CIB1_HUMAN
ID CIB1_HUMAN Reviewed; 191 AA.
AC Q99828; B5BU40; H6WJF3; O00693; O00735; Q6IB49; Q96J54; Q99971;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Calcium and integrin-binding protein 1;
DE Short=CIB;
DE AltName: Full=Calcium- and integrin-binding protein;
DE Short=CIBP;
DE AltName: Full=Calmyrin;
DE AltName: Full=DNA-PKcs-interacting protein;
DE AltName: Full=Kinase-interacting protein;
DE Short=KIP;
DE AltName: Full=SNK-interacting protein 2-28;
DE Short=SIP2-28;
GN Name=CIB1; Synonyms=CIB, KIP, PRKDCIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGA2B, TISSUE
RP SPECIFICITY, AND CALCIUM-BINDING.
RC TISSUE=Fetal liver;
RX PubMed=9030514; DOI=10.1074/jbc.272.8.4651;
RA Naik U.P., Patel P.M., Parise L.V.;
RT "Identification of a novel calcium-binding protein that interacts with the
RT integrin alphaIIb cytoplasmic domain.";
RL J. Biol. Chem. 272:4651-4654(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PRKDC, TISSUE
RP SPECIFICITY, AND VARIANT THR-44.
RX PubMed=9372844; DOI=10.1016/s0921-8777(97)00035-9;
RA Wu X., Lieber M.R.;
RT "Interaction between DNA-dependent protein kinase and a novel protein,
RT KIP.";
RL Mutat. Res. 385:13-20(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-44.
RX PubMed=10826701; DOI=10.3109/10425170009015612;
RA Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.;
RT "Genomic structure of mouse and human genes for DNA-PKcs interacting
RT protein (KIP).";
RL DNA Seq. 10:415-418(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INTERACTION
RP WITH PRKD2; PTK2 AND PAK1, SUBCELLULAR LOCATION (ISOFORM 2), TISSUE
RP SPECIFICITY, PHOSPHORYLATION AT SER-118 (ISOFORM 2), AND MUTAGENESIS OF
RP SER-78 AND THR-167.
RC TISSUE=Brain;
RX PubMed=23503467; DOI=10.1038/onc.2013.43;
RA Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V.,
RA Vandoninck S., Van Lint J., Illing A., Seufferlein T.;
RT "A novel splice variant of calcium and integrin-binding protein 1 mediates
RT protein kinase D2-stimulated tumour growth by regulating angiogenesis.";
RL Oncogene 33:1167-1180(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-44.
RA Yuan O.;
RT "SNK, a Ser/Thr protein kinase, associated proteins.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10477286; DOI=10.1042/bj3420729;
RA Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.;
RT "Calcium-dependent properties of CIB binding to the integrin alphaIIb
RT cytoplasmic domain and translocation to the platelet cytoskeleton.";
RL Biochem. J. 342:729-735(1999).
RN [11]
RP MYRISTOYLATION AT GLY-2, AND INTERACTION WITH PSEN2.
RX PubMed=10366599; DOI=10.1083/jcb.145.6.1277;
RA Stabler S.M., Ostrowski L.L., Janicki S.M., Monteiro M.J.;
RT "A myristoylated calcium-binding protein that preferentially interacts with
RT the Alzheimer's disease presenilin 2 protein.";
RL J. Cell Biol. 145:1277-1292(1999).
RN [12]
RP INTERACTION WITH F8.
RX PubMed=11323029; DOI=10.1016/s0049-3848(01)00229-8;
RA Fang X., Chen C., Wang Q., Gu J., Chi C.;
RT "The interaction of the calcium- and integrin-binding protein (CIBP) with
RT the coagulation factor VIII.";
RL Thromb. Res. 102:177-185(2001).
RN [13]
RP INTERACTION WITH NBR1 AND FEZ1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11856312; DOI=10.1046/j.0014-2956.2001.02681.x;
RA Whitehouse C., Chambers J., Howe K., Cobourne M., Sharpe P., Solomon E.;
RT "NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and
RT calcium and integrin binding protein (CIB) and shows developmentally
RT restricted expression in the neural tube.";
RL Eur. J. Biochem. 269:538-545(2002).
RN [14]
RP FUNCTION, INTERACTION WITH RAC3, AND SUBCELLULAR LOCATION.
RX PubMed=11756406; DOI=10.1074/jbc.m105363200;
RA Haataja L., Kaartinen V., Groffen J., Heisterkamp N.;
RT "The small GTPase Rac3 interacts with the integrin-binding protein CIB and
RT promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading.";
RL J. Biol. Chem. 277:8321-8328(2002).
RN [15]
RP INTERACTION WITH UBR5.
RX PubMed=12011095; DOI=10.1074/jbc.m203527200;
RA Henderson M.J., Russell A.J., Hird S., Munoz M., Clancy J.L.,
RA Lehrbach G.M., Calanni S.T., Jans D.A., Sutherland R.L., Watts C.K.;
RT "EDD, the human hyperplastic discs protein, has a role in progesterone
RT receptor coactivation and potential involvement in DNA damage response.";
RL J. Biol. Chem. 277:26468-26478(2002).
RN [16]
RP INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-115;
RP LEU-131; ILE-153 AND PHE-173.
