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P09055

- ITB1_MOUSE

UniProt

P09055 - ITB1_MOUSE

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Protein
Integrin beta-1
Gene
Itgb1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. 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 GNB2L1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis.6 Publications
Isoform 2: Isoform 2 displaces isoform 1 in striated muscles.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi152 – 1521Magnesium By similarity
Metal bindingi154 – 1541Calcium 1; via carbonyl oxygen By similarity
Metal bindingi156 – 1561Calcium 1 By similarity
Metal bindingi157 – 1571Calcium 1 By similarity
Metal bindingi189 – 1891Calcium 2 By similarity
Metal bindingi244 – 2441Calcium 2 By similarity
Metal bindingi246 – 2461Calcium 2 By similarity
Metal bindingi248 – 2481Calcium 2; via carbonyl oxygen By similarity
Metal bindingi249 – 2491Calcium 2 By similarity
Metal bindingi249 – 2491Magnesium By similarity

GO - Molecular functioni

  1. integrin binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. peptide binding Source: Ensembl
  4. protein binding Source: UniProtKB
  5. receptor activity Source: InterPro

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: MGI
  2. axon extension Source: MGI
  3. calcium-independent cell-matrix adhesion Source: Ensembl
  4. cardiac muscle cell differentiation Source: MGI
  5. cardiac muscle tissue development Source: MGI
  6. cell fate specification Source: MGI
  7. cell migration Source: MGI
  8. cell migration involved in sprouting angiogenesis Source: MGI
  9. cell-cell adhesion mediated by integrin Source: Ensembl
  10. cell-matrix adhesion Source: MGI
  11. cellular calcium ion homeostasis Source: Ensembl
  12. cellular response to ionizing radiation Source: Ensembl
  13. cellular response to mechanical stimulus Source: Ensembl
  14. cellular response to vitamin D Source: Ensembl
  15. formation of radial glial scaffolds Source: MGI
  16. germ cell migration Source: MGI
  17. in utero embryonic development Source: MGI
  18. integrin-mediated signaling pathway Source: UniProtKB-KW
  19. leukocyte cell-cell adhesion Source: Ensembl
  20. maternal process involved in female pregnancy Source: Ensembl
  21. negative regulation of anoikis Source: Ensembl
  22. negative regulation of cell differentiation Source: MGI
  23. negative regulation of cell projection organization Source: Ensembl
  24. negative regulation of cell proliferation Source: Ensembl
  25. negative regulation of neuron differentiation Source: Ensembl
  26. neuron projection development Source: MGI
  27. positive regulation of MAPK cascade Source: Ensembl
  28. positive regulation of apoptotic process Source: Ensembl
  29. positive regulation of cell migration Source: Ensembl
  30. positive regulation of cell proliferation Source: MGI
  31. positive regulation of cell-substrate adhesion Source: Ensembl
  32. positive regulation of endocytosis Source: Ensembl
  33. positive regulation of neuron differentiation Source: Ensembl
  34. positive regulation of neuron projection development Source: Ensembl
  35. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  36. protein transport within lipid bilayer Source: Ensembl
  37. regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl
  38. regulation of cell cycle Source: MGI
  39. response to activity Source: Ensembl
  40. response to drug Source: Ensembl
  41. response to gonadotropin Source: Ensembl
  42. response to transforming growth factor beta Source: Ensembl
  43. sarcomere organization Source: MGI
  44. tight junction assembly Source: Ensembl
  45. tissue homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196644. Syndecan interactions.
REACT_198267. CHL1 interactions.
REACT_198996. Elastic fibre formation.
REACT_198998. Molecules associated with elastic fibres.
REACT_202342. Laminin interactions.
REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_204211. Fibronectin matrix formation.
REACT_211508. Basigin interactions.
REACT_215461. Signal transduction by L1.
REACT_216309. Integrin cell surface interactions.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

