ITGB1
entrez
3688
canonical
uniprot
P05556
canonical
ensembl
ENSG00000150093
resolver
ensp
ENSP00000303351
resolver
ensp
ENSP00000379350
resolver
ensp
ENSP00000712557
resolver
genesymbol
ITGB1
resolver
genesymbol_syn
FNRB
resolver
genesymbol_syn
MDF2
resolver
genesymbol_syn
MSK12
resolver
hgnc
HGNC:6153
resolver
uniprot
A8K6N2
resolver
uniprot
D3DRX9
resolver
uniprot
D3DRY3
resolver
uniprot
D3DRY4
resolver
uniprot
D3DRY5
resolver
uniprot
P78466
resolver
uniprot
P78467
resolver
uniprot
Q13089
resolver
uniprot
Q13090
resolver
uniprot
Q13091
resolver
uniprot
Q13212
resolver
uniprot
Q14622
resolver
uniprot
Q14647
resolver
uniprot
Q29RW2
resolver
uniprot
Q7Z3V1
resolver
uniprot
Q8WUM6
resolver
uniprot_entry
ITB1_HUMAN
resolver
uniprot_sec
A8K6N2
resolver
uniprot_sec
D3DRX9
resolver
uniprot_sec
D3DRY3
resolver
uniprot_sec
D3DRY4
resolver
uniprot_sec
D3DRY5
resolver
uniprot_sec
P78466
resolver
uniprot_sec
P78467
resolver
uniprot_sec
Q13089
resolver
uniprot_sec
Q13090
resolver
uniprot_sec
Q13091
resolver
uniprot_sec
Q13212
resolver
uniprot_sec
Q14622
resolver
uniprot_sec
Q14647
resolver
uniprot_sec
Q29RW2
resolver
uniprot_sec
Q7Z3V1
resolver
uniprot_sec
Q8WUM6
resolver
amino_acid_sequence
MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK
uniprot
proteins
function
FUNCTION: 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 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). ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973). ITGA5:ITGB1 acts as a receptor for SNED1 and mediates R-G-D-dependent cell adhesion to SNED1 (PubMed:39713860). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072). {ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055, ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12473654, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:16256741, ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:33962943, ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:39713860, ECO:0000269|PubMed:7523423}.; FUNCTION: [Isoform 2]: Interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). {ECO:0000305|PubMed:2249781}.; FUNCTION: [Isoform 5]: Isoform 5 displaces isoform 1 in striated muscles. {ECO:0000250|UniProtKB:P09055}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human echoviruses 1 and 8. {ECO:0000269|PubMed:8411387}.; FUNCTION: (Microbial infection) Acts as a receptor for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:20660204}.; FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus/HHV-4. {ECO:0000269|PubMed:17945327}.; FUNCTION: (Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for Human parvovirus B19. {ECO:0000269|PubMed:12907437}.; FUNCTION: (Microbial infection) Integrin ITGA2:ITGB1 acts as a receptor for Human rotavirus. {ECO:0000269|PubMed:12941907}.; FUNCTION: (Microbial infection) Acts as a receptor for Mammalian reovirus. {ECO:0000269|PubMed:16501085}.; FUNCTION: (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. {ECO:0000269|PubMed:10397733}.; FUNCTION: (Microbial infection) Interacts with CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi (PubMed:32487760). Integrin ITGA3:ITGB1 may act as a receptor for R.delemar CotH7 in alveolar epithelial cells, which may be an early step in pulmonary mucormycosis disease progression (PubMed:32487760). {ECO:0000269|PubMed:32487760}.; FUNCTION: (Microbial infection) May serve as a receptor for adhesin A (nadA) of N.meningitidis. {ECO:0000305|PubMed:21471204}.; FUNCTION: (Microbial infection) Facilitates rabies infection in a fibronectin-dependent manner and participates in rabies virus traffic after internalization. {ECO:0000269|PubMed:31666383}.