RX PubMed=12023286; DOI=10.1074/jbc.m202983200;
RA Barry W.T., Boudignon-Proudhon C., Shock D.D., McFadden A., Weiss J.M.,
RA Sondek J., Parise L.V.;
RT "Molecular basis of CIB binding to the integrin alpha IIb cytoplasmic
RT domain.";
RL J. Biol. Chem. 277:28877-28883(2002).
RN [17]
RP FUNCTION.
RX PubMed=12714504; DOI=10.1182/blood-2003-02-0591;
RA Naik U.P., Naik M.U.;
RT "Association of CIB with GPIIb/IIIa during outside-in signaling is required
RT for platelet spreading on fibrinogen.";
RL Blood 102:1355-1362(2003).
RN [18]
RP INTERACTION WITH ITGA2B, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
RX PubMed=14992593; DOI=10.1021/bi035432b;
RA Yamniuk A.P., Nguyen L.T., Hoang T.T., Vogel H.J.;
RT "Metal ion binding properties and conformational states of calcium- and
RT integrin-binding protein.";
RL Biochemistry 43:2558-2568(2004).
RN [19]
RP SUBCELLULAR LOCATION, INTERACTION WITH PSEN2, AND MUTAGENESIS OF ASP-127
RP AND GLU-172.
RX PubMed=15475008; DOI=10.1016/j.yexcr.2004.07.020;
RA Zhu J., Stabler S.M., Ames J.B., Baskakov I., Monteiro M.J.;
RT "Calcium binding sequences in calmyrin regulates interaction with
RT presenilin-2.";
RL Exp. Cell Res. 300:440-454(2004).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTK2/FAK1.
RX PubMed=12881299; DOI=10.1182/blood-2003-05-1703;
RA Naik M.U., Naik U.P.;
RT "Calcium-and integrin-binding protein regulates focal adhesion kinase
RT activity during platelet spreading on immobilized fibrinogen.";
RL Blood 102:3629-3636(2003).
RN [21]
RP SUBUNIT.
RX PubMed=15933764;
RA Sobczak A., Blazejczyk M., Piszczek G., Zhao G., Kuznicki J., Wojda U.;
RT "Calcium-binding calmyrin forms stable covalent dimers in vitro, but in
RT vivo is found in monomeric form.";
RL Acta Biochim. Pol. 52:469-476(2005).
RN [22]
RP FUNCTION, AND INTERACTION WITH IFI6 AND BCL2.
RX PubMed=15685448; DOI=10.1007/s00262-004-0645-2;
RA Tahara E. Jr., Tahara H., Kanno M., Naka K., Takeda Y., Matsuzaki T.,
RA Yamazaki R., Ishihara H., Yasui W., Barrett J.C., Ide T., Tahara E.;
RT "G1P3, an interferon inducible gene 6-16, is expressed in gastric cancers
RT and inhibits mitochondrial-mediated apoptosis in gastric cancer cell line
RT TMK-1 cell.";
RL Cancer Immunol. Immunother. 54:729-740(2005).
RN [23]
RP FUNCTION, AND INTERACTION WITH PAK1.
RX PubMed=16061695; DOI=10.1083/jcb.200502090;
RA Leisner T.M., Liu M., Jaffer Z.M., Chernoff J., Parise L.V.;
RT "Essential role of CIB1 in regulating PAK1 activation and cell migration.";
RL J. Cell Biol. 170:465-476(2005).
RN [24]
RP INTERACTION WITH ITGA2B, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
RX PubMed=15883187; DOI=10.1110/ps.041312805;
RA Yamniuk A.P., Vogel H.J.;
RT "Calcium- and magnesium-dependent interactions between calcium- and
RT integrin-binding protein and the integrin alphaIIb cytoplasmic domain.";
RL Protein Sci. 14:1429-1437(2005).
RN [25]
RP INTERACTION WITH ITPR3.
RX PubMed=16723353; DOI=10.1074/jbc.m602175200;
RA White C., Yang J., Monteiro M.J., Foskett J.K.;
RT "CIB1, a ubiquitously expressed Ca2+-binding protein ligand of the InsP3
RT receptor Ca2+ release channel.";
RL J. Biol. Chem. 281:20825-20833(2006).
RN [26]
RP FUNCTION, INTERACTION WITH PAK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP PHE-173.
RX PubMed=16418530; DOI=10.1083/jcb.200505131;
RA Yuan W., Leisner T.M., McFadden A.W., Wang Z., Larson M.K., Clark S.,
RA Boudignon-Proudhon C., Lam S.C., Parise L.V.;
RT "CIB1 is an endogenous inhibitor of agonist-induced integrin alphaIIbbeta3
RT activation.";
RL J. Cell Biol. 172:169-175(2006).
RN [27]
RP FUNCTION, INTERACTION WITH TAS1R2, AND SUBCELLULAR LOCATION.
RX PubMed=18627437; DOI=10.1111/j.1471-4159.2008.05563.x;
RA Hennigs J.K., Burhenne N., Staehler F., Winnig M., Walter B., Meyerhof W.,
RA Schmale H.;
RT "Sweet taste receptor interacting protein CIB1 is a general inhibitor of
RT InsP3-dependent Ca2+ release in vivo.";
RL J. Neurochem. 106:2249-2262(2008).