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
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:96610. Itgb1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein By similarity. Recycling endosome. Melanosome By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity
Note: 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 to fibrillar adhesions in an ITGB1BP1-dependent manner By similarity.2 Publications
Isoform 2 : Cell membranesarcolemma. Cell junction
Note: In cardiac muscle, isoform 2 is found in costameres and intercalated disks.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 728708Extracellular Reviewed prediction
Add
BLAST
Transmembranei729 – 75123Helical; Reviewed prediction
Add
BLAST
Topological domaini752 – 79847Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. basement membrane Source: Ensembl
  3. cell surface Source: MGI
  4. external side of plasma membrane Source: MGI
  5. filopodium Source: Ensembl
  6. focal adhesion Source: Ensembl
  7. hemidesmosome Source: Ensembl
  8. integrin alpha3-beta1 complex Source: Ensembl
  9. integrin alpha7-beta1 complex Source: MGI
  10. integrin alpha9-beta1 complex Source: Ensembl
  11. intercalated disc Source: MGI
  12. lamellipodium Source: UniProtKB-SubCell
  13. melanosome Source: UniProtKB-SubCell
  14. membrane raft Source: Ensembl
  15. myelin sheath abaxonal region Source: BHF-UCL
  16. neuromuscular junction Source: MGI
  17. plasma membrane Source: MGI
  18. receptor complex Source: MGI
  19. recycling endosome Source: UniProtKB-SubCell
  20. ruffle membrane Source: Ensembl
  21. sarcolemma Source: MGI
  22. synapse 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi783 – 7831Y → F: Reduced endocytosis; when associated with F-795. 1 Publication
Mutagenesisi795 – 7951Y → F: Reduced endocytosis; when associated with F-783. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020
Add
BLAST
Chaini21 – 798778Integrin beta-1
PRO_0000016335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 45 By similarity
Disulfide bondi35 ↔ 464 By similarity
Disulfide bondi38 ↔ 75 By similarity
Disulfide bondi48 ↔ 64 By similarity
Glycosylationi50 – 501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi94 – 941N-linked (GlcNAc...) Reviewed prediction
Glycosylationi97 – 971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi207 ↔ 213 By similarity
Glycosylationi212 – 2121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi261 ↔ 301 By similarity
Glycosylationi269 – 2691N-linked (GlcNAc...) Reviewed prediction
Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
Glycosylationi366 – 3661N-linked (GlcNAc...); atypical1 Publication
Glycosylationi376 – 3761N-linked (GlcNAc...); atypical1 Publication
Disulfide bondi401 ↔ 415 By similarity
Glycosylationi406 – 4061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi417 – 4171N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi435 ↔ 462 By similarity
Disulfide bondi466 ↔ 691 By similarity
Disulfide bondi477 ↔ 489 By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi486 ↔ 525 By similarity
Disulfide bondi491 ↔ 500 By similarity
Disulfide bondi502 ↔ 516 By similarity
Glycosylationi520 – 5201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi531 ↔ 536 By similarity
Disulfide bondi533 ↔ 568 By similarity
Disulfide bondi538 ↔ 553 By similarity
Disulfide bondi555 ↔ 560 By similarity
Disulfide bondi574 ↔ 579 By similarity
Disulfide bondi576 ↔ 607 By similarity
Disulfide bondi581 ↔ 590 By similarity
Glycosylationi584 – 5841N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi592 ↔ 599 By similarity
Disulfide bondi613 ↔ 618 By similarity
Disulfide bondi615 ↔ 661 By similarity
Disulfide bondi620 ↔ 630 By similarity
Disulfide bondi633 ↔ 636 By similarity
Disulfide bondi640 ↔ 649 By similarity
Disulfide bondi646 ↔ 723 By similarity
Disulfide bondi665 ↔ 699 By similarity
Glycosylationi669 – 6691N-linked (GlcNAc...)1 Publication
Modified residuei777 – 7771Phosphothreonine1 Publication
Modified residuei783 – 7831Phosphotyrosine1 Publication
Modified residuei794 – 7941N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP09055.
PaxDbiP09055.
PRIDEiP09055.

PTM databases

PhosphoSiteiP09055.

