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P05556

- ITB1_HUMAN

UniProt

P05556 - ITB1_HUMAN

Protein

Integrin beta-1

Gene

ITGB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 186 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    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. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform 2 interferes with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. 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/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis.7 Publications
    Isoform 5: Isoform 5 displaces isoform 1 in striated muscles.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi152 – 1521Magnesium
    Metal bindingi154 – 1541Calcium 1; via carbonyl oxygen
    Metal bindingi156 – 1561Calcium 1
    Metal bindingi157 – 1571Calcium 1
    Metal bindingi189 – 1891Calcium 2
    Metal bindingi244 – 2441Calcium 2
    Metal bindingi246 – 2461Calcium 2
    Metal bindingi248 – 2481Calcium 2; via carbonyl oxygen
    Metal bindingi249 – 2491Calcium 2
    Metal bindingi249 – 2491Magnesium
    Metal bindingi362 – 3621Calcium 1; via carbonyl oxygen

    GO - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. cell adhesion molecule binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. peptide binding Source: Ensembl
    5. protein binding Source: IntAct
    6. protein heterodimerization activity Source: UniProtKB
    7. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Host cell receptor for virus entry, Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_12560. Basigin interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.
    REACT_160131. Fibronectin matrix formation.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_169262. Laminin interactions.
    REACT_19200. Other semaphorin interactions.
    REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
    REACT_22272. Signal transduction by L1.
    REACT_22292. CHL1 interactions.
    SABIO-RKP05556.
    SignaLinkiP05556.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin beta-1
    Alternative name(s):
    Fibronectin receptor subunit beta
    Glycoprotein IIa
    Short name:
    GPIIA
    VLA-4 subunit beta
    CD_antigen: CD29
    Gene namesi
    Name:ITGB1
    Synonyms:FNRB, MDF2, MSK12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6153. ITGB1.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Recycling endosome. Melanosome. Cleavage furrow. Cell projectionlamellipodium. Cell projectionruffle
    Note: Isoform 2 does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in a few intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions sites to fibrillar adhesions in a ITGB1BP1-dependent manner.
    Isoform 5 : Cell membranesarcolemma By similarity. Cell junction By similarity
    Note: In cardiac muscle, isoform 5 is found in costameres and intercalated disks.By similarity

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. basement membrane Source: Ensembl
    3. cell surface Source: UniProtKB
    4. cleavage furrow Source: UniProtKB-SubCell
    5. cytoplasm Source: BHF-UCL
    6. external side of plasma membrane Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. filopodium Source: BHF-UCL
    9. focal adhesion Source: MGI
    10. hemidesmosome Source: Ensembl
    11. integrin alpha3-beta1 complex Source: Ensembl
    12. integrin alpha7-beta1 complex Source: Ensembl
    13. integrin alpha8-beta1 complex Source: BHF-UCL
    14. integrin alpha9-beta1 complex Source: Ensembl
    15. integrin complex Source: UniProtKB
    16. intercalated disc Source: Ensembl
    17. lamellipodium Source: UniProtKB-SubCell
    18. melanosome Source: UniProtKB-SubCell
    19. membrane Source: UniProtKB
    20. membrane raft Source: BHF-UCL
    21. myelin sheath abaxonal region Source: Ensembl
    22. neuromuscular junction Source: MGI
    23. plasma membrane Source: UniProtKB
    24. receptor complex Source: MGI
    25. recycling endosome Source: UniProtKB-SubCell
    26. ruffle Source: HGNC
    27. sarcolemma Source: MGI

