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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 GNB2L1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis.By similarity
Isoform 2: Isoform 2 displaces isoform 1 in striated muscles.

Sites

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

GO - Molecular functioni

  1. actin binding Source: MGI
  2. cell adhesion molecule binding Source: MGI
  3. collagen binding involved in cell-matrix adhesion Source: MGI
  4. integrin binding Source: MGI
  5. metal ion binding Source: UniProtKB-KW
  6. peptide binding Source: Ensembl
  7. protease binding Source: MGI
  8. protein heterodimerization activity Source: UniProtKB
  9. receptor activity Source: InterPro

GO - Biological processi

  1. axon extension Source: MGI
  2. calcium-independent cell-matrix adhesion Source: MGI
  3. cardiac muscle cell differentiation Source: MGI
  4. cardiac muscle tissue development Source: MGI
  5. cell-cell adhesion mediated by integrin Source: Ensembl
  6. cell fate specification Source: MGI
  7. cell-matrix adhesion Source: MGI
  8. cell migration Source: MGI
  9. cell migration involved in sprouting angiogenesis Source: MGI
  10. cell-substrate 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. dendrite morphogenesis Source: MGI
  16. formation of radial glial scaffolds Source: MGI
  17. G1/S transition of mitotic cell cycle Source: MGI
  18. germ cell migration Source: MGI
  19. heterotypic cell-cell adhesion Source: MGI
  20. integrin-mediated signaling pathway Source: MGI
  21. in utero embryonic development Source: MGI
  22. leukocyte cell-cell adhesion Source: MGI
  23. leukocyte tethering or rolling Source: MGI
  24. maternal process involved in female pregnancy Source: Ensembl
  25. mesodermal cell differentiation Source: Ensembl
  26. negative regulation of anoikis Source: MGI
  27. negative regulation of cell differentiation Source: MGI
  28. negative regulation of cell projection organization Source: Ensembl
  29. negative regulation of cell proliferation Source: Ensembl
  30. negative regulation of neuron differentiation Source: Ensembl
  31. negative regulation of Rho protein signal transduction Source: MGI
  32. neuron projection development Source: MGI
  33. positive regulation of apoptotic process Source: MGI
  34. positive regulation of cell migration Source: Ensembl
  35. positive regulation of cell proliferation Source: MGI
  36. positive regulation of cell-substrate adhesion Source: Ensembl
  37. positive regulation of endocytosis Source: Ensembl
  38. positive regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  39. positive regulation of MAPK cascade Source: Ensembl
  40. positive regulation of neuron projection development Source: Ensembl
  41. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  42. protein transport within lipid bilayer Source: Ensembl
  43. regulation of cell cycle Source: MGI
  44. regulation of collagen catabolic process Source: UniProtKB
  45. regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl
  46. response to activity Source: Ensembl
  47. response to drug Source: Ensembl
  48. response to gonadotropin Source: Ensembl
  49. response to transforming growth factor beta Source: Ensembl
  50. sarcomere organization Source: MGI
  51. tight junction assembly Source: Ensembl
  52. tissue homeostasis Source: Ensembl
  53. 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

ReactomeiREACT_278886. Cell surface interactions at the vascular wall.
REACT_280605. Other semaphorin interactions.
REACT_286043. Laminin interactions.
REACT_286773. Fibronectin matrix formation.
REACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_301006. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_319261. Integrin cell surface interactions.
REACT_323105. Basigin interactions.
REACT_326610. Syndecan interactions.
REACT_329019. CHL1 interactions.
REACT_332220. Molecules associated with elastic fibres.
REACT_334317. Elastic fibre formation.
REACT_344422. Platelet Adhesion to exposed collagen.
REACT_353319. Signal transduction by L1.
REACT_354321. ECM proteoglycans.

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 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96610. Itgb1.

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein Sequence Analysis. Cell projectioninvadopodium membrane By similarity; Single-pass type I membrane protein Sequence Analysis. Cell projectionruffle membrane By similarity; Single-pass type I membrane protein Sequence Analysis. Recycling endosome 2 Publications. 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. 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.By similarity
Isoform 2 : Cell membranesarcolemma. Cell junction
Note: In cardiac muscle, isoform 2 is found in costameres and intercalated disks.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 728708ExtracellularSequence AnalysisAdd
BLAST
Transmembranei729 – 75123HelicalSequence AnalysisAdd
BLAST
Topological domaini752 – 79847CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. basement membrane Source: Ensembl
  3. cell surface Source: UniProtKB
  4. cytoplasm Source: MGI
  5. dendritic spine Source: MGI
  6. external side of plasma membrane Source: MGI
  7. extracellular vesicular exosome Source: MGI
  8. filopodium Source: MGI
  9. focal adhesion Source: MGI
  10. hemidesmosome Source: Ensembl
  11. integrin alpha10-beta1 complex Source: MGI
  12. integrin alpha11-beta1 complex Source: MGI
  13. integrin alpha1-beta1 complex Source: MGI
  14. integrin alpha2-beta1 complex Source: MGI
  15. integrin alpha3-beta1 complex Source: MGI
  16. integrin alpha7-beta1 complex Source: MGI
  17. integrin alpha9-beta1 complex Source: Ensembl
  18. intercalated disc Source: MGI
  19. invadopodium membrane Source: UniProtKB
  20. lamellipodium Source: UniProtKB-SubCell
  21. melanosome Source: UniProtKB-SubCell
  22. membrane Source: MGI
  23. membrane raft Source: MGI
  24. myelin sheath abaxonal region Source: BHF-UCL
  25. neuromuscular junction Source: MGI
  26. plasma membrane Source: MGI
  27. receptor complex Source: MGI
  28. recycling endosome Source: UniProtKB-SubCell
  29. ruffle membrane Source: UniProtKB-SubCell
  30. sarcolemma Source: MGI
  31. synapse Source: MGI
  32. 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)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 – 2020Add
BLAST
Chaini21 – 798778Integrin beta-1PRO_0000016335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 45By similarity
Disulfide bondi35 ↔ 464By similarity
Disulfide bondi38 ↔ 75By similarity
Disulfide bondi48 ↔ 64By similarity
Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi207 ↔ 213By similarity
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi261 ↔ 301By similarity
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
Glycosylationi366 – 3661N-linked (GlcNAc...); atypical1 Publication
Glycosylationi376 – 3761N-linked (GlcNAc...); atypical1 Publication
Disulfide bondi401 ↔ 415By similarity
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi435 ↔ 462By similarity
Disulfide bondi466 ↔ 691By similarity
Disulfide bondi477 ↔ 489By similarity
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi486 ↔ 525By similarity
Disulfide bondi491 ↔ 500By similarity
Disulfide bondi502 ↔ 516By similarity
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi669 – 6691N-linked (GlcNAc...)1 Publication
Modified residuei777 – 7771Phosphothreonine1 Publication
Modified residuei783 – 7831Phosphotyrosine1 Publication
Modified residuei785 – 7851PhosphoserineBy similarity
Modified residuei789 – 7891PhosphothreonineBy similarity
Modified residuei794 – 7941N6-acetyllysineBy 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

BgeeiP09055.
CleanExiMM_ITGB1.
ExpressionAtlasiP09055. baseline and differential.
GenevestigatoriP09055.

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 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. Interacts with EMP2; the interaction may be direct or indirect and ITGB1 has an heterodimer form (PubMed:12189152).By similarity7 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini140 – 378239VWFAAdd
BLAST
Repeati466 – 51550IAdd
BLAST
Repeati516 – 55944IIAdd
BLAST
Repeati560 – 59839IIIAdd
BLAST
Repeati599 – 63537IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 635170Cysteine-rich tandem repeatsAdd
BLAST
Regioni762 – 7676Signal for sorting from recycling endosomes; interaction with ACAP1By similarity
Regioni785 – 7928Interaction with ITGB1BP1By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287997.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP09055.
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. 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:October 31, 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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → Q in BAC40532 (PubMed:16141072).Curated
Sequence conflicti72 – 721K → E in BAE35290 (PubMed:16141072).Curated
Sequence conflicti385 – 3851E → D in BAC36379 (PubMed:16141072).Curated
Sequence conflicti385 – 3851E → P in CAA33272 (PubMed:2523953).Curated
Sequence conflicti392 – 3921G → A in CAA33272 (PubMed:2523953).Curated
Sequence conflicti407 – 4071G → E in BAC36379 (PubMed:16141072).Curated
Sequence conflicti443 – 4453IKI → HSKL in CAA33272 (PubMed:2523953).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei778 – 7781G → Q in isoform 2. 1 PublicationVSP_053581
Alternative sequencei786 – 79813AVTTV…KYEGK → PINNFKNPNYGRKAGL in isoform 2. 1 PublicationVSP_053582Add
BLAST

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. Positions 25-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP09055.

Proteomic databases

MaxQBiP09055.
PaxDbiP09055.
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

eggNOGiNOG287997.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP09055.
KOiK05719.
OMAiENNVYTM.
OrthoDBiEOG7T7GSB.
PhylomeDBiP09055.
TreeFamiTF105392.

Enzyme and pathway databases

ReactomeiREACT_278886. Cell surface interactions at the vascular wall.
REACT_280605. Other semaphorin interactions.
REACT_286043. Laminin interactions.
REACT_286773. Fibronectin matrix formation.
REACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_301006. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_319261. Integrin cell surface interactions.
REACT_323105. Basigin interactions.
REACT_326610. Syndecan interactions.
REACT_329019. CHL1 interactions.
REACT_332220. Molecules associated with elastic fibres.
REACT_334317. Elastic fibre formation.
REACT_344422. Platelet Adhesion to exposed collagen.
REACT_353319. Signal transduction by L1.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiItgb1. mouse.
NextBioi289597.
PROiP09055.
SOURCEiSearch...

Gene expression databases

BgeeiP09055.
CleanExiMM_ITGB1.
ExpressionAtlasiP09055. baseline and differential.
GenevestigatoriP09055.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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(2004) [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 (JUN-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(2003) [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(1988) [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(1988) [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(1995) [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(1995) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. Cited for: INTERACTION WITH FBLN5.
  12. "The tetraspan protein epithelial membrane protein-2 interacts with beta1 integrins and regulates adhesion."
    Wadehra M., Iyer R., Goodglick L., Braun J.
    J. Biol. Chem. 277:41094-41100(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMP2.
  13. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NMRK2.
  14. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
  15. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  16. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  17. Cited for: FUNCTION, MUTAGENESIS OF TYR-783 AND TYR-795.
  18. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FERMT2.
  19. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363; ASN-366; ASN-376 AND ASN-669.
    Tissue: Myoblast.
  21. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGR AND HCK.
  22. "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(2010) [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: October 31, 1988
Last sequence update: October 31, 1988
Last modified: March 31, 2015
This is version 167 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

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 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.