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UniProtKB - B0FYY4 (ITB1_SHEEP)

Entry version 89 (10 Feb 2021)
Sequence version 1 (26 Feb 2008)
Previous versions | rss
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Protein

Integrin beta-1

Gene

ITGB1

Organism
Ovis aries (Sheep)
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
Metal bindingi362Calcium 1; via carbonyl oxygenBy 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

<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-1By similarity
Alternative name(s):
Fibronectin receptor subunit betaBy similarity
Integrin subunit beta-1Imported
VLA-4 subunit beta
CD_antigen: CD29By similarity
<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:ITGB1By similarity
<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>OrganismiOvis aries (Sheep)
<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 identifieri9940 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis
<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
  • UP000002356 <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

<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 – 246ExtracellularSequence analysisAdd BLAST226
<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>Transmembranei247 – 267HelicalSequence analysisAdd BLAST21
Topological domaini268 – 273CytoplasmicSequence analysis6

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 – 20Sequence analysisAdd 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_000035511821 – 798Integrin beta-1Sequence analysisAdd 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%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
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...) 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 residuei777PhosphothreonineBy similarity1
Modified residuei783PhosphotyrosineBy similarity1
Modified residuei785PhosphoserineBy similarity1
Modified residuei789PhosphothreonineBy similarity1
Modified residuei794N6-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-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%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

<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. ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion. 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.

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). ITGA5:ITGB1 interacts with ACE2 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9940.ENSOARP00000018925

<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

Biological Magnetic Resonance Data Bank

More...BMRBi		B0FYY4

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

<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 – 378VWFASequence analysisAdd 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 – 515ISequence analysisAdd BLAST50
Repeati516 – 559IISequence analysisAdd BLAST44
Repeati560 – 598IIISequence analysisAdd BLAST39
Repeati599 – 635IVSequence analysisAdd 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 repeatsSequence analysisAdd 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.Sequence analysis

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1226, Eukaryota

Database of Orthologous Groups

More...OrthoDBi		473040at2759

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%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>Sequencei

<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.

B0FYY4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLQLIFWIG LISSVCCVFG QADENRCLKA NAKSCGECIQ AGPNCGWCTN 
        60         70         80         90        100
STFLQEGMPT SARCDDLEAL KKKGCHPNDI ENPRGSKDIK KNKNVTNRSK 
       110        120        130        140        150
GTAEKLQPED ITQIQPQQLV LQLRSGEPQT FTLKFKRAED YPIDLYYLMD 
       160        170        180        190        200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP 
       210        220        230        240        250
AKLRNPCTNE QNCTSPFSYK NVLSLTDKGE VFNELVGKQR ISGNLDSPEG 
       260        270        280        290        300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 
       310        320        330        340        350
CHLENDMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN 
       360        370        380        390        400
LIPKSAVGTL SANSGNVIQL IIDAYNSLSS EVILENSKLP EGVTINYKSY 
       410        420        430        440        450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TANKCPNKNS ETIKIKPLGF 
       460        470        480        490        500
TEEVEIILQF ICECECQSEG IPGSPKCHDG NGTFECGACR CNEGRVGRHC 
       510        520        530        540        550
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG 
       560        570        580        590        600
KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTTSCM 
       610        620        630        640        650
AVNGQICNGR GVCECGACKC TDPKFQGPTC EMCQTCLGVC AEHKECVQCR 
       660        670        680        690        700
AFNKGEKKDT CAQECSHFNI TKVENRDKLP QPGQVDPLSH CKEKDVDDCW 
       710        720        730        740        750
FYFTYSVNGN NEATVHVVET PECPTGPDII PIVAGVVAGI VLIGPALLLI 
       760        770        780        790 
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
Length:798
Mass (Da):88,110
Last modified:February 26, 2008 - 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:iC8543466755D38BC
GO

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
EU367988 mRNA Translation: ABY71046.1

NCBI Reference Sequences

More...RefSeqi		NP_001107242.1, NM_001113770.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		443141

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		oas:443141

<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
EU367988 mRNA Translation: ABY71046.1
RefSeqiNP_001107242.1, NM_001113770.1

3D structure databases

BMRBiB0FYY4
ModBaseiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Protein-protein interaction databases

STRINGi9940.ENSOARP00000018925

Genome annotation databases

GeneIDi443141
KEGGioas:443141

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3688

Phylogenomic databases

eggNOGiKOG1226, Eukaryota
OrthoDBi473040at2759

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_SHEEP
<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: B0FYY4
<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: November 25, 2008
Last sequence update: February 26, 2008
Last modified: February 10, 2021
This is version 89 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
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