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O14713

- ITBP1_HUMAN

UniProt

O14713 - ITBP1_HUMAN

Protein

Integrin beta-1-binding protein 1

Gene

ITGB1BP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin-and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter.9 Publications

    GO - Molecular functioni

    1. GDP-dissociation inhibitor activity Source: UniProtKB
    2. integrin binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein complex binding Source: UniProtKB
    5. protein transporter activity Source: UniProtKB

    GO - Biological processi

    1. activation of protein kinase B activity Source: UniProtKB
    2. biomineral tissue development Source: UniProtKB-KW
    3. blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: UniProtKB
    4. cell differentiation Source: UniProtKB-KW
    5. cell-matrix adhesion Source: UniProtKB
    6. cell migration Source: HGNC
    7. cellular response to fibroblast growth factor stimulus Source: UniProtKB
    8. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    9. integrin activation Source: UniProtKB
    10. integrin-mediated signaling pathway Source: UniProtKB
    11. intracellular signal transduction Source: ProtInc
    12. myoblast migration Source: UniProtKB
    13. negative regulation of cell adhesion involved in substrate-bound cell migration Source: UniProtKB
    14. negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
    15. negative regulation of cell proliferation Source: UniProtKB
    16. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    17. negative regulation of fibroblast migration Source: UniProtKB
    18. negative regulation of focal adhesion assembly Source: UniProtKB
    19. negative regulation of protein binding Source: UniProtKB
    20. negative regulation of protein kinase activity Source: UniProtKB
    21. negative regulation of protein targeting to membrane Source: UniProtKB
    22. negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
    23. Notch signaling pathway Source: UniProtKB-KW
    24. positive regulation of cell division Source: UniProtKB-KW
    25. positive regulation of cell proliferation Source: UniProtKB
    26. positive regulation of endothelial cell migration Source: UniProtKB
    27. positive regulation of focal adhesion assembly Source: Ensembl
    28. positive regulation of Notch signaling pathway Source: UniProtKB
    29. positive regulation of protein kinase B signaling Source: UniProtKB
    30. positive regulation of protein targeting to membrane Source: UniProtKB
    31. positive regulation of stress fiber assembly Source: UniProtKB
    32. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    33. protein transport Source: UniProtKB
    34. receptor clustering Source: UniProtKB
    35. regulation of blood vessel size Source: UniProtKB
    36. regulation of Cdc42 GTPase activity Source: UniProtKB
    37. regulation of cell adhesion mediated by integrin Source: UniProtKB
    38. regulation of integrin-mediated signaling pathway Source: UniProtKB
    39. transcription, DNA-templated Source: UniProtKB-KW
    40. tube formation Source: UniProtKB

    Keywords - Molecular functioni

    Mitogen

    Keywords - Biological processi

    Angiogenesis, Biomineralization, Cell adhesion, Differentiation, Notch signaling pathway, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin beta-1-binding protein 1
    Alternative name(s):
    Integrin cytoplasmic domain-associated protein 1
    Short name:
    ICAP-1
    Gene namesi
    Name:ITGB1BP1
    Synonyms:ICAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:23927. ITGB1BP1.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cell projectionlamellipodium. Cell projectionruffle
    Note: Nucleocytoplasmic shuttling protein; shuttles between nucleus and cytoplasm in a integrin-dependent manner; probably sequestered in the cytosol by ITGB1. Its localization is dependent on the stage of cell spreading on fibronectin; cytoplasmic in case of round cells, corresponding to the initial step of cell spreading, or nuclear in case of well spread cells. Colocalizes with ROCK1 and NME2 at beta-1 integrin engagement sites. Together with ITGB1 and NME2 is recruited to beta-1 integrin-rich peripheral ruffles and lamellipodia during initial cell spreading on fibronectin and/or collagen.