RN [28]
RP FUNCTION, AND INTERACTION WITH MAP3K5.
RX PubMed=19805025; DOI=10.1073/pnas.0812259106;
RA Yoon K.W., Cho J.H., Lee J.K., Kang Y.H., Chae J.S., Kim Y.M., Kim J.,
RA Kim E.K., Kim S.E., Baik J.H., Naik U.P., Cho S.G., Choi E.J.;
RT "CIB1 functions as a Ca(2+)-sensitive modulator of stress-induced signaling
RT by targeting ASK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17389-17394(2009).
RN [29]
RP SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=19388079; DOI=10.1002/pro.104;
RA Yamniuk A.P., Anderson K.L., Fraser M.E., Vogel H.J.;
RT "Auxiliary Ca2+ binding sites can influence the structure of CIB1.";
RL Protein Sci. 18:1128-1134(2009).
RN [30]
RP INTERACTION WITH SPHK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX PubMed=19854831; DOI=10.1074/jbc.m109.068395;
RA Jarman K.E., Moretti P.A., Zebol J.R., Pitson S.M.;
RT "Translocation of sphingosine kinase 1 to the plasma membrane is mediated
RT by calcium- and integrin-binding protein 1.";
RL J. Biol. Chem. 285:483-492(2010).
RN [31]
RP SUBCELLULAR LOCATION.
RX PubMed=20639889; DOI=10.1038/nm.2181;
RA Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J., Yuan W.,
RA Drexler H., Parise L.V., Molkentin J.D.;
RT "CIB1 is a regulator of pathological cardiac hypertrophy.";
RL Nat. Med. 16:872-879(2010).
RN [32]
RP INTERACTION WITH STMN2, AND SUBCELLULAR LOCATION.
RX PubMed=21215777; DOI=10.1016/j.bbamcr.2010.12.023;
RA Sobczak A., Debowska K., Blazejczyk M., Kreutz M.R., Kuznicki J., Wojda U.;
RT "Calmyrin1 binds to SCG10 protein (stathmin2) to modulate neurite
RT outgrowth.";
RL Biochim. Biophys. Acta 1813:1025-1037(2011).
RN [33]
RP FUNCTION, INTERACTION WITH PLK3, AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=20951827; DOI=10.1016/j.biocel.2010.10.003;
RA Naik M.U., Naik U.P.;
RT "Calcium- and integrin-binding protein 1 regulates microtubule organization
RT and centrosome segregation through polo like kinase 3 during cell cycle
RT progression.";
RL Int. J. Biochem. Cell Biol. 43:120-129(2011).
RN [34]
RP INTERACTION WITH PLK3.
RX PubMed=20473878; DOI=10.1002/ijc.25388;
RA Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P.;
RT "Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in
RT breast cancer cells.";
RL Int. J. Cancer 128:587-596(2011).
RN [35]
RP FUNCTION, AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=21748785; DOI=10.1002/jcb.23255;
RA Naik M.U., Naik U.P.;
RT "Contra-regulation of calcium- and integrin-binding protein 1-induced cell
RT migration on fibronectin by PAK1 and MAP kinase signaling.";
RL J. Cell. Biochem. 112:3289-3299(2011).
RN [36]
RP FUNCTION, AND INTERACTION WITH PLK3.
RX PubMed=21264284; DOI=10.1371/journal.pone.0014513;
RA Kostyak J.C., Naik U.P.;
RT "Calcium- and integrin-binding protein 1 regulates endomitosis and its
RT interaction with Polo-like kinase 3 is enhanced in endomitotic Dami
RT cells.";
RL PLoS ONE 6:E14513-E14513(2011).
RN [37]
RP INTERACTION WITH ITGA2B.
RX PubMed=22779914; DOI=10.1139/o2012-021;
RA Huang H., Bogstie J.N., Vogel H.J.;
RT "Biophysical and structural studies of the human calcium- and integrin-
RT binding protein family: understanding their functional similarities and
RT differences.";
RL Biochem. Cell Biol. 90:646-656(2012).
RN [38]
RP INTERACTION WITH ITGA5 AND ITGAV, AND MUTAGENESIS OF 114-ILE--PHE-117;
RP 152-LEU-ILE-153 AND PHE-173.
RX PubMed=24011356; DOI=10.1021/bi400678y;
RA Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A.,
RA Dokholyan N.V., Leisner T.M., Parise L.V.;
RT "Identification of novel integrin binding partners for calcium and integrin
RT binding protein 1 (CIB1): structural and thermodynamic basis of CIB1
RT promiscuity.";
RL Biochemistry 52:7082-7090(2013).
RN [39]
RP FUNCTION.
RX PubMed=22964641; DOI=10.1038/onc.2012.408;
RA Leisner T.M., Moran C., Holly S.P., Parise L.V.;
RT "CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell
RT death via AKT and ERK signaling.";
RL Oncogene 32:4017-4027(2013).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HPV (MICROBIAL INFECTION),
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH TMC6 AND TMC8,
RP INVOLVEMENT IN EV3, VARIANT EV3 72-ARG--LEU-191 DEL, AND CHARACTERIZATION
RP OF VARIANT EV3 72-ARG--LEU-191 DEL.
