Aliases for ITGB1 Gene
External Ids for ITGB1 Gene
Previous HGNC Symbols for ITGB1 Gene
Previous GeneCards Identifiers for ITGB1 Gene
Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. This gene encodes a beta subunit. Multiple alternatively spliced transcript variants which encode different protein isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for ITGB1 Gene
ITGB1 (Integrin, Beta 1 (Fibronectin Receptor, Beta Polypeptide, Antigen CD29 Includes MDF2, MSK12)) is a Protein Coding gene. Diseases associated with ITGB1 include fraser syndrome and cerebral hypoxia. Among its related pathways are PI3K-Akt signaling pathway and Immune System. GO annotations related to this gene include protein heterodimerization activity and receptor binding. An important paralog of this gene is ITGB4.
UniProtKB/Swiss-Prot for ITGB1 Gene
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 GNB2L1/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.
Isoform 5: Isoform 5 displaces isoform 1 in striated muscles.
(Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for human echoviruses 1 and 8 (PubMed:8411387). Acts as a receptor for cytomegalovirus/HHV-5 (PubMed:20660204). Acts as a receptor for Epstein-Barr virus/HHV-4 (PubMed:17945327). Integrin ITGA5:ITGB1 acts as a receptor for human parvovirus B19 (PubMed:12907437). Integrin ITGA2:ITGB1 acts as a receptor for human rotavirus (PubMed:12941907). Acts as a receptor for mammalian reovirus (PubMed:16501085). In case of HIV-1 infection, integrin ITGA5:ITGB1 binding to extracellular viral Tat protein seems to enhance angiogenesis in Kaposis sarcoma lesions (PubMed:10397733).
Integrins are ubiquitously expressed adhesion molecules. They are cell-surface receptors that exist as heterodimers of alpha and beta subunits. Under physiological conditions, integrins are highly glycosylated and contain a Ca2+ or Mg2+ ion, which is essential for ligand binding.