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi760 – 7612RR → AA: No effect on interaction with ACAP1.
    Mutagenesisi762 – 7676EFAKFE → AAAAAA: Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5.
    Mutagenesisi762 – 7632EF → AA: Slightly reduces interaction with ACAP1.
    Mutagenesisi765 – 7651K → A: Reduces interaction with ACAP1.
    Mutagenesisi766 – 7672FE → AA: Slightly reduces interaction with ACAP1.
    Mutagenesisi768 – 7692KE → AA: No effect on interaction with ACAP1.
    Mutagenesisi778 – 7781G → Q: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication
    Mutagenesisi786 – 7916AVTTVV → PINNFK: Does not interact with ITGB1BP1. 1 Publication
    Mutagenesisi786 – 7861A → P: Loss of beta-1A interaction with FLNA and FLNB. 1 Publication
    Mutagenesisi787 – 7871V → T: Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation. 1 Publication
    Mutagenesisi788 – 7881T → D: Strongly reduces ITGB1BP1 binding; when associated with D-790. 1 Publication
    Mutagenesisi790 – 7901V → D: Strongly reduces ITGB1BP1 binding; when associated with D-788. 1 Publication
    Mutagenesisi792 – 7921N → A: Strongly reduces ITGB1BP1 binding; when associated with A-795. 1 Publication
    Mutagenesisi795 – 7951Y → A: Strongly reduces ITGB1BP1 binding; when associated with A-792. 1 Publication

    Organism-specific databases

    PharmGKBiPA29953.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 798778Integrin beta-1PRO_0000016334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 451 Publication
    Disulfide bondi35 ↔ 4641 Publication
    Disulfide bondi38 ↔ 641 Publication
    Disulfide bondi48 ↔ 751 Publication
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi207 ↔ 2131 Publication
    Glycosylationi212 – 2121N-linked (GlcNAc...)1 Publication
    Disulfide bondi261 ↔ 3011 Publication
    Glycosylationi269 – 2691N-linked (GlcNAc...)1 Publication
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi401 ↔ 4151 Publication
    Glycosylationi403 – 4031N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi406 – 4061N-linked (GlcNAc...)3 Publications
    Glycosylationi411 – 4111N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 4621 Publication
    Disulfide bondi466 ↔ 6911 Publication
    Disulfide bondi477 ↔ 489By similarity
    Glycosylationi481 – 4811N-linked (GlcNAc...)1 Publication
    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 – 7831PhosphotyrosineBy similarity
    Modified residuei794 – 7941N6-acetyllysine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP05556.
    PaxDbiP05556.
    PRIDEiP05556.

    PTM databases

    PhosphoSiteiP05556.

    Miscellaneous databases

    PMAP-CutDBQ8WUM6.

    Expressioni

    Tissue specificityi

    Isoform 1 is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4, rather than isoform 3, is selectively expressed in peripheral T-cells. Isoform 3 is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle).6 Publications

    Gene expression databases

    ArrayExpressiP05556.
    BgeeiP05556.
    GenevestigatoriP05556.

    Organism-specific databases

    HPAiCAB003434.

    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 FGR and HCK. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with RAB21. 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 HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses. Interacts with FLNA, FLNB and RANBP9. Isoform 5 interacts with ACE2. Isoform 1 interacts with the C-terminal region of FLNC. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2; the interaction is inhibited in presence of ITGB1BP1. 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 human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts with ACAP1; required for ITGB1 recycling. Interacts with ASAP3. Isoform 5 interacts with alpha-7A and alpha-7B in adult skeletal muscle. Isoform 5 interacts with alpha-7B in cardiomyocytes of adult heart.25 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANGPTL4Q9BY762EBI-703066,EBI-2968146
    BMRF2P031922EBI-703066,EBI-9348955From a different organism.
    CSF2RBP329275EBI-703066,EBI-1809771
    ENGP178133EBI-703066,EBI-2834630
    FABP3P054132EBI-703066,EBI-704216
    FLNAP213335EBI-703066,EBI-350432
    ITGA2P173013EBI-703066,EBI-702960
    ITGA4P136123EBI-703066,EBI-703044
    LYNP079484EBI-703066,EBI-79452
    PTPN1P180312EBI-703066,EBI-968788
    PXNP490232EBI-6082935,EBI-702209
    Rab21P352823EBI-703066,EBI-1993555From a different organism.
    TLN1Q9Y4902EBI-703066,EBI-2462036

    Protein-protein interaction databases

    BioGridi109894. 65 interactions.
    DIPiDIP-312N.
    IntActiP05556. 39 interactions.
    MINTiMINT-140089.

