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 - P05556 (ITB1_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Integrin beta-1

Gene

ITGB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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-4/beta-1 is a receptor for VCAM1. It 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. 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. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). 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. 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. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). 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 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881).13 Publications
Isoform 5: Isoform 5 displaces isoform 1 in striated muscles.By similarity
(Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8.1 Publication
(Microbial infection) Acts as a receptor for Cytomegalovirus/HHV-5.1 Publication
(Microbial infection) Acts as a receptor for Epstein-Barr virus/HHV-4.1 Publication
(Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human parvovirus B19.1 Publication
(Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus.1 Publication
(Microbial infection) Acts as a receptor for Mammalian reovirus.1 Publication
(Microbial infection) In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi152Magnesium1
Metal bindingi154Calcium 1; via carbonyl oxygen1
Metal bindingi156Calcium 11
Metal bindingi157Calcium 11
Metal bindingi189Calcium 21
Metal bindingi244Calcium 21
Metal bindingi246Calcium 21
Metal bindingi248Calcium 2; via carbonyl oxygen1
Metal bindingi249Calcium 21
Metal bindingi249Magnesium1
Metal bindingi362Calcium 1; via carbonyl oxygen1

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cell adhesion molecule binding Source: UniProtKB
  • collagen binding involved in cell-matrix adhesion Source: UniProtKB
  • coreceptor activity Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • integrin binding Source: Ensembl
  • laminin binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • protease binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • axon extension Source: Ensembl
  • basement membrane organization Source: Ensembl
  • B cell differentiation Source: BHF-UCL
  • calcium-independent cell-matrix adhesion Source: MGI
  • cardiac muscle cell differentiation Source: Ensembl
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-cell adhesion mediated by integrin Source: BHF-UCL
  • cell fate specification Source: Ensembl
  • cell-matrix adhesion Source: UniProtKB
  • cell migration Source: HGNC
  • cell migration involved in sprouting angiogenesis Source: Ensembl
  • cell-substrate adhesion Source: UniProtKB
  • cellular defense response Source: ProtInc
  • cellular response to low-density lipoprotein particle stimulus Source: UniProtKB
  • cytokine-mediated signaling pathway Source: Reactome
  • dendrite morphogenesis Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • formation of radial glial scaffolds Source: Ensembl
  • G1/S transition of mitotic cell cycle Source: Ensembl
  • germ cell migration Source: Ensembl
  • heterotypic cell-cell adhesion Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: ProtInc
  • integrin-mediated signaling pathway Source: UniProtKB
  • in utero embryonic development Source: Ensembl
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • leukocyte migration Source: Reactome
  • leukocyte tethering or rolling Source: UniProtKB
  • mesodermal cell differentiation Source: UniProtKB
  • negative regulation of anoikis Source: UniProtKB
  • negative regulation of cell differentiation Source: Ensembl
  • negative regulation of Rho protein signal transduction Source: Ensembl
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of GTPase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: BHF-UCL
  • positive regulation of protein localization to plasma membrane Source: UniProtKB
  • positive regulation of receptor activity Source: BHF-UCL
  • receptor internalization Source: UniProtKB
  • regulation of cell cycle Source: Ensembl
  • regulation of collagen catabolic process Source: UniProtKB
  • regulation of immune response Source: Reactome
  • sarcomere organization Source: Ensembl
  • visual learning Source: Ensembl
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHost cell receptor for virus entry, Integrin, Receptor
Biological processCell adhesion, Host-virus interaction
LigandCalcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1566948. Elastic fibre formation.
R-HSA-1566977. Fibronectin matrix formation.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-210991. Basigin interactions.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000157. Laminin interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-416700. Other semaphorin interactions.
R-HSA-445144. Signal transduction by L1.
R-HSA-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-HSA-447041. CHL1 interactions.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6785807. Interleukin-4 and 13 signaling.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-8874081. MET activates PTK2 signaling.
R-HSA-8875513. MET interacts with TNS proteins.
SABIO-RKiP05556.
SignaLinkiP05556.
SIGNORiP05556.