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

ArrayExpressiP09055.
BgeeiP09055.
CleanExiMM_ITGB1.
GenevestigatoriP09055.

Interactioni

Subunit structurei

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 GNB2L1 and SRC. Interacts with AMICA1; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling AMICA1 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.6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200826. 6 interactions.
DIPiDIP-46247N.
IntActiP09055. 19 interactions.
MINTiMINT-1573412.

Structurei

3D structure databases

ProteinModelPortaliP09055.
SMRiP09055. Positions 25-787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 378239VWFA
Add
BLAST
Repeati466 – 51550I
Add
BLAST
Repeati516 – 55944II
Add
BLAST
Repeati560 – 59839III
Add
BLAST
Repeati599 – 63537IV
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 635170Cysteine-rich tandem repeats
Add
BLAST
Regioni762 – 7676Signal for sorting from recycling endosomes; interaction with ACAP1 By similarity
Regioni785 – 7928Interaction with ITGB1BP1 By similarity

Sequence similaritiesi

Contains 1 VWFA domain.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287997.
GeneTreeiENSGT00730000110513.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiQ8BTU0.
KOiK05719.
OMAiENNVYTM.
OrthoDBiEOG7T7GSB.
PhylomeDBiP09055.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
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.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 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. Align

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

MNLQLVSWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN    50
TTFLQEGMPT SARCDDLEAL KKKGCQPSDI ENPRGSQTIK KNKNVTNRSK 100
GMAEKLRPED ITQIQPQQLL LKLRSGEPQK FTLKFKRAED YPIDLYYLMD 150
LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP 200
AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR ISGNLDSPEG 250
GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 300
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN 350
LIPKSAVGTL SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY 400
CKNGVNGTGE NGRKCSNISI GDEVQFEISI TANKCPNKES ETIKIKPLGF 450
TEEVEVVLQF ICKCNCQSHG IPASPKCHEG NGTFECGACR CNEGRVGRHC 500
ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG 550
KFCECDNFNC DRSNGLICGG NGVCRCRVCE CYPNYTGSAC DCSLDTGPCL 600
ASNGQICNGR GICECGACKC TDPKFQGPTC ETCQTCLGVC AEHKECVQCR 650
AFNKGEKKDT CAQECSHFNL TKVESREKLP QPVQVDPVTH CKEKDIDDCW 700
FYFTYSVNGN NEAIVHVVET PDCPTGPDII PIVAGVVAGI VLIGLALLLI 750
WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK 798
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 BAC36379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei778 – 7781G → Q in isoform 2.
VSP_053581
Alternative sequencei786 – 79813AVTTV…KYEGK → PINNFKNPNYGRKAGL in isoform 2.
VSP_053582Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → Q in BAC40532. 1 Publication
Sequence conflicti72 – 721K → E in BAE35290. 1 Publication
Sequence conflicti385 – 3851E → D in BAC36379. 1 Publication
Sequence conflicti385 – 3851E → P in CAA33272. 1 Publication
Sequence conflicti392 – 3921G → A in CAA33272. 1 Publication
Sequence conflicti407 – 4071G → E in BAC36379. 1 Publication
Sequence conflicti443 – 4453IKI → HSKL in CAA33272. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22791.1. [P09055-1 ]
PIRi PL0104. IJMSFB.
S01659.
RefSeqi NP_034708.1. NM_010578.2. [P09055-1 ]
UniGenei Mm.263396.

3D structure databases

ProteinModelPortali P09055.
SMRi P09055. Positions 25-787.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200826. 6 interactions.
DIPi DIP-46247N.
IntActi P09055. 19 interactions.
MINTi MINT-1573412.

PTM databases

PhosphoSitei P09055.

Proteomic databases

MaxQBi P09055.
PaxDbi P09055.
PRIDEi P09055.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000090006 ; ENSMUSP00000087457 ; ENSMUSG00000025809 . [P09055-1 ]
GeneIDi 16412.
KEGGi mmu:16412.
UCSCi uc009nzv.2. mouse. [P09055-1 ]

Organism-specific databases

CTDi 3688.
MGIi MGI:96610. Itgb1.