    Structurei

    Secondary structure

    1
    798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni36 – 383
    Beta strandi39 – 413
    Helixi67 – 704
    Turni71 – 744
    Turni77 – 793
    Beta strandi86 – 916
    Turni108 – 1103
    Beta strandi118 – 1236
    Beta strandi131 – 1366
    Beta strandi143 – 1508
    Helixi153 – 1553
    Helixi156 – 1627
    Helixi165 – 1739
    Turni174 – 1763
    Beta strandi178 – 18710
    Turni193 – 1953
    Turni200 – 2045
    Beta strandi209 – 2113
    Beta strandi218 – 22710
    Helixi229 – 2368
    Beta strandi245 – 2495
    Helixi251 – 26010
    Helixi262 – 2654
    Beta strandi269 – 28012
    Turni285 – 2884
    Helixi289 – 2913
    Turni311 – 3133
    Helixi319 – 32810
    Beta strandi331 – 3388
    Helixi339 – 3413
    Helixi342 – 35110
    Beta strandi355 – 3606
    Helixi367 – 37913
    Beta strandi382 – 3865
    Beta strandi393 – 4008
    Helixi402 – 4043
    Beta strandi406 – 4083
    Helixi409 – 4135
    Beta strandi423 – 43412
    Beta strandi438 – 44710
    Beta strandi454 – 4607
    Helixi752 – 76918
    Helixi770 – 7723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K11model-B786-797[»]
    1LHAmodel-A86-543[»]
    3G9WX-ray2.16C/D752-785[»]
    3T9KX-ray2.30A/B758-769[»]
    3VI3X-ray2.90B/D21-465[»]
    3VI4X-ray2.90B/D21-465[»]
    4DX9X-ray3.006/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z784-798[»]
    ProteinModelPortaliP05556.
    SMRiP05556. Positions 25-787.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05556.

    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 ACAP1
    Regioni785 – 7928Interaction with ITGB1BP1

    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.
    HOVERGENiHBG006190.
    KOiK05719.
    OMAiENNVYTM.
    OrthoDBiEOG7T7GSB.
    PhylomeDBiP05556.
    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 (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05556-1) [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

    MNLQPIFWIG LISSVCCVFA QTDENRCLKA NAKSCGECIQ AGPNCGWCTN    50
    STFLQEGMPT SARCDDLEAL KKKGCPPDDI ENPRGSKDIK KNKNVTNRSK 100
    GTAEKLKPED ITQIQPQQLV LRLRSGEPQT FTLKFKRAED YPIDLYYLMD 150
    LSYSMKDDLE NVKSLGTDLM NEMRRITSDF RIGFGSFVEK TVMPYISTTP 200
    AKLRNPCTSE QNCTSPFSYK NVLSLTNKGE VFNELVGKQR ISGNLDSPEG 250
    GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ 300
    CHLENNMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN 350
    LIPKSAVGTL SANSSNVIQL IIDAYNSLSS EVILENGKLS EGVTISYKSY 400
    CKNGVNGTGE NGRKCSNISI GDEVQFEISI TSNKCPKKDS DSFKIRPLGF 450
    TEEVEVILQY ICECECQSEG IPESPKCHEG NGTFECGACR CNEGRVGRHC 500
    ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK RDNTNEIYSG 550
    KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTSTCE 600
    ASNGQICNGR GICECGVCKC TDPKFQGQTC EMCQTCLGVC AEHKECVQCR 650
    AFNKGEKKDT CTQECSYFNI TKVESRDKLP QPVQPDPVSH CKEKDVDDCW 700
    FYFTYSVNGN NEVMVHVVEN PECPTGPDII PIVAGVVAGI VLIGLALLLI 750
    WKLLMIIHDR REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK 798
    Length:798
    Mass (Da):88,415
    Last modified:December 16, 2008 - v2
    Checksum:iDE35979C1625578C
    GO
    Isoform 2 (identifier: P05556-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta-1B

    The sequence of this isoform differs from the canonical sequence as follows:
         778-798: GENPIYKSAVTTVVNPKYEGK → VSYKTSKKQSGL

    Show »
    Length:789
    Mass (Da):87,446
    Checksum:i75834A92490CFBB0
    GO
    Isoform 3 (identifier: P05556-3) [UniParc]FASTAAdd to Basket