RX PubMed=30068544; DOI=10.1084/jem.20170308;
RA de Jong S.J., Crequer A., Matos I., Hum D., Gunasekharan V., Lorenzo L.,
RA Jabot-Hanin F., Imahorn E., Arias A.A., Vahidnezhad H., Youssefian L.,
RA Markle J.G., Patin E., D'Amico A., Wang C.Q.F., Full F., Ensser A.,
RA Leisner T.M., Parise L.V., Bouaziz M., Maya N.P., Cadena X.R., Saka B.,
RA Saeidian A.H., Aghazadeh N., Zeinali S., Itin P., Krueger J.G., Laimins L.,
RA Abel L., Fuchs E., Uitto J., Franco J.L., Burger B., Orth G., Jouanguy E.,
RA Casanova J.L.;
RT "The human CIB1-EVER1-EVER2 complex governs keratinocyte-intrinsic immunity
RT to beta-papillomaviruses.";
RL J. Exp. Med. 215:2289-2310(2018).
RN [42]
RP STRUCTURE BY NMR OF 9-191.
RX PubMed=10822252;
RX DOI=10.1002/(sici)1099-1352(200003/04)13:2<83::aid-jmr491>3.0.co;2-a;
RA Hwang P.M., Vogel H.J.;
RT "Structures of the platelet calcium- and integrin-binding protein and the
RT alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-
RT regulated recognition; homology modelling and NMR studies.";
RL J. Mol. Recognit. 13:83-92(2000).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 9-191 IN COMPLEX WITH CALCIUM
RP IONS, AND SUBUNIT.
RX PubMed=15574431; DOI=10.1074/jbc.m411515200;
RA Gentry H.R., Singer A.U., Betts L., Yang C., Ferrara J.D., Sondek J.,
RA Parise L.V.;
RT "Structural and biochemical characterization of CIB1 delineates a new
RT family of EF-hand-containing proteins.";
RL J. Biol. Chem. 280:8407-8415(2005).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 9-191.
RX PubMed=15840829; DOI=10.1110/ps.041270805;
RA Blamey C.J., Ceccarelli C., Naik U.P., Bahnson B.J.;
RT "The crystal structure of calcium- and integrin-binding protein 1: insights
RT into redox regulated functions.";
RL Protein Sci. 14:1214-1221(2005).
RN [45]
RP STRUCTURE BY NMR OF 1-191 IN COMPLEXES WITH CALCIUM IONS AND MAGNESIUM ION,
RP AND INTERACTION WITH ITGA2B.
RX PubMed=21388953; DOI=10.1074/jbc.m110.179028;
RA Huang H., Ishida H., Yamniuk A.P., Vogel H.J.;
RT "Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with
RT the platelet integrin alphaIIb cytoplasmic domain.";
RL J. Biol. Chem. 286:17181-17192(2011).
RN [46]
RP STRUCTURE BY NMR OF 1-191 IN COMPLEX WITH ITGA2B PEPTIDE AND CALCIUM IONS,
RP AND INTERACTION WITH ITGA2B.
RX PubMed=22283712; DOI=10.1021/ja2111306;
RA Huang H., Vogel H.J.;
RT "Structural basis for the activation of platelet integrin alphaIIbbeta3 by
RT calcium- and integrin-binding protein 1.";
RL J. Am. Chem. Soc. 134:3864-3872(2012).
CC -!- FUNCTION: Calcium-binding protein that plays a role in the regulation
CC of numerous cellular processes, such as cell differentiation, cell
CC division, cell proliferation, cell migration, thrombosis, angiogenesis,
CC cardiac hypertrophy and apoptosis. Involved in bone marrow
CC megakaryocyte differentiation by negatively regulating thrombopoietin-
CC mediated signaling pathway. Participates in the endomitotic cell cycle
CC of megakaryocyte, a form of mitosis in which both karyokinesis and
CC cytokinesis are interrupted. Plays a role in integrin signaling by
CC negatively regulating alpha-IIb/beta3 activation in thrombin-stimulated
CC megakaryocytes preventing platelet aggregation. Up-regulates PTK2/FAK1
CC activity, and is also needed for the recruitment of PTK2/FAK1 to focal
CC adhesions; it thus appears to play an important role in focal adhesion
CC formation. Positively regulates cell migration on fibronectin in a
CC CDC42-dependent manner, the effect being negatively regulated by PAK1.
CC Functions as a negative regulator of stress activated MAP kinase (MAPK)
CC signaling pathways. Down-regulates inositol 1,4,5-trisphosphate
CC receptor-dependent calcium signaling. Involved in sphingosine kinase
CC SPHK1 translocation to the plasma membrane in a N-myristoylation-
CC dependent manner preventing TNF-alpha-induced apoptosis. Regulates
CC serine/threonine-protein kinase PLK3 activity for proper completion of
CC cell division progression. Plays a role in microtubule (MT) dynamics
CC during neuronal development; disrupts the MT depolymerization activity
CC of STMN2 attenuating NGF-induced neurite outgrowth and the MT
CC reorganization at the edge of lamellipodia. Promotes cardiomyocyte
CC hypertrophy via activation of the calcineurin/NFAT signaling pathway.