uniprot
proteins
mass_dalton
88415
uniprot
proteins
mutagenesis
MUTAGEN 760..761; /note="RR->AA: No effect on interaction with ACAP1."; /evidence="ECO:0000269|PubMed:22645133"; MUTAGEN 762..767; /note="EFAKFE->AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5."; /evidence="ECO:0000269|PubMed:22645133"; MUTAGEN 762..763; /note="EF->AA: Slightly reduces interaction with ACAP1."; MUTAGEN 765; /note="K->A: Reduces interaction with ACAP1."; MUTAGEN 766..767; /note="FE->AA: Slightly reduces interaction with ACAP1."; MUTAGEN 768..769; /note="KE->AA: No effect on interaction with ACAP1."; /evidence="ECO:0000269|PubMed:22645133"; MUTAGEN 778; /note="G->Q: Loss of beta-1A interaction with FLNA and FLNB."; /evidence="ECO:0000269|PubMed:11807098"; MUTAGEN 783; /note="Y->A: No effect on cell surface location but impairs interaction with TNS3 and PEAK1."; /evidence="ECO:0000269|PubMed:35687021"; MUTAGEN 786..791; /note="AVTTVV->PINNFK: Does not interact with ITGB1BP1."; /evidence="ECO:0000269|PubMed:11807099"; MUTAGEN 786; /note="A->P: Loss of beta-1A interaction with FLNA and FLNB."; /evidence="ECO:0000269|PubMed:11807098"; MUTAGEN 787; /note="V->T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation."; /evidence="ECO:0000269|PubMed:21768292"; MUTAGEN 788; /note="T->D: Strongly reduces ITGB1BP1 binding; when associated with D-790."; /evidence="ECO:0000269|PubMed:23317506"; MUTAGEN 790; /note="V->D: Strongly reduces ITGB1BP1 binding; when associated with D-788."; /evidence="ECO:0000269|PubMed:23317506"; MUTAGEN 792; /note="N->A: Strongly reduces ITGB1BP1 binding; when associated with A-795."; /evidence="ECO:0000269|PubMed:23317506"; MUTAGEN 795; /note="Y->A: No effect on cell surface location but impairs interaction with TNS3 and PEAK1. Strongly reduces ITGB1BP1 binding; when associated with A-792."; /evidence="ECO:0000269|PubMed:23317506, ECO:0000269|PubMed:35687021
uniprot
proteins
protein_family
Integrin beta chain family
uniprot
proteins
pubmed
10397733
uniprot
proteins
pubmed
10455171
uniprot
proteins
pubmed
10613898
uniprot
proteins
pubmed
11741838
uniprot
proteins
pubmed
11807098
uniprot
proteins
pubmed
11807099
uniprot
proteins
pubmed
11919189
uniprot
proteins
pubmed
12473654
uniprot
proteins
pubmed
12695522
uniprot
proteins
pubmed
12807887
uniprot
proteins
pubmed
12907437
uniprot
proteins
pubmed
12941907
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14722085
uniprot
proteins
pubmed
15156152
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15181153
uniprot
proteins
pubmed
15276642
uniprot
proteins
pubmed
15466886
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1551917
uniprot
proteins
pubmed
16076904
uniprot
proteins
pubmed
16256741
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16501085
uniprot
proteins
pubmed
16754960
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17158232
uniprot
proteins
pubmed
17158881
uniprot
proteins
pubmed
17643115
uniprot
proteins
pubmed
17925226
uniprot
proteins
pubmed
17945327
uniprot
proteins
pubmed
17956333
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18635536
uniprot
proteins
pubmed
18804435
uniprot
proteins
pubmed
19064666
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20660204
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21325030
uniprot
proteins
pubmed
21471204
uniprot
proteins
pubmed
21768292
uniprot
proteins
pubmed
22027826
uniprot
proteins
pubmed
22451694
uniprot
proteins
pubmed
2249781
uniprot
proteins
pubmed
22645133
uniprot
proteins
pubmed
22654117
uniprot
proteins
pubmed
23125415
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23317506
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24789099
uniprot
proteins
pubmed
24814316
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25398877
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29030430
uniprot
proteins
pubmed
2958481
uniprot
proteins
pubmed
31331973
uniprot
proteins
pubmed
31666383
uniprot
proteins
pubmed
32487760
uniprot
proteins
pubmed
33102950
uniprot
proteins
pubmed
33962943
uniprot
proteins
pubmed
35687021
uniprot
proteins
pubmed
35802072
uniprot
proteins
pubmed
37184585
uniprot
proteins
pubmed
39713860
uniprot
proteins
pubmed
7504269
uniprot
proteins
pubmed
7523423
uniprot
proteins
pubmed
7544298
uniprot
proteins
pubmed
7545396
uniprot
proteins
pubmed
7681433
uniprot
proteins
pubmed
8411387
uniprot
proteins
pubmed
8567725
uniprot
proteins
pubmed
9494094
uniprot
proteins
pubmed
9501082
uniprot
proteins
sequence_length
798
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:32487760, ECO:0000269|PubMed:35687021, ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:11919189}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:16256741}. Melanosome {ECO:0000269|PubMed:17081065}. Cleavage furrow {ECO:0000269|PubMed:17956333}. Cell projection, lamellipodium {ECO:0000269|PubMed:11919189}. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:35687021}. Note=Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. {ECO:0000269|PubMed:10455171}.; SUBCELLULAR LOCATION: [Isoform 2]: Note=Does not localize to focal adhesions. {ECO:0000269|PubMed:10455171}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P09055}. Cell junction {ECO:0000250|UniProtKB:P09055}. Note=In cardiac muscle, found in costameres and intercalated disks. {ECO:0000250|UniProtKB:P09055}.
uniprot
proteins
transmembrane_region
TRANSMEM 729..751; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins