Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09055

- ITB1_MOUSE

UniProt

P09055 - ITB1_MOUSE

Protein

Integrin beta-1

Gene

Itgb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.
    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. 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. axon extension Source: MGI
    2. calcium-independent cell-matrix adhesion Source: Ensembl
    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. cellular calcium ion homeostasis Source: Ensembl
    11. cellular response to ionizing radiation Source: Ensembl
    12. cellular response to mechanical stimulus Source: Ensembl
    13. cellular response to vitamin D Source: Ensembl
    14. formation of radial glial scaffolds Source: MGI
    15. G1/S transition of mitotic cell cycle Source: MGI
    16. germ cell migration Source: MGI
    17. integrin-mediated signaling pathway Source: UniProtKB-KW
    18. in utero embryonic development Source: MGI
    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 apoptotic process Source: Ensembl
    28. positive regulation of cell migration Source: Ensembl
    29. positive regulation of cell proliferation Source: MGI
    30. positive regulation of cell-substrate adhesion Source: Ensembl
    31. positive regulation of endocytosis Source: Ensembl
    32. positive regulation of MAPK cascade 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 cell cycle Source: MGI
    38. regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl
    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

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

    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

    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 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei729 – 75123HelicalSequence AnalysisAdd
    BLAST

    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 161 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