    Also known as: Beta-1C

    The sequence of this isoform differs from the canonical sequence as follows:
         778-798: GENPIYKSAVTTVVNPKYEGK → SLSVAQPGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

    Show »
    Length:825
    Mass (Da):91,620
    Checksum:iD5DCB510A049FBEC
    GO
    Isoform 4 (identifier: P05556-4) [UniParc]FASTAAdd to Basket

    Also known as: Beta-1C-2

    The sequence of this isoform differs from the canonical sequence as follows:
         778-798: GENPIYKSAVTTVVNPKYEGK → PGVQWCDISSLQPLTSRFQQFSCLSLPSTWDYRVKILFIRVP

    Show »
    Length:819
    Mass (Da):91,034
    Checksum:i5838866B6DA6CECC
    GO
    Isoform 5 (identifier: P05556-5) [UniParc]FASTAAdd to Basket

    Also known as: Beta-1D

    The sequence of this isoform differs from the canonical sequence as follows:
         778-798: GENPIYKSAVTTVVNPKYEGK → QENPIYKSPINNFKNPNYGRKAGL

    Show »
    Length:801
    Mass (Da):88,884
    Checksum:i5A2DA413650A16BE
    GO

    Sequence cautioni

    The sequence CAD97649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121T → H in CAA30790. (PubMed:2958481)Curated
    Sequence conflicti215 – 2151S → T in CAA30790. (PubMed:2958481)Curated
    Sequence conflicti261 – 2655CGSLI → VWMLL in AAI13902. (PubMed:15489334)Curated
    Sequence conflicti385 – 3862EN → DG in AAI13902. (PubMed:15489334)Curated
    Sequence conflicti463 – 4631E → V in BAF84386. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei778 – 79821GENPI…KYEGK → VSYKTSKKQSGL in isoform 2. CuratedVSP_002741Add
    BLAST
    Alternative sequencei778 – 79821GENPI…KYEGK → SLSVAQPGVQWCDISSLQPL TSRFQQFSCLSLPSTWDYRV KILFIRVP in isoform 3. CuratedVSP_002742Add
    BLAST
    Alternative sequencei778 – 79821GENPI…KYEGK → PGVQWCDISSLQPLTSRFQQ FSCLSLPSTWDYRVKILFIR VP in isoform 4. CuratedVSP_002743Add
    BLAST
    Alternative sequencei778 – 79821GENPI…KYEGK → QENPIYKSPINNFKNPNYGR KAGL in isoform 5. CuratedVSP_002744Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07979 mRNA. Translation: CAA30790.1.
    AK291697 mRNA. Translation: BAF84386.1.
    BX537407 mRNA. Translation: CAD97649.1. Different initiation.
    AL365203 Genomic DNA. Translation: CAI14426.1.
    CH471072 Genomic DNA. Translation: EAW85948.1.
    CH471072 Genomic DNA. Translation: EAW85949.1.
    CH471072 Genomic DNA. Translation: EAW85950.1.
    CH471072 Genomic DNA. Translation: EAW85951.1.
    CH471072 Genomic DNA. Translation: EAW85952.1.
    CH471072 Genomic DNA. Translation: EAW85953.1.
    CH471072 Genomic DNA. Translation: EAW85954.1.
    CH471072 Genomic DNA. Translation: EAW85955.1.
    CH471072 Genomic DNA. Translation: EAW85957.1.
    CH471072 Genomic DNA. Translation: EAW85958.1.
    CH471072 Genomic DNA. Translation: EAW85959.1.
    BC020057 mRNA. Translation: AAH20057.1.
    BC113901 mRNA. Translation: AAI13902.1.
    U33879 Genomic DNA. Translation: AAA79832.1.
    U33880, U33879 Genomic DNA. Translation: AAA79833.1.
    U33882, U33879, U33881 Genomic DNA. Translation: AAA79834.1.
    U33882, U33879 Genomic DNA. Translation: AAA79835.1.
    M34189 mRNA. Translation: AAA59182.1.
    M84237 mRNA. Translation: AAA74402.1.
    M84237 mRNA. Translation: AAA74403.1.
    U28252 mRNA. Translation: AAA81366.1.
    CCDSiCCDS7174.1. [P05556-1]
    PIRiB27079.
    RefSeqiNP_002202.2. NM_002211.3. [P05556-1]
    NP_391988.1. NM_033668.2. [P05556-5]
    NP_596867.1. NM_133376.2. [P05556-1]
    XP_005252505.1. XM_005252448.1. [P05556-5]
    UniGeneiHs.643813.

