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Protein

Integrin beta-1

Gene

Itgb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 and 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. 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. 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/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. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity). 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 (By similarity). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity).By similarity6 Publications
Isoform 2: Isoform 2 displaces isoform 1 in striated muscles.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi152MagnesiumBy similarity1
Metal bindingi154Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 1By similarity1
Metal bindingi157Calcium 1By similarity1
Metal bindingi189Calcium 2By similarity1
Metal bindingi244Calcium 2By similarity1
Metal bindingi246Calcium 2By similarity1
Metal bindingi248Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi249Calcium 2By similarity1
Metal bindingi249MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • axon extension Source: MGI
  • calcium-independent cell-matrix adhesion Source: MGI
  • cardiac muscle cell differentiation Source: MGI
  • cardiac muscle tissue development Source: MGI
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-cell adhesion mediated by integrin Source: Ensembl
  • cell fate specification Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell migration Source: MGI
  • cell migration involved in sprouting angiogenesis Source: MGI
  • cell-substrate adhesion Source: MGI
  • cellular response to low-density lipoprotein particle stimulus Source: UniProtKB
  • dendrite morphogenesis Source: MGI
  • formation of radial glial scaffolds Source: MGI
  • G1/S transition of mitotic cell cycle Source: MGI
  • germ cell migration Source: MGI
  • heterotypic cell-cell adhesion Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • in utero embryonic development Source: MGI
  • leukocyte cell-cell adhesion Source: MGI
  • leukocyte tethering or rolling Source: MGI
  • mesodermal cell differentiation Source: Ensembl
  • negative regulation of anoikis Source: MGI
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of Rho protein signal transduction Source: MGI
  • neuron projection development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  • positive regulation of GTPase activity Source: MGI
  • receptor internalization Source: UniProtKB
  • regulation of cell cycle Source: MGI
  • regulation of collagen catabolic process Source: UniProtKB
  • sarcomere organization Source: MGI
  • visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1566948. Elastic fibre formation.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-210991. Basigin interactions.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000157. Laminin interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-416700. Other semaphorin interactions.
R-MMU-445144. Signal transduction by L1.
R-MMU-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-MMU-447041. CHL1 interactions.
R-MMU-8874081. MET activates PTK2 signaling.
R-MMU-8875513. MET interacts with TNS proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-1
Alternative name(s):
Fibronectin receptor subunit beta
VLA-4 subunit beta
CD_antigen: CD29
Gene namesi
Name:Itgb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96610. Itgb1.

Subcellular locationi

Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 728ExtracellularSequence analysisAdd BLAST708
Transmembranei729 – 751HelicalSequence analysisAdd BLAST23
Topological domaini752 – 798CytoplasmicSequence analysisAdd BLAST47