CC Stimulates calcineurin PPP3R1 activity by mediating its anchoring to
CC the sarcolemma. In ischemia-induced (pathological or adaptive)
CC angiogenesis, stimulates endothelial cell proliferation, migration and
CC microvessel formation by activating the PAK1 and ERK1/ERK2 signaling
CC pathway. Promotes also cancer cell survival and proliferation. May
CC regulate cell cycle and differentiation of spermatogenic germ cells,
CC and/or differentiation of supporting Sertoli cells.
CC -!- FUNCTION: [Isoform 2]: Plays a regulatory role in angiogenesis and
CC tumor growth by mediating PKD/PRKD2-induced vascular endothelial growth
CC factor A (VEGFA) secretion. {ECO:0000269|PubMed:23503467}.
CC -!- FUNCTION: (Microbial infection) Involved in keratinocyte-intrinsic
CC immunity to human beta-papillomaviruses (HPVs).
CC {ECO:0000269|PubMed:30068544}.
CC -!- SUBUNIT: Monomer. Interacts with MYO1C. Interacts (via C-terminal
CC region) with PPP3R1 and CACNA1C; the interactions increase upon
CC cardiomyocytes hypertrophy (By similarity). Interacts with the
CC heterodimeric integrin alpha-IIb/beta3 (ITGA2B-ITGB3). Interacts with
CC ITGA2B (via cytoplasmic domain); the interaction is direct and calcium-
CC dependent. Interacts with the protein kinases PLK2/SNK and PRKDC (via
CC the region immediately upstream of the kinase domain). Interacts with
CC PLK3; the interaction inhibits PLK3 kinase activity. Interacts with
CC PSEN2. Interacts (via C-terminus) with F8. Interacts with NBR1 (via C-
CC terminus). Interacts with FEZ1 (via C-terminus). Interacts with UBR5
CC (via C-terminus); the interaction is sensitive to DNA damage, and may
CC target CIB1 for ubiquitin-mediated degradation. Interacts with IFI6;
CC the interaction is direct (PubMed:15685448). Interacts with BCL2
CC (PubMed:15685448). Interacts with ITPR3; the interaction occurs in a
CC calcium-dependent manner. Interacts with PTK2/FAK1. Interacts with
CC MAP3K5; the interaction inhibits MAP3K5 activation by phosphorylation,
CC and its subsequent interaction with TRAF2. Isoform 2 interacts with
CC PRKD2 (via N-terminal AP-rich region), PTK2/FAK1 and PAK1. Interacts
CC with TAS1R2 (via C-terminus); the interaction is independent of the
CC myristoylation state of CIB1. Interacts (via C-terminal region) with
CC STMN2 (via the N-terminal region); the interaction is direct, occurs in
CC a calcium-dependent manner and attenuates the STMN2-induced neurite
CC outgrowth inhibition. Interacts with SPHK1, the interaction occurs in a
CC calcium-dependent manner. Interacts with ITGA2B (via C-terminal
CC cytoplasmic tail); the interaction occurs upon platelet aggregation and
CC is stabilized/increased in a calcium and magnesium-dependent manner.
CC Interacts with PAK1 (via N-terminal region); the interaction is direct
CC and occurs in a calcium-dependent manner. Interacts with RAC3 (via C-
CC terminal region); the interaction induces their association with the
CC cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion. Interacts
CC with ITGA5 and ITGAV. Interacts and forms a complex with TMC6 and TMC8
CC (PubMed:30068544). {ECO:0000250, ECO:0000269|PubMed:10366599,
CC ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:11323029,
CC ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11856312,
CC ECO:0000269|PubMed:12011095, ECO:0000269|PubMed:12023286,
CC ECO:0000269|PubMed:12881299, ECO:0000269|PubMed:14992593,
CC ECO:0000269|PubMed:15475008, ECO:0000269|PubMed:15574431,
CC ECO:0000269|PubMed:15685448, ECO:0000269|PubMed:15883187,
CC ECO:0000269|PubMed:15933764, ECO:0000269|PubMed:16061695,
CC ECO:0000269|PubMed:16418530, ECO:0000269|PubMed:16723353,
CC ECO:0000269|PubMed:18627437, ECO:0000269|PubMed:19388079,
CC ECO:0000269|PubMed:19805025, ECO:0000269|PubMed:19854831,
CC ECO:0000269|PubMed:20473878, ECO:0000269|PubMed:20951827,
CC ECO:0000269|PubMed:21215777, ECO:0000269|PubMed:21264284,
CC ECO:0000269|PubMed:21388953, ECO:0000269|PubMed:22283712,
CC ECO:0000269|PubMed:22779914, ECO:0000269|PubMed:23503467,
CC ECO:0000269|PubMed:24011356, ECO:0000269|PubMed:30068544,
CC ECO:0000269|PubMed:9030514, ECO:0000269|PubMed:9372844}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
CC 4/HPV4 protein E8, human papillomavirus 5/HPV5 protein E1, and human
CC papillomavirus 16/HPV16 proteins E2 and E5.
CC {ECO:0000269|PubMed:30068544}.