Protein family/group databases

TCDBi9.B.87.1.8. the selenoprotein p receptor (selp-receptor) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-1
Alternative name(s):
Fibronectin receptor subunit beta
Glycoprotein IIa
Short name:
GPIIA
VLA-4 subunit beta
CD_antigen: CD29
Gene namesi
Name:ITGB1
Synonyms:FNRB, MDF2, MSK12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000150093.18.
HGNCiHGNC:6153. ITGB1.
MIMi135630. gene.
neXtProtiNX_P05556.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 728ExtracellularSequence analysisAdd BLAST708
Transmembranei729 – 751HelicalSequence analysisAdd BLAST23
Topological domaini752 – 798CytoplasmicSequence analysisAdd BLAST47

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi760 – 761RR → AA: No effect on interaction with ACAP1. 1 Publication2
Mutagenesisi762 – 767EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5. 1 Publication6
Mutagenesisi762 – 763EF → AA: Slightly reduces interaction with ACAP1. 2
Mutagenesisi765K → A: Reduces interaction with ACAP1. 1
Mutagenesisi766 – 767FE → AA: Slightly reduces interaction with ACAP1. 2
Mutagenesisi768 – 769KE → AA: No effect on interaction with ACAP1. 1 Publication2
Mutagenesisi778G → Q: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication1
Mutagenesisi786 – 791AVTTVV → PINNFK: Does not interact with ITGB1BP1. 1 Publication6
Mutagenesisi786A → P: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication1
Mutagenesisi787V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. 1 Publication1
Mutagenesisi788T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. 1 Publication1
Mutagenesisi790V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. 1 Publication1
Mutagenesisi792N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. 1 Publication1
Mutagenesisi795Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. 1 Publication1

Organism-specific databases

DisGeNETi3688.
OpenTargetsiENSG00000150093.
PharmGKBiPA29953.

Chemistry databases

ChEMBLiCHEMBL1905.
DrugBankiDB00098. Anti-thymocyte Globulin (Rabbit).
GuidetoPHARMACOLOGYi2455.

Polymorphism and mutation databases

BioMutaiITGB1.
DMDMi218563324.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000001633421 – 798Integrin beta-1Add BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 451 Publication
Disulfide bondi35 ↔ 4641 Publication
Disulfide bondi38 ↔ 641 Publication
Disulfide bondi48 ↔ 751 Publication
Glycosylationi50N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi97N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi207 ↔ 2131 Publication
Glycosylationi212N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi261 ↔ 3011 Publication
Glycosylationi269N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi363N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi401 ↔ 4151 Publication
Glycosylationi403N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi406N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi411N-linked (GlcNAc...) asparagine; atypical1 Publication1
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 4621 Publication
Disulfide bondi466 ↔ 6911 Publication
Disulfide bondi477 ↔ 489By similarity
Glycosylationi481N-linked (GlcNAc...) asparagine1 Publication1
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
Modified residuei777PhosphothreonineCombined sources1
Modified residuei783PhosphotyrosineCombined sources1
Modified residuei785PhosphoserineCombined sources1
Modified residuei789PhosphothreonineCombined sources1
Modified residuei794N6-acetyllysine; alternateCombined sources1
Cross-linki794Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources

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

EPDiP05556.
MaxQBiP05556.
PaxDbiP05556.
PeptideAtlasiP05556.
PRIDEiP05556.

PTM databases

iPTMnetiP05556.
PhosphoSitePlusiP05556.
SwissPalmiP05556.
UniCarbKBiP05556.

Miscellaneous databases

PMAP-CutDBiQ8WUM6.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle).6 Publications

Gene expression databases

BgeeiENSG00000150093.
ExpressionAtlasiP05556. baseline and differential.
GenevisibleiP05556. HS.

Organism-specific databases

HPAiCAB003434.

Interactioni

Subunit structurei

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. Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FGR and HCK. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with RAB21. 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 FLNA, FLNB and RANBP9. Isoform 5 interacts with ACE2. Isoform 1 interacts with the C-terminal region of FLNC. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. 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. Isoform 5 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 5 interacts with alpha-7B in cardiomyocytes of adult heart. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has an heterodimer form (By similarity). ITGA5:ITGB1 interacts with NOV. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415). ITGA5:ITGB1 interacts with FBN1 (PubMed:12807887, PubMed:17158881).By similarity26 Publications
(Microbial infection) Integrin ITGA2:ITGB1 interacts with human echoviruses 1 and 8 capsid proteins.1 Publication
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB.1 Publication
(Microbial infection) Interacts with Epstein-Barr virus/HHV-4 gB protein.1 Publication
(Microbial infection) Integrin ITGA5:ITGB1 interacts with human parvovirus B19 capsid protein.1 Publication
(Microbial infection) Integrin ITGA2:ITGB1 interacts with human rotavirus VP4 protein.1 Publication
(Microbial infection) Interacts with mammalian reovirus capsid proteins.1 Publication
(Microbial infection) Integrin ITGA5:ITGB1 interacts with HIV-1 Tat.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • cell adhesion molecule binding Source: UniProtKB
  • collagen binding involved in cell-matrix adhesion Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • integrin binding Source: Ensembl
  • laminin binding Source: Ensembl
  • protease binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109894. 99 interactors.
CORUMiP05556.
DIPiDIP-312N.
ELMiP05556.
IntActiP05556. 74 interactors.
MINTiP05556.
STRINGi9606.ENSP00000303351.