    GO - Cellular componenti

    1. cell periphery Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: HGNC
    5. extracellular vesicular exosome Source: UniProt
    6. lamellipodium Source: HGNC
    7. membrane Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. plasma membrane Source: UniProtKB
    11. ruffle Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 72KK → AA: Abolishes nuclear import and transcriptional activity.
    Mutagenesisi38 – 381T → A: Stimulates cell spreading on fibronectin to a similar extent as inhibition of CaMKII. 2 Publications
    Mutagenesisi38 – 381T → D: Changes in cell spreading. 2 Publications
    Mutagenesisi38 – 381T → D: Strong defect in cell spreading. 2 Publications
    Mutagenesisi82 – 821L → A: Reduces ITGB1 binding. 1 Publication
    Mutagenesisi82 – 821L → Q: No effect on ITGB1 binding. 1 Publication
    Mutagenesisi86 – 861L → Q: No effect on ITGB1 binding. 1 Publication
    Mutagenesisi89 – 891I → R: Reduces KRIT1 binding. No effect on ITGB1 binding. 1 Publication
    Mutagenesisi93 – 931D → A: Abolishes KRIT1 binding; when associated with A-96. 1 Publication
    Mutagenesisi96 – 961Q → A: Abolishes KRIT1 binding; when associated with A-93. 1 Publication
    Mutagenesisi135 – 1395LYLII → AYAA: Reduces KRIT1 and ITGB1 binding. 1 Publication
    Mutagenesisi135 – 1351L → A: Abolishes ITGB1 binding. 1 Publication
    Mutagenesisi138 – 1381I → A: Abolishes ITGB1 binding. 2 Publications
    Mutagenesisi139 – 1391I → A: Abolishes ITGB1 binding. 1 Publication
    Mutagenesisi144 – 1441Y → T: Abolishes ITGB1 binding. 1 Publication
    Mutagenesisi184 – 1841C → D: Reduces KRIT1 and ITGB1 binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134913590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 200200Integrin beta-1-binding protein 1PRO_0000084264Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphothreonine; by CaMK21 Publication

    Post-translational modificationi

    Phosphorylation at Thr-38 seems to enhance integrin alpha5beta1-mediated cell adhesion. The degree of phosphorylation is regulated by integrin-dependent cell-matrix interaction.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14713.
    PaxDbiO14713.
    PRIDEiO14713.

    PTM databases

    PhosphoSiteiO14713.

    Expressioni

    Tissue specificityi

    Expressed in endothelial cells and fibroblasts (at protein level). Ubiquitously expressed. Expressed in intestine, colon, testis, ovary, thymus, spleen and prostate.2 Publications

    Gene expression databases

    ArrayExpressiO14713.
    BgeeiO14713.
    CleanExiHS_ITGB1BP1.
    GenevestigatoriO14713.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus and PTB domain) with ROCK1 By similarity. Found in a complex, at least composed of ITGB1BP1, KRIT1 and RAP1A. Interacts (via C-terminal region) with ITGB1 (via C-terminal cytoplasmic tail); the interaction prevents talin TLN1 binding to ITGB1 and KRIT1 and ITGB1 compete for the same binding site. Interacts with KRIT1 (via N-terminal NPXY motif); the interaction induces the opening conformation of KRIT1 and KRIT1 and ITGB1 compete for the same binding site. Isoform 2 does not interact with ITGB1. Interacts with CDC42 (GTP- or GDP-bound form); the interaction is increased with the CDC42-membrane bound forms and prevents both CDC42 activation and cell spreading. Interacts (via C-terminal domain region) with NME2. Interacts with FERMT2 and RAC1.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NME2P223927EBI-2127367,EBI-713693

    Protein-protein interaction databases

    BioGridi114689. 10 interactions.
    IntActiO14713. 7 interactions.
    STRINGi9606.ENSP00000347504.

    Structurei

    Secondary structure

    1
    200
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 7414
    Helixi85 – 9713
    Beta strandi99 – 1013
    Beta strandi109 – 1157
    Beta strandi118 – 1236
    Beta strandi129 – 1346
    Helixi135 – 1373
    Beta strandi138 – 1458
    Beta strandi148 – 1503
    Beta strandi153 – 1608
    Beta strandi167 – 1759
    Helixi177 – 19216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K11model-A58-196[»]
    4DX8X-ray2.54A/B/D/E49-200[»]
    4DX9X-ray3.000/1/2/3/4/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i/k/m/o/q/s/u/w/y49-200[»]
    4JIFX-ray1.70A49-200[»]
    ProteinModelPortaliO14713.
    SMRiO14713. Positions 55-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 200143PIDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni136 – 1394Interaction with KRIT1
    Regioni139 – 1413Interaction with ITGB1

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi6 – 72Nuclear localization signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 5748Ser/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PID domain.Curated

    Phylogenomic databases

    eggNOGiNOG45114.
    HOGENOMiHOG000015089.
    HOVERGENiHBG052155.
    InParanoidiO14713.
    OMAiRMLCYDD.
    OrthoDBiEOG7WT447.
    PhylomeDBiO14713.
    TreeFamiTF105393.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR019517. Integrin-bd_ICAP-1.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view]
    PfamiPF10480. ICAP-1_inte_bdg. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14713-1) [UniParc]FASTAAdd to Basket

    Also known as: ICAP1-alpha

    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

    MFRKGKKRHS SSSSQSSEIS TKSKSVDSSL GGLSRSSTVA SLDTDSTKSS    50
    GQSNNNSDTC AEFRIKYVGA IEKLKLSEGK GLEGPLDLIN YIDVAQQDGK 100
    LPFVPPEEEF IMGVSKYGIK VSTSDQYDVL HRHALYLIIR MVCYDDGLGA 150
    GKSLLALKTT DASNEEYSLW VYQCNSLEQA QAICKVLSTA FDSVLTSEKP 200