CC -!- INTERACTION:
CC Q99828; P10092: CALCB; NbExp=3; IntAct=EBI-372594, EBI-12883326;
CC Q99828; P26842: CD27; NbExp=7; IntAct=EBI-372594, EBI-520729;
CC Q99828; P40199: CEACAM6; NbExp=3; IntAct=EBI-372594, EBI-4314501;
CC Q99828; Q04637-9: EIF4G1; NbExp=7; IntAct=EBI-372594, EBI-12012124;
CC Q99828; Q6UXG2-3: ELAPOR1; NbExp=3; IntAct=EBI-372594, EBI-12920100;
CC Q99828; P04066: FUCA1; NbExp=3; IntAct=EBI-372594, EBI-2512153;
CC Q99828; Q8NEA6-2: GLIS3; NbExp=5; IntAct=EBI-372594, EBI-12232117;
CC Q99828; P05362: ICAM1; NbExp=3; IntAct=EBI-372594, EBI-1035358;
CC Q99828; Q92993: KAT5; NbExp=3; IntAct=EBI-372594, EBI-399080;
CC Q99828; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-372594, EBI-11742507;
CC Q99828; P48449: LSS; NbExp=3; IntAct=EBI-372594, EBI-3930711;
CC Q99828; Q99683: MAP3K5; NbExp=7; IntAct=EBI-372594, EBI-476263;
CC Q99828; O43639: NCK2; NbExp=3; IntAct=EBI-372594, EBI-713635;
CC Q99828; O00746: NME4; NbExp=3; IntAct=EBI-372594, EBI-744871;
CC Q99828; O60422: ONECUT3; NbExp=3; IntAct=EBI-372594, EBI-17431136;
CC Q99828; P23759-2: PAX7; NbExp=3; IntAct=EBI-372594, EBI-12859446;
CC Q99828; Q9H7N4: SCAF1; NbExp=5; IntAct=EBI-372594, EBI-1222181;
CC Q99828; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-372594, EBI-9090795;
CC Q99828; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-372594, EBI-5235340;
CC Q99828; Q7RTT5: SSX7; NbExp=5; IntAct=EBI-372594, EBI-12879730;
CC Q99828; Q3KNT9: TMEM95; NbExp=3; IntAct=EBI-372594, EBI-12892569;
CC Q99828; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-372594, EBI-10241197;
CC Q99828; O00401: WASL; NbExp=7; IntAct=EBI-372594, EBI-957615;
CC Q99828; P61981: YWHAG; NbExp=3; IntAct=EBI-372594, EBI-359832;
CC Q99828; Q6ZSB9: ZBTB49; NbExp=3; IntAct=EBI-372594, EBI-2859943;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell membrane,
CC sarcolemma. Cell membrane. Apical cell membrane. Cell projection,
CC ruffle membrane. Cell projection, filopodium tip. Cell projection,
CC growth cone {ECO:0000269|PubMed:21215777}. Cell projection,
CC lamellipodium {ECO:0000269|PubMed:21215777}. Cytoplasm. Cytoplasm,
CC cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome. Cytoplasm, perinuclear region. Nucleus
CC {ECO:0000269|PubMed:30068544}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:21215777}. Perikaryon
CC {ECO:0000269|PubMed:21215777}. Note=Colocalized with PPP3R1 at the cell
CC membrane of cardiomyocytes in the hypertrophic heart (By similarity).
CC Colocalized with NBR1 to the perinuclear region. Colocalizes with
CC TAS1R2 in apical regions of taste receptor cells. Colocalized with RAC3
CC in the perinuclear area and at the cell periphery. Colocalized with
CC PAK1 within membrane ruffles during cell spreading upon readhesion to
CC fibronectin. Redistributed to the cytoskeleton upon platelet
CC aggregation. Translocates from the cytosol to the plasma membrane in a
CC calcium-dependent manner. Colocalized with PLK3 at centrosomes in
CC ductal breast carcinoma cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:23503467}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:23503467}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99828-1; Sequence=Displayed;
CC Name=2; Synonyms=CIB1a;
CC IsoId=Q99828-2; Sequence=VSP_053740;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in the epidermis,
CC hair follicles and keratinocytes (PubMed:30068544). Detected in
CC platelets and in cell lines of megakaryocytic and erythrocytic
CC lineages. Both isoform 1 and isoform 2 are detected in various cancer
CC cell lines, with isoform 2 being the predominant form (at protein
CC level). {ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:11856312,
CC ECO:0000269|PubMed:23503467, ECO:0000269|PubMed:30068544,
CC ECO:0000269|PubMed:9030514, ECO:0000269|PubMed:9372844}.
CC -!- INDUCTION: Up-regulated during breast cancer progression.
CC -!- DOMAIN: The EF-hands may also bind magnesium ions in the presence of
CC high Mg(2+) levels and low Ca(2+) levels.
CC -!- PTM: Phosphorylation of isoform 2 at Ser-118 by PRKD2 increases its
CC ability to stimulate tumor angiogenesis. {ECO:0000305|PubMed:23503467}.