    Genome annotation databases

    EnsembliENST00000302278; ENSP00000303351; ENSG00000150093. [P05556-1]
    ENST00000396033; ENSP00000379350; ENSG00000150093. [P05556-1]
    ENST00000423113; ENSP00000388694; ENSG00000150093. [P05556-5]
    GeneIDi3688.
    KEGGihsa:3688.
    UCSCiuc001iwr.4. human. [P05556-5]
    uc001iws.4. human. [P05556-1]

    Polymorphism databases

    DMDMi218563324.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    CD29 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07979 mRNA. Translation: CAA30790.1 .
    AK291697 mRNA. Translation: BAF84386.1 .
    BX537407 mRNA. Translation: CAD97649.1 . Different initiation.
    AL365203 Genomic DNA. Translation: CAI14426.1 .
    CH471072 Genomic DNA. Translation: EAW85948.1 .
    CH471072 Genomic DNA. Translation: EAW85949.1 .
    CH471072 Genomic DNA. Translation: EAW85950.1 .
    CH471072 Genomic DNA. Translation: EAW85951.1 .
    CH471072 Genomic DNA. Translation: EAW85952.1 .
    CH471072 Genomic DNA. Translation: EAW85953.1 .
    CH471072 Genomic DNA. Translation: EAW85954.1 .
    CH471072 Genomic DNA. Translation: EAW85955.1 .
    CH471072 Genomic DNA. Translation: EAW85957.1 .
    CH471072 Genomic DNA. Translation: EAW85958.1 .
    CH471072 Genomic DNA. Translation: EAW85959.1 .
    BC020057 mRNA. Translation: AAH20057.1 .
    BC113901 mRNA. Translation: AAI13902.1 .
    U33879 Genomic DNA. Translation: AAA79832.1 .
    U33880 , U33879 Genomic DNA. Translation: AAA79833.1 .
    U33882 , U33879 , U33881 Genomic DNA. Translation: AAA79834.1 .
    U33882 , U33879 Genomic DNA. Translation: AAA79835.1 .
    M34189 mRNA. Translation: AAA59182.1 .
    M84237 mRNA. Translation: AAA74402.1 .
    M84237 mRNA. Translation: AAA74403.1 .
    U28252 mRNA. Translation: AAA81366.1 .
    CCDSi CCDS7174.1. [P05556-1 ]
    PIRi B27079.
    RefSeqi NP_002202.2. NM_002211.3. [P05556-1 ]
    NP_391988.1. NM_033668.2. [P05556-5 ]
    NP_596867.1. NM_133376.2. [P05556-1 ]
    XP_005252505.1. XM_005252448.1. [P05556-5 ]
    UniGenei Hs.643813.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K11 model - B 786-797 [» ]
    1LHA model - A 86-543 [» ]
    3G9W X-ray 2.16 C/D 752-785 [» ]
    3T9K X-ray 2.30 A/B 758-769 [» ]
    3VI3 X-ray 2.90 B/D 21-465 [» ]
    3VI4 X-ray 2.90 B/D 21-465 [» ]
    4DX9 X-ray 3.00 6/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z 784-798 [» ]
    ProteinModelPortali P05556.
    SMRi P05556. Positions 25-787.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109894. 65 interactions.
    DIPi DIP-312N.
    IntActi P05556. 39 interactions.
    MINTi MINT-140089.

    Chemistry

    BindingDBi P05556.
    ChEMBLi CHEMBL2095226.

    PTM databases

    PhosphoSitei P05556.

    Polymorphism databases

    DMDMi 218563324.

    Proteomic databases

    MaxQBi P05556.
    PaxDbi P05556.
    PRIDEi P05556.