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Length:200
    Mass (Da):21,782
    Last modified:January 1, 1998 - v1
    Checksum:i0F041238E68FBE23
    GO
    Isoform 2 (identifier: O14713-2) [UniParc]FASTAAdd to Basket

    Also known as: ICAP1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         128-177: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:150
    Mass (Da):16,140
    Checksum:iFC6E3D387878DB81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501A → V in AAH12264. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 17750Missing in isoform 2. 1 PublicationVSP_003898Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012023 mRNA. Translation: AAB88671.1.
    AF012024 mRNA. Translation: AAB88672.1.
    CH471053 Genomic DNA. Translation: EAX00992.1.
    CH471053 Genomic DNA. Translation: EAX00995.1.
    CH471053 Genomic DNA. Translation: EAX01000.1.
    CH471053 Genomic DNA. Translation: EAX01001.1.
    AC080162 Genomic DNA. Translation: AAY14857.1.
    CH471053 Genomic DNA. Translation: EAX00993.1.
    CH471053 Genomic DNA. Translation: EAX00997.1.
    BC012264 mRNA. Translation: AAH12264.1.
    CCDSiCCDS1662.1. [O14713-1]
    CCDS1663.1. [O14713-2]
    RefSeqiNP_004754.1. NM_004763.3. [O14713-1]
    NP_071729.1. NM_022334.3. [O14713-2]
    XP_005246240.1. XM_005246183.2. [O14713-1]
    XP_005246241.1. XM_005246184.2. [O14713-1]
    XP_005246242.1. XM_005246185.2. [O14713-1]
    XP_005246243.1. XM_005246186.2. [O14713-1]
    XP_005246244.1. XM_005246187.2. [O14713-1]
    XP_005246246.1. XM_005246189.2. [O14713-2]
    XP_006711966.1. XM_006711903.1. [O14713-1]
    UniGeneiHs.467662.

    Genome annotation databases

    EnsembliENST00000238091; ENSP00000238091; ENSG00000119185. [O14713-2]
    ENST00000355346; ENSP00000347504; ENSG00000119185. [O14713-1]
    ENST00000360635; ENSP00000353850; ENSG00000119185. [O14713-1]
    ENST00000488451; ENSP00000419524; ENSG00000119185. [O14713-2]
    GeneIDi9270.
    KEGGihsa:9270.
    UCSCiuc002qzj.3. human. [O14713-1]
    uc002qzk.3. human. [O14713-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012023 mRNA. Translation: AAB88671.1 .
    AF012024 mRNA. Translation: AAB88672.1 .
    CH471053 Genomic DNA. Translation: EAX00992.1 .
    CH471053 Genomic DNA. Translation: EAX00995.1 .
    CH471053 Genomic DNA. Translation: EAX01000.1 .
    CH471053 Genomic DNA. Translation: EAX01001.1 .
    AC080162 Genomic DNA. Translation: AAY14857.1 .
    CH471053 Genomic DNA. Translation: EAX00993.1 .
    CH471053 Genomic DNA. Translation: EAX00997.1 .
    BC012264 mRNA. Translation: AAH12264.1 .
    CCDSi CCDS1662.1. [O14713-1 ]
    CCDS1663.1. [O14713-2 ]
    RefSeqi NP_004754.1. NM_004763.3. [O14713-1 ]
    NP_071729.1. NM_022334.3. [O14713-2 ]
    XP_005246240.1. XM_005246183.2. [O14713-1 ]
    XP_005246241.1. XM_005246184.2. [O14713-1 ]
    XP_005246242.1. XM_005246185.2. [O14713-1 ]
    XP_005246243.1. XM_005246186.2. [O14713-1 ]
    XP_005246244.1. XM_005246187.2. [O14713-1 ]
    XP_005246246.1. XM_005246189.2. [O14713-2 ]
    XP_006711966.1. XM_006711903.1. [O14713-1 ]
    UniGenei Hs.467662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K11 model - A 58-196 [» ]
    4DX8 X-ray 2.54 A/B/D/E 49-200 [» ]
    4DX9 X-ray 3.00 0/1/2/3/4/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e/g/i/k/m/o/q/s/u/w/y 49-200 [» ]
    4JIF X-ray 1.70 A 49-200 [» ]
    ProteinModelPortali O14713.
    SMRi O14713. Positions 55-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114689. 10 interactions.
    IntActi O14713. 7 interactions.
    STRINGi 9606.ENSP00000347504.

    PTM databases

    PhosphoSitei O14713.