CC -!- DISEASE: Epidermodysplasia verruciformis 3 (EV3) [MIM:618267]: A form
CC of epidermodysplasia verruciformis, a rare genodermatosis associated
CC with a high risk of skin carcinoma that results from an abnormal
CC susceptibility to infection by specific human papillomaviruses,
CC including the oncogenic HPV5. Infection leads to the early development
CC of disseminated flat wart-like and pityriasis versicolor-like skin
CC lesions. Cutaneous Bowen's carcinomas in situ and invasive squamous
CC cell carcinomas develop in about half of the patients, mainly on sun-
CC exposed skin areas. EV3 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:30068544}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The binding of either calcium or magnesium significantly
CC increases the structural stability of the protein in comparison to apo-
CC CIB (calcium- and magnesium-free form). {ECO:0000305|PubMed:14992593}.
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DR EMBL; U82226; AAC51106.1; -; mRNA.
DR EMBL; U85611; AAB53387.1; -; mRNA.
DR EMBL; AB021866; BAA36281.1; -; Genomic_DNA.
DR EMBL; JQ246073; AEZ06077.1; -; mRNA.
DR EMBL; U83236; AAB39758.1; -; mRNA.
DR EMBL; CR456955; CAG33236.1; -; mRNA.
DR EMBL; AB451276; BAG70090.1; -; mRNA.
DR EMBL; AB451406; BAG70220.1; -; mRNA.
DR EMBL; CH471101; EAX02090.1; -; Genomic_DNA.
DR EMBL; BC000846; AAH00846.1; -; mRNA.
DR CCDS; CCDS10360.1; -. [Q99828-1]
DR CCDS; CCDS73781.1; -. [Q99828-2]
DR RefSeq; NP_001264693.1; NM_001277764.1. [Q99828-2]
DR RefSeq; NP_006375.2; NM_006384.3. [Q99828-1]
DR PDB; 1DGU; NMR; -; A=9-191.
DR PDB; 1DGV; NMR; -; A=9-191.
DR PDB; 1XO5; X-ray; 1.99 A; A/B=9-191.
DR PDB; 1Y1A; X-ray; 2.30 A; A/B=9-191.
DR PDB; 2L4H; NMR; -; A=1-191.
DR PDB; 2L4I; NMR; -; A=1-191.
DR PDB; 2LM5; NMR; -; A=1-191.
DR PDB; 6OCX; X-ray; 1.90 A; A/B/C/D=1-191.
DR PDB; 6OD0; X-ray; 2.15 A; A/B=1-191.
DR PDBsum; 1DGU; -.
DR PDBsum; 1DGV; -.
DR PDBsum; 1XO5; -.
DR PDBsum; 1Y1A; -.
DR PDBsum; 2L4H; -.
DR PDBsum; 2L4I; -.
DR PDBsum; 2LM5; -.
DR PDBsum; 6OCX; -.
DR PDBsum; 6OD0; -.
DR AlphaFoldDB; Q99828; -.
DR BMRB; Q99828; -.
DR SMR; Q99828; -.
DR BioGRID; 115774; 78.
DR CORUM; Q99828; -.
DR DIP; DIP-31260N; -.
DR IntAct; Q99828; 41.
DR MINT; Q99828; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR TCDB; 8.A.82.1.9; the calmodulin calcium binding protein (calmodulin) family.
DR iPTMnet; Q99828; -.
DR PhosphoSitePlus; Q99828; -.
DR BioMuta; CIB1; -.
DR DMDM; 134047806; -.
DR EPD; Q99828; -.
DR jPOST; Q99828; -.
DR MassIVE; Q99828; -.
DR MaxQB; Q99828; -.
DR PaxDb; Q99828; -.
DR PeptideAtlas; Q99828; -.
DR PRIDE; Q99828; -.
DR ProteomicsDB; 78493; -. [Q99828-1]
DR Antibodypedia; 28761; 397 antibodies from 34 providers.
DR DNASU; 10519; -.
DR Ensembl; ENST00000328649.11; ENSP00000333873.6; ENSG00000185043.12. [Q99828-1]
DR Ensembl; ENST00000612800.1; ENSP00000479860.1; ENSG00000185043.12. [Q99828-2]
DR GeneID; 10519; -.
DR KEGG; hsa:10519; -.
DR MANE-Select; ENST00000328649.11; ENSP00000333873.6; NM_006384.4; NP_006375.2.
DR UCSC; uc002bpb.5; human. [Q99828-1]
DR CTD; 10519; -.
DR DisGeNET; 10519; -.
DR GeneCards; CIB1; -.
DR HGNC; HGNC:16920; CIB1.
DR HPA; ENSG00000185043; Low tissue specificity.
DR MalaCards; CIB1; -.
DR MIM; 602293; gene.
DR MIM; 618267; phenotype.
DR neXtProt; NX_Q99828; -.
DR OpenTargets; ENSG00000185043; -.
DR Orphanet; 302; Epidermodysplasia verruciformis.
DR PharmGKB; PA38423; -.
DR VEuPathDB; HostDB:ENSG00000185043; -.
DR GeneTree; ENSGT00940000158927; -.
DR HOGENOM; CLU_061288_6_1_1; -.
DR InParanoid; Q99828; -.
DR OMA; GHNRNAK; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q99828; -.
DR TreeFam; TF313865; -.
DR PathwayCommons; Q99828; -.