Chemistry databases

BindingDBiP05556.

Structurei

Secondary structure

1798
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni26 – 31Combined sources6
Helixi35 – 40Combined sources6
Beta strandi45 – 47Combined sources3
Helixi61 – 63Combined sources3
Beta strandi64 – 66Combined sources3
Helixi67 – 71Combined sources5
Turni72 – 74Combined sources3
Turni77 – 79Combined sources3
Beta strandi86 – 91Combined sources6
Helixi108 – 110Combined sources3
Beta strandi118 – 124Combined sources7
Beta strandi129 – 136Combined sources8
Beta strandi143 – 150Combined sources8
Helixi153 – 155Combined sources3
Helixi156 – 161Combined sources6
Helixi162 – 164Combined sources3
Helixi165 – 173Combined sources9
Turni174 – 176Combined sources3
Beta strandi180 – 187Combined sources8
Turni193 – 195Combined sources3
Helixi200 – 204Combined sources5
Beta strandi209 – 211Combined sources3
Beta strandi218 – 227Combined sources10
Helixi229 – 236Combined sources8
Beta strandi245 – 249Combined sources5
Helixi251 – 260Combined sources10
Helixi262 – 264Combined sources3
Beta strandi269 – 280Combined sources12
Helixi287 – 291Combined sources5
Turni311 – 313Combined sources3
Helixi319 – 328Combined sources10
Beta strandi331 – 337Combined sources7
Helixi339 – 341Combined sources3
Helixi342 – 351Combined sources10
Beta strandi352 – 359Combined sources8
Beta strandi362 – 364Combined sources3
Helixi367 – 379Combined sources13
Beta strandi382 – 386Combined sources5
Beta strandi393 – 400Combined sources8
Helixi402 – 404Combined sources3
Beta strandi406 – 408Combined sources3
Helixi409 – 413Combined sources5
Beta strandi423 – 432Combined sources10
Beta strandi437 – 439Combined sources3
Beta strandi441 – 447Combined sources7
Beta strandi454 – 461Combined sources8
Helixi752 – 769Combined sources18
Helixi770 – 772Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K11model-B786-797[»]
1LHAmodel-A86-543[»]
3G9WX-ray2.16C/D752-785[»]
3T9KX-ray2.30A/B758-769[»]
3VI3X-ray2.90B/D21-465[»]
3VI4X-ray2.90B/D21-465[»]
4DX9X-ray3.006/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z784-798[»]
4WJKX-ray1.85B21-465[»]
4WK0X-ray1.78B21-465[»]
4WK2X-ray2.50B21-465[»]
4WK4X-ray2.50B21-465[»]
ProteinModelPortaliP05556.
SMRiP05556.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05556.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 378VWFAAdd BLAST239
Repeati466 – 515IAdd BLAST50
Repeati516 – 559IIAdd BLAST44
Repeati560 – 598IIIAdd BLAST39
Repeati599 – 635IVAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 213CX3CL1-binding1 Publication7
Regioni295 – 314CX3CL1-binding1 PublicationAdd BLAST20
Regioni466 – 635Cysteine-rich tandem repeatsAdd BLAST170
Regioni762 – 767Signal for sorting from recycling endosomes; interaction with ACAP16
Regioni785 – 792Interaction with ITGB1BP18

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOVERGENiHBG006190.
InParanoidiP05556.
KOiK05719.
OMAiNVYTMSH.
OrthoDBiEOG091G029W.
PhylomeDBiP05556.
TreeFamiTF105392.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiView protein in InterPro
IPR013111. EGF_extracell.
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.
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.

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05556-1) [UniParc]FASTAAdd to basket
Also known as: Beta-1A

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

« Hide

        10         20         30         40         50
MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN 
        60         70         80         90        100
STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK 
       110        120        130        140        150
GTAEKLKPED ITQIQPQQLV LRLRSGEPQT FTLKFKRAED YPIDLYYLMD 
       160        170        180        190        200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP 
       210        220        230        240        250
AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR ISGNLDSPEG 
       260        270        280        290        300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 
       310        320        330        340        350
CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN 
       360        370        380        390        400
LIPKSAVGTL SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY 
       410        420        430        440        450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TSNKCPKKDS DSFKIRPLGF 
       460        470        480        490        500
TEEVEVILQY ICECECQSEG IPESPKCHEG NGTFECGACR CNEGRVGRHC 
       510        520        530        540        550
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG 
       560        570        580        590        600
KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE 
       610        620        630        640        650
ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR 
       660        670        680        690        700
AFNKGEKKDT CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW 
       710        720        730        740        750
FYFTYSVNGN NEVMVHVVEN PECPTGPDII PIVAGVVAGI VLIGLALLLI 
       760        770        780        790 
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
Length:798
Mass (Da):88,415
Last modified:December 16, 2008 - v2
Checksum:iDE35979C1625578C
GO
Isoform 2 (identifier: P05556-2) [UniParc]FASTAAdd to basket
Also known as: Beta-1B