GO - Cellular componenti

  • cell-cell adherens junction Source: MGI
  • cell surface Source: UniProtKB
  • cytoplasm Source: MGI
  • dendritic spine Source: MGI
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • filopodium Source: MGI
  • focal adhesion Source: UniProtKB
  • integrin alpha10-beta1 complex Source: MGI
  • integrin alpha11-beta1 complex Source: MGI
  • integrin alpha1-beta1 complex Source: MGI
  • integrin alpha2-beta1 complex Source: MGI
  • integrin alpha3-beta1 complex Source: MGI
  • integrin alpha7-beta1 complex Source: MGI
  • intercalated disc Source: MGI
  • invadopodium membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • membrane raft Source: MGI
  • myelin sheath abaxonal region Source: BHF-UCL
  • neuromuscular junction Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
  • recycling endosome Source: UniProtKB-SubCell
  • ruffle membrane Source: UniProtKB-SubCell
  • sarcolemma Source: MGI
  • synapse Source: MGI
  • synaptic membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Isoform 2 knockout mice are viable and fertile, but male mice display a mild abnormality of cardiac function reflected by an increased expression of atrial natriuretic peptide and beta myosin heavy chain. Muscles do not show any histological or ultrastructural alterations. Replacement of isoform 1 by isoform 2 results in embryonic lethality before 16.5 dpc with a plethora of developmental defects including open neural tube, which is abnormally waved both rostrally and caudally. Some embryos lack part of the hindbrain and in most embryos the first branchial arch is shortened, which in some of the embryos leaves the tongue exposed. Abnormally strong fibronectin staining is seen in the mesenchyme under the open neural tube. Extravasation of red blood cells is evident in various tissues and they are also found in the pericardial cavity. Choroid plexus is virtually absent correlating with the presence of an abnormally smooth head and small brain cavities. At later developmental stages, a striking feature is the lack of a lower jaw and a dysmorphic lower face. These defects are in part caused by the abnormal migration of neuroepithelial cells.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi783Y → F: Reduced endocytosis; when associated with F-795. 1 Publication1
Mutagenesisi795Y → F: Reduced endocytosis; when associated with F-783. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000001633521 – 798Integrin beta-1Add BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 45By similarity
Disulfide bondi35 ↔ 464By similarity
Disulfide bondi38 ↔ 75By similarity
Disulfide bondi48 ↔ 64By similarity
Glycosylationi50N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi97N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi207 ↔ 213By similarity
Glycosylationi212N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi261 ↔ 301By similarity
Glycosylationi269N-linked (GlcNAc...)Sequence analysis1
Glycosylationi363N-linked (GlcNAc...)1 Publication1
Glycosylationi366N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi376N-linked (GlcNAc...); atypical1 Publication1
Disulfide bondi401 ↔ 415By similarity
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi466 ↔ 691By similarity
Disulfide bondi477 ↔ 489By similarity
Glycosylationi481N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi486 ↔ 525By similarity
Disulfide bondi491 ↔ 500By similarity
Disulfide bondi502 ↔ 516By similarity
Glycosylationi520N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi531 ↔ 536By similarity
Disulfide bondi533 ↔ 568By similarity
Disulfide bondi538 ↔ 553By similarity
Disulfide bondi555 ↔ 560By similarity
Disulfide bondi574 ↔ 579By similarity
Disulfide bondi576 ↔ 607By similarity
Disulfide bondi581 ↔ 590By similarity
Glycosylationi584N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi592 ↔ 599By similarity
Disulfide bondi613 ↔ 618By similarity
Disulfide bondi615 ↔ 661By similarity
Disulfide bondi620 ↔ 630By similarity
Disulfide bondi633 ↔ 636By similarity
Disulfide bondi640 ↔ 649By similarity
Disulfide bondi646 ↔ 723By similarity
Disulfide bondi665 ↔ 699By similarity
Glycosylationi669N-linked (GlcNAc...)1 Publication1
Modified residuei777PhosphothreonineCombined sources1
Modified residuei783PhosphotyrosineCombined sources1
Modified residuei785PhosphoserineBy similarity1
Modified residuei789PhosphothreonineBy similarity1
Modified residuei794N6-acetyllysine; alternateBy similarity1
Cross-linki794Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity

Post-translational modificationi

The cysteine residues are involved in intrachain disulfide bonds.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP09055.
MaxQBiP09055.
PaxDbiP09055.
PeptideAtlasiP09055.
PRIDEiP09055.

PTM databases

iPTMnetiP09055.
PhosphoSitePlusiP09055.
SwissPalmiP09055.

Expressioni

Tissue specificityi

Isoform 2 is expressed in skeletal and cardiac muscles only (at protein level). Isoform 1 is very weakly expressed in striated muscles and not detected in adult skeletal muscle fibers and cardiomyocytes.1 Publication

Developmental stagei

Isoform 2 is not detected in proliferating myoblasts, but it appears immediately after myoblast fusion and its amount continues to rise during myotube growth and maturation reaching its highest level at day 9 through day 10, when mature differentiated myotubes appear in cell culture. Isoform 1 expression is down-regulated during myodifferentiation in culture and it is completely displaced by isoform 2 in mature differentiated myotubes.1 Publication

Gene expression databases

BgeeiENSMUSG00000025809.
CleanExiMM_ITGB1.
ExpressionAtlasiP09055. baseline and differential.
GenevisibleiP09055. MM.

