from recycling endosomes; interaction with ACAP1By similarity6
Regioni786 – 793Interaction 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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P49134

KEGG Orthology (KO)

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KOi
K05719

Database of Orthologous Groups

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OrthoDBi
473040at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P49134

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

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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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P49134-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLQLVFWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN
60 70 80 90 100
TTFLQEGMPT SARCDDLEAL KKKGCHPSDI 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 ENQLKLNPLG
460 470 480 490 500
FTEEVEVVLQ FICKCNCQSH GIPASPKCHE GNGTFECGAC RCNEGRVGRH
510 520 530 540 550
CECSTDEVNS EDMDAYCRKE NSSEICSNNG ECVCGQCVCR KRENTNEIYS
560 570 580 590 600
GKFCECDNFN CDRSNGLICG GNGVCRCRVC ECYPNYTGSA CDCSLDTVPC
610 620 630 640 650
VATNGQICNG RGICECGACK CTDPKFQGPT CETCQTCLGV CAEHKECVQC
660 670 680 690 700
RAFNKGEKKD TCAQECSHFN LTKVESREKL PQPVQVDPVT HCKEKDIDDC
710 720 730 740 750
WFYFTYSVNS KGEAHVHVVE TPDCPTGPDI IPIVAGVVAG IVLIGLALLL
760 770 780 790
IWKLLMIIHD RREFAKFEKE KMNAKWDTGE NPIYKSAVTT VVNPKYEGK
Length:799
Mass (Da):88,495
Last modified:February 1, 1996 - 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:iF4475202EB8A3EA6
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSK5A0A0G2JSK5_RAT
Integrin beta
Itgb1 rCG_50886
798Annotation 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>

<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 AAI31846 differs from that shown. Reason: Frameshift.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 conflicti76H → Q in AAI31846 (PubMed:15489334).Curated1
Sequence conflicti711K → N in AAI31846 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U12309 mRNA Translation: AAA86669.1
BC131845 mRNA Translation: AAI31846.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4126

NCBI Reference Sequences

More...
RefSeqi
NP_058718.2, NM_017022.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24511

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24511

UCSC genome browser

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UCSCi
RGD:2927, rat

<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
U12309 mRNA Translation: AAA86669.1
BC131845 mRNA Translation: AAI31846.1 Frameshift.
PIRiJC4126
RefSeqiNP_058718.2, NM_017022.2

3D structure databases

SMRiP49134
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi246668, 7 interactors
CORUMiP49134
IntActiP49134, 4 interactors
MINTiP49134
STRINGi10116.ENSRNOP00000014785

PTM databases

GlyGeniP49134, 12 sites
iPTMnetiP49134
PhosphoSitePlusiP49134

Proteomic databases

jPOSTiP49134
PaxDbiP49134
PRIDEiP49134

Genome annotation databases

GeneIDi24511
KEGGirno:24511
UCSCiRGD:2927, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3688
RGDi2927, Itgb1

Phylogenomic databases

eggNOGiKOG1226, Eukaryota
InParanoidiP49134
KOiK05719
OrthoDBi473040at2759
PhylomeDBiP49134
TreeFamiTF105392

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P49134

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_RAT
<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: P49134
Secondary accession number(s): A2RRT8
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: August 12, 2020
This is version 184 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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