UniProtKB - P05556 (ITB1_HUMAN)
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Protein
Integrin beta-1
Gene
ITGB1
Organism
Homo sapiens (Human)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 152 | Magnesium | 1 | |
Metal bindingi | 154 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 156 | Calcium 1 | 1 | |
Metal bindingi | 157 | Calcium 1 | 1 | |
Metal bindingi | 189 | Calcium 2 | 1 | |
Metal bindingi | 244 | Calcium 2 | 1 | |
Metal bindingi | 246 | Calcium 2 | 1 | |
Metal bindingi | 248 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 249 | Calcium 2 | 1 | |
Metal bindingi | 249 | Magnesium | 1 | |
Metal bindingi | 362 | Calcium 1; via carbonyl oxygen | 1 |
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
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
Keywordsi
Molecular function | Host cell receptor for virus entry, Integrin, Receptor |
Biological process | Cell adhesion, Host-virus interaction |
Ligand | Calcium, Magnesium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-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-RKi | P05556. |
SignaLinki | P05556. |
SIGNORi | P05556. |
Protein family/group databases
TCDBi | 9.B.87.1.8. the selenoprotein p receptor (selp-receptor) family. |
Names & Taxonomyi
Protein namesi | Recommended name: Integrin beta-1Alternative 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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000150093.18. |
HGNCi | HGNC:6153. ITGB1. |
MIMi | 135630. gene. |
neXtProti | NX_P05556. |
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 21 – 728 | ExtracellularSequence analysisAdd BLAST | 708 | |
Transmembranei | 729 – 751 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 752 – 798 | CytoplasmicSequence analysisAdd BLAST | 47 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Endosome, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 760 – 761 | RR → AA: No effect on interaction with ACAP1. 1 Publication | 2 | |
Mutagenesisi | 762 – 767 | EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5. 1 Publication | 6 | |
Mutagenesisi | 762 – 763 | EF → AA: Slightly reduces interaction with ACAP1. | 2 | |
Mutagenesisi | 765 | K → A: Reduces interaction with ACAP1. | 1 | |
Mutagenesisi | 766 – 767 | FE → AA: Slightly reduces interaction with ACAP1. | 2 | |
Mutagenesisi | 768 – 769 | KE → AA: No effect on interaction with ACAP1. 1 Publication | 2 | |
Mutagenesisi | 778 | G → Q: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication | 1 | |
Mutagenesisi | 786 – 791 | AVTTVV → PINNFK: Does not interact with ITGB1BP1. 1 Publication | 6 | |
Mutagenesisi | 786 | A → P: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication | 1 | |
Mutagenesisi | 787 | V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. 1 Publication | 1 | |
Mutagenesisi | 788 | T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. 1 Publication | 1 | |
Mutagenesisi | 790 | V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. 1 Publication | 1 | |
Mutagenesisi | 792 | N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. 1 Publication | 1 | |
Mutagenesisi | 795 | Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 3688. |
OpenTargetsi | ENSG00000150093. |
PharmGKBi | PA29953. |
Chemistry databases
ChEMBLi | CHEMBL1905. |
DrugBanki | DB00098. Anti-thymocyte Globulin (Rabbit). |
GuidetoPHARMACOLOGYi | 2455. |
Polymorphism and mutation databases
BioMutai | ITGB1. |
DMDMi | 218563324. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | Add BLAST | 20 | |
ChainiPRO_0000016334 | 21 – 798 | Integrin beta-1Add BLAST | 778 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 27 ↔ 45 | 1 Publication | ||
Disulfide bondi | 35 ↔ 464 | 1 Publication | ||
Disulfide bondi | 38 ↔ 64 | 1 Publication | ||
Disulfide bondi | 48 ↔ 75 | 1 Publication | ||
Glycosylationi | 50 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 94 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 97 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 207 ↔ 213 | 1 Publication | ||
Glycosylationi | 212 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 261 ↔ 301 | 1 Publication | ||
Glycosylationi | 269 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 363 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 401 ↔ 415 | 1 Publication | ||
Glycosylationi | 403 | N-linked (GlcNAc...) asparagine; atypical1 Publication | 1 | |
Glycosylationi | 406 | N-linked (GlcNAc...) asparagine3 Publications | 1 | |
Glycosylationi | 411 | N-linked (GlcNAc...) asparagine; atypical1 Publication | 1 | |
