Integrin beta-1 (ITGB1)
The protein contains 798 amino acids for an estimated molecular weight of 88415 Da.
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 (By similarity). 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. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compa (updated: Feb. 10, 2021)
Protein identification was indicated in the following studies:
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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Biological Process
Axon extension
B cell differentiation
Basement membrane organization
Calcium-independent cell-matrix adhesion
Cardiac muscle cell differentiation
CD40 signaling pathway
Cell adhesion
Cell adhesion mediated by integrin
Cell fate specification
Cell migration
Cell migration involved in sprouting angiogenesis
Cell projection organization
Cell-cell adhesion mediated by integrin
Cell-matrix adhesion
Cell-substrate adhesion
Cellular defense response
Cellular response to low-density lipoprotein particle stimulus
Cytokine-mediated signaling pathway
Dendrite morphogenesis
Establishment of mitotic spindle orientation
Extracellular matrix organization
Formation of radial glial scaffolds
G1/S transition of mitotic cell cycle
Germ cell migration
Heterotypic cell-cell adhesion
Homophilic cell adhesion via plasma membrane adhesion molecules
In utero embryonic development
Integrin-mediated signaling pathway
Lamellipodium assembly
Leukocyte cell-cell adhesion
Leukocyte migration
Leukocyte tethering or rolling
Maintenance of blood-brain barrier
Mesodermal cell differentiation
Negative regulation of anoikis
Negative regulation of cell differentiation
Negative regulation of Rho protein signal transduction
Phagocytosis
Positive regulation of angiogenesis
Positive regulation of apoptotic process
Positive regulation of cell migration
Positive regulation of cell population proliferation
Positive regulation of fibroblast migration
Positive regulation of glutamate uptake involved in transmission of nerve impulse
Positive regulation of GTPase activity
Positive regulation of protein kinase B signaling
Positive regulation of protein localization to plasma membrane
Positive regulation of signaling receptor activity
Positive regulation of wound healing
Reactive gliosis
Receptor internalization
Regulation of cell cycle
Regulation of collagen catabolic process
Regulation of immune response
Regulation of inward rectifier potassium channel activity
Regulation of spontaneous synaptic transmission
Sarcomere organization
Viral entry into host cell
Viral life cycle
Visual learning
Cellular Component
Cell surface
Cleavage furrow
Cytoplasm
Dendritic spine
Endosome membrane
External side of plasma membrane
Extracellular exosome
Filopodium
Focal adhesion
Glial cell projection
Glutamatergic synapse
Integral component of synaptic membrane
Integrin alpha1-beta1 complex
Integrin alpha10-beta1 complex
Integrin alpha11-beta1 complex
Integrin alpha2-beta1 complex
Integrin alpha3-beta1 complex
Integrin alpha4-beta1 complex
Integrin alpha5-beta1 complex
Integrin alpha7-beta1 complex
Integrin alpha8-beta1 complex
Intercalated disc
Invadopodium membrane
Lamellipodium
Melanosome
Membrane
Membrane raft
Myelin sheath abaxonal region
Neuromuscular junction
Obsolete cell
Perinuclear region of cytoplasm
Plasma membrane
Protein-containing complex
Receptor complex
Recycling endosome
Ruffle
Ruffle membrane
Sarcolemma
Schaffer collateral - CA1 synapse
Molecular Function
Actin binding
Cadherin binding
Cell adhesion molecule binding
Collagen binding involved in cell-matrix adhesion
Coreceptor activity
Fibronectin binding
Integrin binding
Laminin binding
Metal ion binding
Protease binding
Protein heterodimerization activity
Protein tyrosine kinase binding
Protein-containing complex binding
Virus receptor activity
The reference OMIM entry for this protein is 135630
Integrin, beta-1; itgb1
Glycoprotein iia
Gp iia
Fibronectin receptor, beta subunit; fnrb
Very late activation protein, beta polypeptide
Vla-beta; vlab
Cd29
GENE FAMILY
Fibronectin receptors contain a beta subunit that appears to be analogous to band-3 of integrin (Pytela et al., 1986; Johansson et al., 1987). Hynes (1987) proposed that there are 3 subfamilies within the family of human adhesion protein receptor heterodimers based upon the number of different beta subunits. The other 2 subfamilies are the platelet and the endothelial cell heterodimers, which use GP IIIa (ITGB3; 173470), and the leukocyte heterodimers, which contain a 95,000 Da beta subunit that is homologous to GP IIIa but is clearly a different protein (ITGB2; 600065).GENE FUNCTION
Arregui et al. (2000) demonstrated that cell-permeable (Trojan) peptides containing the third helix of the antennapedia homeodomain fused to a peptide mimicking the juxtamembrane (JMP) region of the cytoplasmic domain of N-cadherin (CDH2; 114020) result in the inhibition of both CDH2 and ITGB1 function. Microscopic analysis showed that expression of JMP, which binds to the cytoplasmic domain of CDH2, results in a reduction of neurite outgrowth on cadherin substrates. Treatment of cells with JMP resulted in the release of FER (176942) from the cadherin complex and its accumulation in the integrin complex. The accumulation of FER in the integrin complex and the inhibitory effects of JMP could be reversed with a peptide that mimics the first coiled-coil domain of FER. The results suggested that FER mediates crosstalk between CDH2 and ITGB1. Human herpesvirus-8 (HHV-8) is implicated in the pathogenesis of Kaposi sarcoma. HHV-8 envelope glycoprotein B possesses the RGD amino acid motif known to interact with integrin molecules. Akula et al. (2002) found that HHV-8 infectivity was inhibited by RGD peptides, antibodies against the RGD-dependent integrins ITGA3 (605025) and ITGB1, and by soluble ITGA3/ITGB1. Expression of human ITGA3 increased the infectivity of virus for Chinese hamster ovary cells. Anti-glycoprotein B antibodies immunoprecipitated the virus-ITGA3 and -ITGB1 complexes, and virus-binding studies suggested a role for ITGA3/ITGB1 in HHV-8 entry. Further, HHV-8 infection induced the integrin-mediated activation of focal adhesion kinase (FAK; 600758). These findings implicated a role for ITGA3/ITGB1 and the associated signaling pathways in HHV-8 entry into target cells. Lu and Cyster (2002) studied the mechanisms that control localization of marginal zone B cells. They demonstrated that marginal zone B cells express elevated levels of the integrins LFA1 (see 153370) and alpha-4 (192975)-beta-1, and that the marginal zone B cells bind to the ligands ICAM1 (147840) and VCAM1 (192225). These ligands are expressed within the marginal zone in a lymphotoxin-dependent manner. Combined inhibition of LFA1 and alpha-4-beta-1 causes a rapid and selective release of B cells from the marginal zone. Furthermore, lipopolysaccharide-triggered marginal zone B cell relocalization involves downregulation of integrin-mediated adhesion. Lu and Cyster (2002) concluded that their studies identified key requirements for marginal zone B cell localization and established a role for integrins in peripheral lymphoid tissue compartmentalization. By examining the cation dependence of JAM2 (606870) adhesion to a T-cell line, Cunningham et al. (2002) identified a manganese-enhanced binding component indicative of integrin involvement. Using neutralizing integrin antibodies, they showed that the manganese-enhanced binding component was due to an inte ... More on the omim web site
Feb. 16, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 135630 was added.
Nov. 16, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).