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → VSYKTSKKQSGL

Show »
Length:789
Mass (Da):87,446
Checksum:i75834A92490CFBB0
GO
Isoform 3 (identifier: P05556-3) [UniParc]FASTAAdd to basket
Also known as: Beta-1C

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → SLSVAQPGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

Show »
Length:825
Mass (Da):91,620
Checksum:iD5DCB510A049FBEC
GO
Isoform 4 (identifier: P05556-4) [UniParc]FASTAAdd to basket
Also known as: Beta-1C-2

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → PGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

Show »
Length:819
Mass (Da):91,034
Checksum:i5838866B6DA6CECC
GO
Isoform 5 (identifier: P05556-5) [UniParc]FASTAAdd to basket
Also known as: Beta-1D

The sequence of this isoform differs from the canonical sequence as follows:
     778-798: GENPIYKSAVTTVVNPKYEGK → QENPIYKSPINNFKNPNYGRKAGL

Show »
Length:801
Mass (Da):88,884
Checksum:i5A2DA413650A16BE
GO

Sequence cautioni

The sequence CAD97649 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112T → H in CAA30790 (PubMed:2958481).Curated1
Sequence conflicti215S → T in CAA30790 (PubMed:2958481).Curated1
Sequence conflicti261 – 265CGSLI → VWMLL in AAI13902 (PubMed:15489334).Curated5
Sequence conflicti385 – 386EN → DG in AAI13902 (PubMed:15489334).Curated2
Sequence conflicti463E → V in BAF84386 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002741778 – 798GENPI…KYEGK → VSYKTSKKQSGL in isoform 2. CuratedAdd BLAST21
Alternative sequenceiVSP_002742778 – 798GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3. CuratedAdd BLAST21
Alternative sequenceiVSP_002743778 – 798GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4. CuratedAdd BLAST21
Alternative sequenceiVSP_002744778 – 798GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5. CuratedAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07979 mRNA. Translation: CAA30790.1.
AK291697 mRNA. Translation: BAF84386.1.
BX537407 mRNA. Translation: CAD97649.1. Different initiation.
AL365203 Genomic DNA. Translation: CAI14426.1.
CH471072 Genomic DNA. Translation: EAW85948.1.
CH471072 Genomic DNA. Translation: EAW85949.1.
CH471072 Genomic DNA. Translation: EAW85950.1.
CH471072 Genomic DNA. Translation: EAW85951.1.
CH471072 Genomic DNA. Translation: EAW85952.1.
CH471072 Genomic DNA. Translation: EAW85953.1.
CH471072 Genomic DNA. Translation: EAW85954.1.
CH471072 Genomic DNA. Translation: EAW85955.1.
CH471072 Genomic DNA. Translation: EAW85957.1.
CH471072 Genomic DNA. Translation: EAW85958.1.
CH471072 Genomic DNA. Translation: EAW85959.1.
BC020057 mRNA. Translation: AAH20057.1.
BC113901 mRNA. Translation: AAI13902.1.
U33879 Genomic DNA. Translation: AAA79832.1.
U33880, U33879 Genomic DNA. Translation: AAA79833.1.
U33882, U33879, U33881 Genomic DNA. Translation: AAA79834.1.
U33882, U33879 Genomic DNA. Translation: AAA79835.1.
M34189 mRNA. Translation: AAA59182.1.
M84237 mRNA. Translation: AAA74402.1.
M84237 mRNA. Translation: AAA74403.1.
U28252 mRNA. Translation: AAA81366.1.
CCDSiCCDS7174.1. [P05556-1]
PIRiB27079.
RefSeqiNP_002202.2. NM_002211.3. [P05556-1]
NP_391988.1. NM_033668.2. [P05556-5]
NP_596867.1. NM_133376.2. [P05556-1]
UniGeneiHs.643813.

Genome annotation databases

EnsembliENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
GeneIDi3688.
KEGGihsa:3688.
UCSCiuc001iwr.5. human. [P05556-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiITB1_HUMAN
AccessioniPrimary (citable) accession number: P05556
Secondary accession number(s): A8K6N2
, D3DRX9, D3DRY3, D3DRY4, D3DRY5, P78466, P78467, Q13089, Q13090, Q13091, Q13212, Q14622, Q14647, Q29RW2, Q7Z3V1, Q8WUM6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 16, 2008
Last modified: March 28, 2018
This is version 226 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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