Interactioni

Subunit structurei

Interacts with seprase FAP (seprase); the interaction occurs at the cell surface of invadopodia membrane in a collagen-dependent manner (By similarity). 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. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. 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 RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with MYO10. 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. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2. Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 2 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 (PubMed:12189152). ITGA5:ITGB1 interacts with NOV (By similarity). ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (By similarity). ITGA5:ITGB1 interacts with FBN1 (By similarity).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Csf2rbP269552EBI-644224,EBI-1810026
Nme2Q017683EBI-644224,EBI-642573
Tmem158Q6F5E03EBI-644224,EBI-645317
WaslQ91YD92EBI-644224,EBI-642417

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200826. 49 interactors.
DIPiDIP-46247N.
IntActiP09055. 60 interactors.
MINTiMINT-1573412.
STRINGi10090.ENSMUSP00000087457.

Structurei

3D structure databases

ProteinModelPortaliP09055.
SMRiP09055.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 378VWFAAdd BLAST239
Repeati466 – 515IAdd BLAST50
Repeati516 – 559IIAdd BLAST44
Repeati560 – 598IIIAdd BLAST39
Repeati599 – 635IVAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 213CX3CL1-bindingBy similarity7
Regioni295 – 314CX3CL1-bindingBy similarityAdd BLAST20
Regioni466 – 635Cysteine-rich tandem repeatsAdd BLAST170
Regioni762 – 767Signal for sorting from recycling endosomes; interaction with ACAP1By similarity6
Regioni785 – 792Interaction with ITGB1BP1By similarity8

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP09055.
KOiK05719.
OMAiSSVCCVF.
OrthoDBiEOG091G029W.
PhylomeDBiP09055.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamiPF07974. 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.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P09055-1) [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.

« Hide

        10         20         30         40         50
MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN
60 70 80 90 100
TTFLQEGMPT SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK
110 120 130 140 150
GMAEKLRPED ITQIQPQQLL LKLRSGEPQK FTLKFKRAED YPIDLYYLMD
160 170 180 190 200
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP
210 220 230 240 250
AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR ISGNLDSPEG
260 270 280 290 300
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
310 320 330 340 350
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN
360 370 380 390 400
LIPKSAVGTL SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY
410 420 430 440 450
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TANKCPNKES ETIKIKPLGF
460 470 480 490 500
TEEVEVVLQF ICKCNCQSHG IPASPKCHEG NGTFECGACR CNEGRVGRHC
510 520 530 540 550
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG
560 570 580 590 600
KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL
610 620 630 640 650
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR
660 670 680 690 700
AFNKGEKKDT CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW
710 720 730 740 750
FYFTYSVNGN NEAIVHVVET PDCPTGPDII PIVAGVVAGI VLIGLALLLI
760 770 780 790
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
Length:798
Mass (Da):88,231
Last modified:November 1, 1988 - v1
Checksum:i26788F7F0A168B56
GO
Isoform 2 (identifier: P09055-2) [UniParc]FASTAAdd to basket
Also known as: Beta-1D

The sequence of this isoform differs from the canonical sequence as follows:
     778-778: G → Q
     786-798: AVTTVVNPKYEGK → PINNFKNPNYGRKAGL