Glycosylationi | 417 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 435 ↔ 462 | 1 Publication | ||
Disulfide bondi | 466 ↔ 691 | 1 Publication | ||
Disulfide bondi | 477 ↔ 489 | By similarity | ||
Glycosylationi | 481 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 486 ↔ 525 | By similarity | ||
Disulfide bondi | 491 ↔ 500 | By similarity | ||
Disulfide bondi | 502 ↔ 516 | By similarity | ||
Glycosylationi | 520 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 531 ↔ 536 | By similarity | ||
Disulfide bondi | 533 ↔ 568 | By similarity | ||
Disulfide bondi | 538 ↔ 553 | By similarity | ||
Disulfide bondi | 555 ↔ 560 | By similarity | ||
Disulfide bondi | 574 ↔ 579 | By similarity | ||
Disulfide bondi | 576 ↔ 607 | By similarity | ||
Disulfide bondi | 581 ↔ 590 | By similarity | ||
Glycosylationi | 584 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 592 ↔ 599 | By similarity | ||
Disulfide bondi | 613 ↔ 618 | By similarity | ||
Disulfide bondi | 615 ↔ 661 | By similarity | ||
Disulfide bondi | 620 ↔ 630 | By similarity | ||
Disulfide bondi | 633 ↔ 636 | By similarity | ||
Disulfide bondi | 640 ↔ 649 | By similarity | ||
Disulfide bondi | 646 ↔ 723 | By similarity | ||
Disulfide bondi | 665 ↔ 699 | By similarity | ||
Glycosylationi | 669 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 777 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 783 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 785 | PhosphoserineCombined sources | 1 | |
Modified residuei | 789 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 794 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 794 | Glycyl 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 conjugationProteomic databases
EPDi | P05556. |
MaxQBi | P05556. |
PaxDbi | P05556. |
PeptideAtlasi | P05556. |
PRIDEi | P05556. |
PTM databases
iPTMneti | P05556. |
PhosphoSitePlusi | P05556. |
SwissPalmi | P05556. |
UniCarbKBi | P05556. |
Miscellaneous databases
PMAP-CutDBi | Q8WUM6. |
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
Bgeei | ENSG00000150093. |
ExpressionAtlasi | P05556. baseline and differential. |
Genevisiblei | P05556. HS. |
Organism-specific databases
HPAi | CAB003434. |
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
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
Protein-protein interaction databases
BioGridi | 109894. 99 interactors. |
CORUMi | P05556. |
DIPi | DIP-312N. |
ELMi | P05556. |
IntActi | P05556. 74 interactors. |
MINTi | P05556. |
STRINGi | 9606.ENSP00000303351. |
Chemistry databases
BindingDBi | P05556. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Turni | 26 – 31 | Combined sources | 6 | |
Helixi | 35 – 40 | Combined sources | 6 | |
Beta strandi | 45 – 47 | Combined sources | 3 | |
Helixi | 61 – 63 | Combined sources | 3 | |
Beta strandi | 64 – 66 | Combined sources | 3 | |
Helixi | 67 – 71 | Combined sources | 5 | |
Turni | 72 – 74 | Combined sources | 3 | |
Turni | 77 – 79 | Combined sources | 3 | |
Beta strandi | 86 – 91 | Combined sources | 6 | |
Helixi | 108 – 110 | Combined sources | 3 | |
Beta strandi | 118 – 124 | Combined sources | 7 | |
Beta strandi | 129 – 136 | Combined sources | 8 | |
Beta strandi | 143 – 150 | Combined sources | 8 | |
Helixi | 153 – 155 | Combined sources | 3 | |
Helixi | 156 – 161 | Combined sources | 6 | |
Helixi | 162 – 164 | Combined sources | 3 | |
Helixi | 165 – 173 | Combined sources | 9 | |
Turni | 174 – 176 | Combined sources | 3 | |
Beta strandi | 180 – 187 | Combined sources | 8 | |
Turni | 193 – 195 | Combined sources | 3 | |
Helixi | 200 – 204 | Combined sources | 5 | |
Beta strandi | 209 – 211 | Combined sources | 3 | |
Beta strandi | 218 – 227 | Combined sources | 10 | |
Helixi | 229 – 236 | Combined sources | 8 | |
Beta strandi | 245 – 249 | Combined sources | 5 | |
Helixi | 251 – 260 | Combined sources | 10 | |
Helixi | 262 – 264 | Combined sources | 3 | |
Beta strandi | 269 – 280 | Combined sources | 12 | |
Helixi | 287 – 291 | Combined sources | 5 | |
Turni | 311 – 313 | Combined sources | 3 | |
Helixi | 319 – 328 | Combined sources | 10 | |
Beta strandi | 331 – 337 | Combined sources | 7 | |
Helixi | 339 – 341 | Combined sources | 3 | |
Helixi | 342 – 351 | Combined sources | 10 | |
Beta strandi | 352 – 359 | Combined sources | 8 | |
Beta strandi | 362 – 364 | Combined sources | 3 | |
Helixi | 367 – 379 | Combined sources | 13 | |
Beta strandi | 382 – 386 | Combined sources | 5 | |
Beta strandi | 393 – 400 | Combined sources | 8 | |
Helixi | 402 – 404 | Combined sources | 3 | |
Beta strandi | 406 – 408 | Combined sources | 3 | |
Helixi | 409 – 413 | Combined sources | 5 | |