    Protocols and materials databases

    DNASUi 3688.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302278 ; ENSP00000303351 ; ENSG00000150093 . [P05556-1 ]
    ENST00000396033 ; ENSP00000379350 ; ENSG00000150093 . [P05556-1 ]
    ENST00000423113 ; ENSP00000388694 ; ENSG00000150093 . [P05556-5 ]
    GeneIDi 3688.
    KEGGi hsa:3688.
    UCSCi uc001iwr.4. human. [P05556-5 ]
    uc001iws.4. human. [P05556-1 ]

    Organism-specific databases

    CTDi 3688.
    GeneCardsi GC10M033189.
    HGNCi HGNC:6153. ITGB1.
    HPAi CAB003434.
    MIMi 135630. gene.
    neXtProti NX_P05556.
    PharmGKBi PA29953.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287997.
    HOVERGENi HBG006190.
    KOi K05719.
    OMAi ENNVYTM.
    OrthoDBi EOG7T7GSB.
    PhylomeDBi P05556.
    TreeFami TF105392.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_12560. Basigin interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.
    REACT_160131. Fibronectin matrix formation.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_169262. Laminin interactions.
    REACT_19200. Other semaphorin interactions.
    REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
    REACT_22272. Signal transduction by L1.
    REACT_22292. CHL1 interactions.
    SABIO-RK P05556.
    SignaLinki P05556.