Show »
Length:801
Mass (Da):88,700
Checksum:i7559450B2812F5A2
GO

Sequence cautioni

The sequence BAC36379 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5L → Q in BAC40532 (PubMed:16141072).Curated1
Sequence conflicti72K → E in BAE35290 (PubMed:16141072).Curated1
Sequence conflicti385E → D in BAC36379 (PubMed:16141072).Curated1
Sequence conflicti385E → P in CAA33272 (PubMed:2523953).Curated1
Sequence conflicti392G → A in CAA33272 (PubMed:2523953).Curated1
Sequence conflicti407G → E in BAC36379 (PubMed:16141072).Curated1
Sequence conflicti443 – 445IKI → HSKL in CAA33272 (PubMed:2523953).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_053581778G → Q in isoform 2. 1 Publication1
Alternative sequenceiVSP_053582786 – 798AVTTV…KYEGK → PINNFKNPNYGRKAGL in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00769 mRNA. Translation: CAA68738.1.
AK076526 mRNA. Translation: BAC36379.1. Different initiation.
AK088729 mRNA. Translation: BAC40532.1.
AK159689 mRNA. Translation: BAE35290.1.
AK167682 mRNA. Translation: BAE39731.1.
AC156608 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11832.1.
BC050906 mRNA. Translation: AAH50906.1.
X15202 mRNA. Translation: CAA33272.1.
U37029 mRNA. Translation: AAA80243.1.
U47283 Genomic DNA. Translation: AAA88821.1.
CCDSiCCDS22791.1. [P09055-1]
PIRiPL0104. IJMSFB.
S01659.
RefSeqiNP_034708.1. NM_010578.2. [P09055-1]
UniGeneiMm.263396.

Genome annotation databases

EnsembliENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809. [P09055-1]
GeneIDi16412.
KEGGimmu:16412.
UCSCiuc009nzv.2. mouse. [P09055-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00769 mRNA. Translation: CAA68738.1.
AK076526 mRNA. Translation: BAC36379.1. Different initiation.
AK088729 mRNA. Translation: BAC40532.1.
AK159689 mRNA. Translation: BAE35290.1.
AK167682 mRNA. Translation: BAE39731.1.
AC156608 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11832.1.
BC050906 mRNA. Translation: AAH50906.1.
X15202 mRNA. Translation: CAA33272.1.
U37029 mRNA. Translation: AAA80243.1.
U47283 Genomic DNA. Translation: AAA88821.1.
CCDSiCCDS22791.1. [P09055-1]
PIRiPL0104. IJMSFB.
S01659.
RefSeqiNP_034708.1. NM_010578.2. [P09055-1]
UniGeneiMm.263396.

3D structure databases

ProteinModelPortaliP09055.
SMRiP09055.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200826. 49 interactors.
DIPiDIP-46247N.
IntActiP09055. 60 interactors.
MINTiMINT-1573412.
STRINGi10090.ENSMUSP00000087457.

PTM databases

iPTMnetiP09055.
PhosphoSitePlusiP09055.
SwissPalmiP09055.

Proteomic databases

EPDiP09055.
MaxQBiP09055.
PaxDbiP09055.
PeptideAtlasiP09055.
PRIDEiP09055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090006; ENSMUSP00000087457; ENSMUSG00000025809. [P09055-1]
GeneIDi16412.
KEGGimmu:16412.
UCSCiuc009nzv.2. mouse. [P09055-1]

Organism-specific databases

CTDi3688.
MGIiMGI:96610. Itgb1.

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP09055.
KOiK05719.
OMAiSSVCCVF.
OrthoDBiEOG091G029W.
PhylomeDBiP09055.
TreeFamiTF105392.

Enzyme and pathway databases

ReactomeiR-MMU-1566948. Elastic fibre formation.
R-MMU-1566977. Fibronectin matrix formation.
R-MMU-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-MMU-202733. Cell surface interactions at the vascular wall.
R-MMU-210991. Basigin interactions.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000157. Laminin interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-416700. Other semaphorin interactions.
R-MMU-445144. Signal transduction by L1.
R-MMU-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-MMU-447041. CHL1 interactions.
R-MMU-8874081. MET activates PTK2 signaling.
R-MMU-8875513. MET interacts with TNS proteins.

Miscellaneous databases

ChiTaRSiItgb1. mouse.
PROiP09055.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025809.
CleanExiMM_ITGB1.
ExpressionAtlasiP09055. baseline and differential.
GenevisibleiP09055. MM.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
PfamiPF07974. 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.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITB1_MOUSE
AccessioniPrimary (citable) accession number: P09055
Secondary accession number(s): F6R105
, Q3TIW5, Q3TWH6, Q60993, Q61126, Q8BTU0, Q8BVU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 30, 2016
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.