Phylogenomic databases

eggNOGi NOG287997.
GeneTreei ENSGT00730000110513.
HOGENOMi HOG000252936.
HOVERGENi HBG006190.
InParanoidi Q8BTU0.
KOi K05719.
OMAi ENNVYTM.
OrthoDBi EOG7T7GSB.
PhylomeDBi P09055.
TreeFami TF105392.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196644. Syndecan interactions.
REACT_198267. CHL1 interactions.
REACT_198996. Elastic fibre formation.
REACT_198998. Molecules associated with elastic fibres.
REACT_202342. Laminin interactions.
REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_204211. Fibronectin matrix formation.
REACT_211508. Basigin interactions.
REACT_215461. Signal transduction by L1.
REACT_216309. Integrin cell surface interactions.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

NextBioi 289597.
PROi P09055.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09055.
Bgeei P09055.
CleanExi MM_ITGB1.
Genevestigatori P09055.

Family and domain databases

Gene3Di 1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProi IPR013111. EGF_extracell.
IPR027071. Integrin_beta-1.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view ]
PANTHERi PTHR10082. PTHR10082. 1 hit.
PTHR10082:SF28. PTHR10082:SF28. 1 hit.
Pfami PF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view ]
PIRSFi PIRSF002512. Integrin_B. 1 hit.
PRINTSi PR01186. INTEGRINB.
SMARTi SM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view ]
SUPFAMi SSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEi PS00022. EGF_1. 2 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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  1. "Murine mRNA for the beta-subunit of integrin is increased in BALB/c-3T3 cells entering the G1 phase from the G0 state."
    Tominaga S.
    FEBS Lett. 238:315-319(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Head, Osteoclast, Placenta and Thymocyte.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Molecular cloning of a murine fibronectin receptor and its expression during inflammation. Expression of VLA-5 is increased in activated peritoneal macrophages in a manner discordant from major histocompatibility complex class II."
    Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L., Brown E.J.
    J. Exp. Med. 169:1589-1605(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-798 (ISOFORM 1).
    Strain: BALB/c.
  7. "Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts."
    Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.
    Exp. Cell Res. 180:537-545(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 595-798 (ISOFORM 1).
  8. "Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells."
    Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A., Tarone G., Koteliansky V.E., Burridge K.
    J. Cell Biol. 132:211-226(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-798 (ISOFORM 2), FUNCTION, INTERACTION WITH ITGA7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Myoblast.
  9. "Genomic organization of the mouse beta 1 gene: conservation of the beta 1D but not of the beta 1B and beta 1C integrin splice variants."
    Baudoin C., Van der Flier A., Borradori L., Sonnenberg A.
    Cell Adhes. Commun. 4:1-11(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 723-798.
    Tissue: Skeletal muscle.
  10. "Knockout and knockin of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development."
    Baudoin C., Goumans M.J., Mummery C., Sonnenberg A.
    Genes Dev. 12:1202-1216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition."
    Li J., Rao H., Burkin D., Kaufman S.J., Wu C.
    Dev. Biol. 261:209-219(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NMRK2.
  12. "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin."
    Fukushi J., Makagiansar I.T., Stallcup W.B.
    Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
  13. "Disabled-2 (Dab2) is required for transforming growth factor beta-induced epithelial to mesenchymal transition (EMT)."
    Prunier C., Howe P.H.
    J. Biol. Chem. 280:17540-17548(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  15. Cited for: FUNCTION, MUTAGENESIS OF TYR-783 AND TYR-795.
  16. "Kindlin-2 controls bidirectional signaling of integrins."
    Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M., Fassler R.
    Genes Dev. 22:1325-1330(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FERMT2.
  17. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363; ASN-366; ASN-376 AND ASN-669.
    Tissue: Myoblast.
  19. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
    Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
    FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGR AND HCK.
  20. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
    Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
    J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

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: September 3, 2014
This is version 160 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

External Data

Dasty 3

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