    Miscellaneous databases

    ChiTaRSi ITGB1. human.
    EvolutionaryTracei P05556.
    GeneWikii CD29.
    GenomeRNAii 3688.
    NextBioi 14435.
    PMAP-CutDB Q8WUM6.
    PROi P05556.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05556.
    Bgeei P05556.
    Genevestigatori P05556.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Endometrium.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Skin.
    7. "Expression and functional analysis of a cytoplasmic domain variant of the beta 1 integrin subunit."
      Balzac F., Belkin A.M., Koteliansky V.E., Balabanov Y.V., Altruda F., Silengo L., Tarone G.
      J. Cell Biol. 121:171-178(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 717-757, CHARACTERIZATION OF BETA-1B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. "Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility."
      Balzac F., Retta S.F., Albini A., Melchiorri A., Koteliansky V.E., Geuna M., Silengo L., Tarone G.
      J. Cell Biol. 127:557-565(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 717-757, FUNCTION.
    9. "A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing."
      Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G., Silengo L.
      Gene 95:261-266(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    10. "An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain."
      Languino L.R., Ruoslahti E.
      J. Biol. Chem. 267:7116-7120(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    11. "Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle."
      Zhidkova N.I., Belkin A.M., Mayne R.
      Biochem. Biophys. Res. Commun. 214:279-285(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    12. "A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle."
      van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A.
      FEBS Lett. 369:340-344(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
    13. "Identification of beta1C-2, a novel variant of the integrin beta1 subunit generated by utilization of an alternative splice acceptor site in exon C."
      Svineng G., Faessler R., Johansson S.
      Biochem. J. 330:1255-1263(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4), TISSUE SPECIFICITY.
    14. "Interaction of ACE2 and integrin beta1 in failing human heart."
      Lin Q., Keller R.S., Weaver B., Zisman L.S.
      Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 775-784 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ACE2.
    15. "Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2."
      Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J., Finberg R.W.
      J. Virol. 67:6847-6852(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN ECHOVIRUS 1 AND HUMAN ECHOVIRUS 8 CAPSID PROTEINS.
    16. "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: SUBCELLULAR LOCATION.
    17. "Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin."
      Sasaki T., Brakebusch C., Engel J., Timpl R.
      EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LGALS3BP.
    18. "The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."
      Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
      Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    19. "A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation."
      Li J., Mayne R., Wu C.
      J. Cell Biol. 147:1391-1398(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NMRK2.
      Tissue: Heart.
    20. "Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation."
      Zhang J., Clatterbuck R.E., Rigamonti D., Chang D.D., Dietz H.C.
      Hum. Mol. Genet. 10:2953-2960(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1.
    21. "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement."
      Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C.
      J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
      van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
      J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNA AND FLNB, MUTAGENESIS OF GLY-778 AND ALA-786.
    23. "The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
      Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
      J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1, MUTAGENESIS OF 786-ALA--VAL-791.
    24. "Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha."
      Bouvard D., Vignoud L., Dupe-Manet S., Abed N., Fournier H.N., Vincent-Monegat C., Retta S.F., Fassler R., Block M.R.
      J. Biol. Chem. 278:6567-6574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ITGB1BP1.
    25. "RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."
      Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E.
      J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9.
    26. "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: INTERACTION WITH ITGA3; LGALS3 AND CSPG4.
    27. "Myosin-X provides a motor-based link between integrins and the cytoskeleton."
      Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S.
      Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYO10.
    28. "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration."
      Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.
      Dev. Cell 9:663-673(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACAP1, SUBCELLULAR LOCATION.
    29. "The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins."
      Gontier Y., Taivainen A., Fontao L., Sonnenberg A., van der Flier A., Carpen O., Faulkner G., Borradori L.
      J. Cell Sci. 118:3739-3749(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNB AND FLNC.
    30. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406.
      Tissue: Plasma.
    31. "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins."
      Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J.
      J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB21.
    32. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    33. "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
      Chuang N.N., Huang C.C.
      Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
    34. "Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments."
      Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., Ozanne B.W., Norman J.C.
      Dev. Cell 13:496-510(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB25.
    35. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    36. "JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation."
      Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O., Bourdoulous S.
      J. Cell Biol. 183:1159-1173(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, INTERACTION WITH AMICA1.
    37. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212; ASN-481 AND ASN-669.
      Tissue: Liver.
    38. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-403; ASN-406 AND ASN-411.
      Tissue: Leukemic T-cell.
    39. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    40. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-794, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry."
      Feire A.L., Roy R.M., Manley K., Compton T.
      J. Virol. 84:10026-10037(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 GB.
    42. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    43. "ACAP4 protein cooperates with Grb2 protein to orchestrate epidermal growth factor-stimulated integrin beta1 recycling in cell migration."
      Yu X., Wang F., Liu H., Adams G., Aikhionbare F., Liu D., Cao X., Fan L., Hu G., Chen Y., Frost A., Partridge E., Ding X., Yao X.
      J. Biol. Chem. 286:43735-43747(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASAP3.
    44. "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, INTERACTION WITH FERMT2 AND TLN1, MUTAGENESIS OF VAL-787.
    45. "Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins."
      Qu H., Tu Y., Shi X., Larjava H., Saleem M.A., Shattil S.J., Fukuda K., Qin J., Kretzler M., Wu C.
      J. Cell Sci. 124:879-891(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FERMT2.
    46. "Mechanistic insights into regulated cargo binding by ACAP1 protein."
      Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.
      J. Biol. Chem. 287:28675-28685(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 758-769 IN COMPLEX WITH ACAP1, INTERACTION WITH ACAP1 AND ITGA5, SUBCELLULAR LOCATION, MUTAGENESIS OF 760-ARG-ARG-761; 762-GLU--PHE-767 AND 768-LYS-GLU-769.
    47. "Crystal structure of alpha5beta1 integrin ectodomain: atomic details of the fibronectin receptor."
      Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.
      J. Cell Biol. 197:131-140(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-465 IN COMPLEX WITH ANTIBODY; ITGA5 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-269 AND ASN-406, METAL-BINDING SITES, SUBUNIT.
    48. "Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation."
      Liu W., Draheim K.M., Zhang R., Calderwood D.A., Boggon T.J.
      Mol. Cell 49:719-729(2013)
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 784-798 IN COMPLEX WITH ITGB1BP1, INTERACTION WITH ITGB1BP1, MUTAGENESIS OF THR-788; VAL-790; ASN-792 AND TYR-795.

    Entry informationi

    Entry nameiITB1_HUMAN
    AccessioniPrimary (citable) accession number: P05556
    Secondary accession number(s): A8K6N2
    , D3DRX9, D3DRY3, D3DRY4, D3DRY5, P78466, P78467, Q13089, Q13090, Q13091, Q13212, Q14622, Q14647, Q29RW2, Q7Z3V1, Q8WUM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 186 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3