ITGB1 / CD29 Immunizing Blocking Peptide

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]

ITGB1: an integral membrane protein that heterodimerizes with an alpha-3 chain, forming a receptor for many extracellular-matrix proteins including fibronectin, laminin, collagen, epiligrin and thrombospondin. . Beta 1 integrins recognize the amino-acid motif RGD in a wide array of ligands. Five alternatively spliced variants with alternate carboxy termini have been described. Two alternatively spliced isoforms have been described. Isoform beta-1a is widely expressed; other isoforms are generally expressed with a more restricted distribution. Isoform beta-1b is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoforms beta-1c and beta-1c-2 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 beta-c-2, rather than isoform beta-1c, is selectively expressed in primary t-cells. Isoform beta-1c is expressed in nonproliferating and differentiated prostate gland epithelial cells. Isoform beta-1d is expressed specifically in striated muscle (skeletal and cardiac muscle).

Protein type: Motility/polarity/chemotaxis; Receptor, misc.; Membrane protein, integral; Cell surface; Cell adhesion

Chromosomal Location of Human Ortholog: 10p11.2

Cellular Component: acrosome; basement membrane; cell surface; cleavage furrow; cytoplasm; dendritic spine; external side of plasma membrane; filopodium; focal adhesion; hemidesmosome; integrin complex; lamellipodium; lipid raft; melanosome; membrane; neuromuscular junction; perinuclear region of cytoplasm; plasma membrane; receptor complex; recycling endosome; ruffle; sarcolemma

Molecular Function: actin binding; alpha-actinin binding; C-X3-C chemokine binding; cell adhesion molecule binding; coreceptor activity; fibronectin binding; glycoprotein binding; integrin binding; laminin binding; metal ion binding; peptide binding; protease binding; protein binding; protein complex binding; protein domain specific binding; protein heterodimerization activity; protein kinase binding; viral receptor activity

Biological Process: axon extension; B cell differentiation; calcium-independent cell-matrix adhesion; cardiac muscle cell differentiation; cell fate specification; cell migration; cell migration during sprouting angiogenesis; cell-cell adhesion mediated by integrin; cell-matrix adhesion; cell-substrate adhesion; cellular calcium ion homeostasis; cellular defense response; dendrite morphogenesis; entry of virus into host cell; extracellular matrix organization and biogenesis; formation of radial glial scaffolds; G1/S transition of mitotic cell cycle; germ cell migration; heterotypic cell-cell adhesion; homophilic cell adhesion; in utero embryonic development; integrin-mediated signaling pathway; leukocyte adhesion; leukocyte migration; leukocyte tethering or rolling; maternal process involved in pregnancy; mesodermal cell differentiation; negative regulation of cell projection organization and biogenesis; negative regulation of cell proliferation; negative regulation of neuron differentiation; negative regulation of Rho protein signal transduction; positive regulation of apoptosis; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of endocytosis; positive regulation of GTPase activity; positive regulation of MAPKKK cascade; positive regulation of peptidyl-tyrosine phosphorylation; protein transport within lipid bilayer; receptor internalization; regulation of cell cycle; regulation of G-protein coupled receptor protein signaling pathway; regulation of immune response; response to activity; response to drug; sarcomere organization; stress fiber formation; tissue homeostasis; transforming growth factor beta receptor signaling pathway; visual learning