    Proteomic databases

    MaxQBi O14713.
    PaxDbi O14713.
    PRIDEi O14713.

    Protocols and materials databases

    DNASUi 9270.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238091 ; ENSP00000238091 ; ENSG00000119185 . [O14713-2 ]
    ENST00000355346 ; ENSP00000347504 ; ENSG00000119185 . [O14713-1 ]
    ENST00000360635 ; ENSP00000353850 ; ENSG00000119185 . [O14713-1 ]
    ENST00000488451 ; ENSP00000419524 ; ENSG00000119185 . [O14713-2 ]
    GeneIDi 9270.
    KEGGi hsa:9270.
    UCSCi uc002qzj.3. human. [O14713-1 ]
    uc002qzk.3. human. [O14713-2 ]

    Organism-specific databases

    CTDi 9270.
    GeneCardsi GC02M009496.
    HGNCi HGNC:23927. ITGB1BP1.
    MIMi 607153. gene.
    neXtProti NX_O14713.
    PharmGKBi PA134913590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45114.
    HOGENOMi HOG000015089.
    HOVERGENi HBG052155.
    InParanoidi O14713.
    OMAi RMLCYDD.
    OrthoDBi EOG7WT447.
    PhylomeDBi O14713.
    TreeFami TF105393.

    Miscellaneous databases

    ChiTaRSi ITGB1BP1. human.
    GeneWikii ITGB1BP1.
    GenomeRNAii 9270.
    NextBioi 34745.
    PROi O14713.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14713.
    Bgeei O14713.
    CleanExi HS_ITGB1BP1.
    Genevestigatori O14713.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR019517. Integrin-bd_ICAP-1.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    [Graphical view ]
    Pfami PF10480. ICAP-1_inte_bdg. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin."
      Chang D.D., Wong C., Smith H., Liu J.
      J. Cell Biol. 138:1149-1157(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH ITGB1, PHOSPHORYLATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Interaction of the integrin beta1 cytoplasmic domain with ICAP-1 protein."
      Zhang X.A., Hemler M.E.
      J. Biol. Chem. 274:11-19(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGB1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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).
      Tissue: Ovary.
    6. "Calcium/calmodulin-dependent protein kinase II controls integrin alpha5beta1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1alpha."
      Bouvard D., Block M.R.
      Biochem. Biophys. Res. Commun. 252:46-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-38, MUTAGENESIS OF THR-38.
    7. "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: FUNCTION, INTERACTION WITH ITGB1 AND KRIT1.
    8. "KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis."
      Zawistowski J.S., Serebriiskii I.G., Lee M.F., Golemis E.A., Marchuk D.A.
      Hum. Mol. Genet. 11:389-396(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KRIT1.
    9. "Molecular basis for interaction between Icap1alpha PTB domain and beta 1 integrin."
      Chang D.D., Hoang B.Q., Liu J., Springer T.A.
      J. Biol. Chem. 277:8140-8145(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1, MUTAGENESIS OF THR-38; LEU-82; LEU-86; LEU-135; ILE-138; ILE-139 AND TYR-144, 3D-STRUCTURE MODELING.
    10. "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: FUNCTION, INTERACTION WITH NME2, SUBCELLULAR LOCATION.
    11. "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: FUNCTION, INTERACTION WITH CDC42; ITGB1 AND RAC1.
    12. "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 ITGB1, SUBCELLULAR LOCATION.
    13. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    14. "Nuclear translocation of integrin cytoplasmic domain-associated protein 1 stimulates cellular proliferation."
      Fournier H.N., Dupe-Manet S., Bouvard D., Luton F., Degani S., Block M.R., Retta S.F., Albiges-Rizo C.
      Mol. Biol. Cell 16:1859-1871(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 6-LYS-LYS-7 AND ILE-138.
    15. "Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1."
      Beraud-Dufour S., Gautier R., Albiges-Rizo C., Chardin P., Faurobert E.
      FEBS J. 274:5518-5532(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH KRIT1 AND RAP1A, INTERACTION WITH KRIT1.
    16. "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting angiogenesis."
      Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E., Adam M.G., Telzerow A., Augustin H.G., Fischer A.
      Circ. Res. 107:592-601(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "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 ITGB1 AND FERMT2.
    18. "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 0:0-0(2013)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 49-200 IN COMPLEXES WITH KRIT1 AND ITGB1, FUNCTION, INTERACTION WITH KRIT1 AND ITGB1, MUTAGENESIS OF ILE-89; ASP-93; GLN-96; 135-LEU--ILE-139 AND CYS-184.

    Entry informationi

    Entry nameiITBP1_HUMAN
    AccessioniPrimary (citable) accession number: O14713
    Secondary accession number(s): D6W4Y9, O14714, Q53RS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3