DR SignaLink; Q99828; -.
DR SIGNOR; Q99828; -.
DR BioGRID-ORCS; 10519; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; CIB1; human.
DR EvolutionaryTrace; Q99828; -.
DR GeneWiki; CIB1; -.
DR GenomeRNAi; 10519; -.
DR Pharos; Q99828; Tbio.
DR PRO; PR:Q99828; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q99828; protein.
DR Bgee; ENSG00000185043; Expressed in bronchial epithelial cell and 194 other tissues.
DR ExpressionAtlas; Q99828; baseline and differential.
DR Genevisible; Q99828; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:HGNC-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:HGNC-UCL.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IMP:HGNC-UCL.
DR GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; IMP:CACAO.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:CACAO.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IGI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IMP:HGNC-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:HGNC-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; TAS:ProtInc.
DR GO; GO:0007113; P:endomitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:2000256; P:positive regulation of male germ cell proliferation; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IGI:BHF-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Apoptosis; Calcium;
KW Cell adhesion; Cell cycle; Cell division; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Differentiation; Golgi apparatus; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..191
FT /note="Calcium and integrin-binding protein 1"
FT /id="PRO_0000073531"
FT DOMAIN 103..138
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 148..183
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10366599"
FT VAR_SEQ 29
FT /note="L -> LSVYVVLAPHLVDNEQQARSGNEHTGRPIAENTDSSPLSTR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:23503467"
FT /id="VSP_053740"
FT VARIANT 44
FT /note="S -> T (in dbSNP:rs3210935)"
FT /evidence="ECO:0000269|PubMed:10826701,
FT ECO:0000269|PubMed:9372844, ECO:0000269|Ref.5"
FT /id="VAR_019565"
FT VARIANT 72..191
FT /note="Missing (in EV3; absence of CIB1 protein in
FT homozygous patient cells)"
FT /evidence="ECO:0000269|PubMed:30068544"
FT /id="VAR_081784"
FT VARIANT 106
FT /note="I -> T (in dbSNP:rs11551250)"
FT /id="VAR_048636"
FT MUTAGEN 2
FT /note="G->A: Inhibits translocation to the plasma membrane.
FT Increased apoptosis after TNF stimulation."
FT /evidence="ECO:0000269|PubMed:19854831"
FT MUTAGEN 78
FT /note="S->A: Loss of phosphorylation by PKD/PRKD2; in
FT isoform 2."
FT /evidence="ECO:0000269|PubMed:23503467"
FT MUTAGEN 78
FT /note="S->E: Phosphomimetic; promotes tumor growth by an
FT indirect mechanism; in isoform 2."
FT /evidence="ECO:0000269|PubMed:23503467"
FT MUTAGEN 114..117
FT /note="IFDF->AAAA: Loss of binding to ITGAV."
FT /evidence="ECO:0000269|PubMed:24011356"
FT MUTAGEN 115
FT /note="F->A: Loss of binding to ITGA2B."
FT /evidence="ECO:0000269|PubMed:12023286"
FT MUTAGEN 127
FT /note="D->N: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:15475008"
FT MUTAGEN 131
FT /note="L->A,T: Loss of binding to ITGA2B."
FT /evidence="ECO:0000269|PubMed:12023286"
FT MUTAGEN 152..153
FT /note="LI->AA: Loss of binding to ITGA2B."
FT /evidence="ECO:0000269|PubMed:24011356"
FT MUTAGEN 153
FT /note="I->A: Loss of binding to ITGA2B."
FT /evidence="ECO:0000269|PubMed:12023286"
FT MUTAGEN 167
FT /note="T->A: No effect on phosphorylation by PKD/PRKD2; in
FT isoform 2."
FT /evidence="ECO:0000269|PubMed:23503467"
FT MUTAGEN 172
FT /note="E->Q: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:15475008"
FT MUTAGEN 173
FT /note="F->A: Loss of binding to ITGA2B."
FT /evidence="ECO:0000269|PubMed:12023286,
FT ECO:0000269|PubMed:16418530, ECO:0000269|PubMed:24011356"
FT MUTAGEN 173
FT /note="F->A: Loss of binding to ITGA2B. Does not inhibit
FT interaction with PAK1."
FT /evidence="ECO:0000269|PubMed:12023286,
FT ECO:0000269|PubMed:16418530, ECO:0000269|PubMed:24011356"
FT CONFLICT 136
FT /note="T -> M (in Ref. 6; CAG33236)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> F (in Ref. 4; AEZ06077)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1XO5"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2L4I"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6OCX"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1DGU"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:6OCX"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1Y1A"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:6OCX"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:6OCX"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1Y1A"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:6OCX"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:6OCX"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1XO5"
FT MOD_RES Q99828-2:118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23503467"
SQ SEQUENCE 191 AA; 21703 MW; 9AA19A0DE7AA1E05 CRC64;
MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPQ EQRSVESSLR AQVPFEQILS
LPELKANPFK ERICRVFSTS PAKDSLSFED FLDLLSVFSD TATPDIKSHY AFRIFDFDDD
GTLNREDLSR LVNCLTGEGE DTRLSASEMK QLIDNILEES DIDRDGTINL SEFQHVISRS
PDFASSFKIV L