Beta strandi | 423 – 432 | Combined sources | 10 | |
Beta strandi | 437 – 439 | Combined sources | 3 | |
Beta strandi | 441 – 447 | Combined sources | 7 | |
Beta strandi | 454 – 461 | Combined sources | 8 | |
Helixi | 752 – 769 | Combined sources | 18 | |
Helixi | 770 – 772 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1K11 | model | - | B | 786-797 | [»] | |
1LHA | model | - | A | 86-543 | [»] | |
3G9W | X-ray | 2.16 | C/D | 752-785 | [»] | |
3T9K | X-ray | 2.30 | A/B | 758-769 | [»] | |
3VI3 | X-ray | 2.90 | B/D | 21-465 | [»] | |
3VI4 | X-ray | 2.90 | B/D | 21-465 | [»] | |
4DX9 | X-ray | 3.00 | 6/7/8/9/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/z | 784-798 | [»] | |
4WJK | X-ray | 1.85 | B | 21-465 | [»] | |
4WK0 | X-ray | 1.78 | B | 21-465 | [»] | |
4WK2 | X-ray | 2.50 | B | 21-465 | [»] | |
4WK4 | X-ray | 2.50 | B | 21-465 | [»] | |
ProteinModelPortali | P05556. | |||||
SMRi | P05556. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05556. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 140 – 378 | VWFAAdd BLAST | 239 | |
Repeati | 466 – 515 | IAdd BLAST | 50 | |
Repeati | 516 – 559 | IIAdd BLAST | 44 | |
Repeati | 560 – 598 | IIIAdd BLAST | 39 | |
Repeati | 599 – 635 | IVAdd BLAST | 37 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 207 – 213 | CX3CL1-binding1 Publication | 7 | |
Regioni | 295 – 314 | CX3CL1-binding1 PublicationAdd BLAST | 20 | |
Regioni | 466 – 635 | Cysteine-rich tandem repeatsAdd BLAST | 170 | |
Regioni | 762 – 767 | Signal for sorting from recycling endosomes; interaction with ACAP1 | 6 | |
Regioni | 785 – 792 | Interaction with ITGB1BP1 | 8 |
Sequence similaritiesi
Belongs to the integrin beta chain family.Curated
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1226. Eukaryota. ENOG410XP60. LUCA. |
GeneTreei | ENSGT00760000119064. |
HOVERGENi | HBG006190. |
InParanoidi | P05556. |
KOi | K05719. |
OMAi | NVYTMSH. |
OrthoDBi | EOG091G029W. |
PhylomeDBi | P05556. |
TreeFami | TF105392. |
Family and domain databases
Gene3Di | 3.40.50.410. 1 hit. |
InterProi | View 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. |
PANTHERi | PTHR10082. PTHR10082. 1 hit. PTHR10082:SF28. PTHR10082:SF28. 1 hit. |
Pfami | View 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. |
PIRSFi | PIRSF002512. Integrin_B. 1 hit. |
PRINTSi | PR01186. INTEGRINB. |
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. |
SUPFAMi | SSF53300. SSF53300. 1 hit. SSF69179. SSF69179. 1 hit. SSF69687. SSF69687. 1 hit. |
PROSITEi | View protein in PROSITE PS00022. EGF_1. 2 hits. PS00243. INTEGRIN_BETA. 3 hits. |
s (5)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 5 produced by isoformsialternative 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.
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
Sequence cautioni
The sequence CAD97649 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 112 | T → H in CAA30790 (PubMed:2958481).Curated | 1 | |
Sequence conflicti | 215 | S → T in CAA30790 (PubMed:2958481).Curated | 1 | |
Sequence conflicti | 261 – 265 | CGSLI → VWMLL in AAI13902 (PubMed:15489334).Curated | 5 | |
Sequence conflicti | 385 – 386 | EN → DG in AAI13902 (PubMed:15489334).Curated | 2 | |
Sequence conflicti | 463 | E → V in BAF84386 (PubMed:14702039).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_002741 | 778 – 798 | GENPI…KYEGK → VSYKTSKKQSGL in isoform 2. CuratedAdd BLAST | 21 | |
Alternative sequenceiVSP_002742 | 778 – 798 | GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3. CuratedAdd BLAST | 21 | |
Alternative sequenceiVSP_002743 | 778 – 798 | GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4. CuratedAdd BLAST | 21 | |
Alternative sequenceiVSP_002744 | 778 – 798 | GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5. CuratedAdd BLAST | 21 |
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. |
CCDSi | CCDS7174.1. [P05556-1] |
PIRi | B27079. |
RefSeqi | NP_002202.2. NM_002211.3. [P05556-1] NP_391988.1. NM_033668.2. [P05556-5] NP_596867.1. NM_133376.2. [P05556-1] |
UniGenei | Hs.643813. |
Genome annotation databases
Ensembli | ENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1] ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1] ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5] |
GeneIDi | 3688. |
KEGGi | hsa:3688. |
UCSCi | uc001iwr.5. human. [P05556-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | ITB1_HUMAN | |
Accessioni | P05556Primary (citable) accession number: P05556 Secondary accession number(s): A8K6N2 Q8WUM6 | |
Entry historyi | Integrated 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |