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Calcium and integrin-binding protein 1 (CIB) (Calcium- and integrin-binding protein) (CIBP) (Calmyrin) (DNA-PKcs-interacting protein) (Kinase-interacting protein) (KIP) (SNK-interacting protein 2-28) (SIP2-28)

 CIB1_HUMAN              Reviewed;         191 AA.
Q99828; B5BU40; H6WJF3; O00693; O00735; Q6IB49; Q96J54; Q99971;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 4.
30-AUG-2017, entry version 171.
RecName: Full=Calcium and integrin-binding protein 1;
Short=CIB;
AltName: Full=Calcium- and integrin-binding protein;
Short=CIBP;
AltName: Full=Calmyrin;
AltName: Full=DNA-PKcs-interacting protein;
AltName: Full=Kinase-interacting protein;
Short=KIP;
AltName: Full=SNK-interacting protein 2-28;
Short=SIP2-28;
Name=CIB1; Synonyms=CIB, KIP, PRKDCIP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ITGA2B,
TISSUE SPECIFICITY, AND CALCIUM-BINDING.
TISSUE=Fetal liver;
PubMed=9030514; DOI=10.1074/jbc.272.8.4651;
Naik U.P., Patel P.M., Parise L.V.;
"Identification of a novel calcium-binding protein that interacts with
the integrin alphaIIb cytoplasmic domain.";
J. Biol. Chem. 272:4651-4654(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PRKDC, TISSUE
SPECIFICITY, AND VARIANT THR-44.
PubMed=9372844; DOI=10.1016/S0921-8777(97)00035-9;
Wu X., Lieber M.R.;
"Interaction between DNA-dependent protein kinase and a novel protein,
KIP.";
Mutat. Res. 385:13-20(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-44.
PubMed=10826701; DOI=10.3109/10425170009015612;
Hattori A., Seki N., Hayashi A., Kozuma S., Saito T.;
"Genomic structure of mouse and human genes for DNA-PKcs interacting
protein (KIP).";
DNA Seq. 10:415-418(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2),
INTERACTION WITH PRKD2; PTK2 AND PAK1, SUBCELLULAR LOCATION (ISOFORM
2), TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-118 (ISOFORM 2), AND
MUTAGENESIS OF SER-78 AND THR-167.
TISSUE=Brain;
PubMed=23503467; DOI=10.1038/onc.2013.43;
Armacki M., Joodi G., Nimmagadda S.C., de Kimpe L., Pusapati G.V.,
Vandoninck S., Van Lint J., Illing A., Seufferlein T.;
"A novel splice variant of calcium and integrin-binding protein 1
mediates protein kinase D2-stimulated tumour growth by regulating
angiogenesis.";
Oncogene 33:1167-1180(2014).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-44.
Yuan O.;
"SNK, a Ser/Thr protein kinase, associated proteins.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10477286; DOI=10.1042/bj3420729;
Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J.,
Parise L.V.;
"Calcium-dependent properties of CIB binding to the integrin alphaIIb
cytoplasmic domain and translocation to the platelet cytoskeleton.";
Biochem. J. 342:729-735(1999).
[11]
MYRISTOYLATION AT GLY-2, AND INTERACTION WITH PSEN2.
PubMed=10366599; DOI=10.1083/jcb.145.6.1277;
Stabler S.M., Ostrowski L.L., Janicki S.M., Monteiro M.J.;
"A myristoylated calcium-binding protein that preferentially interacts
with the Alzheimer's disease presenilin 2 protein.";
J. Cell Biol. 145:1277-1292(1999).
[12]
INTERACTION WITH F8.
PubMed=11323029; DOI=10.1016/S0049-3848(01)00229-8;
Fang X., Chen C., Wang Q., Gu J., Chi C.;
"The interaction of the calcium- and integrin-binding protein (CIBP)
with the coagulation factor VIII.";
Thromb. Res. 102:177-185(2001).
[13]
INTERACTION WITH NBR1 AND FEZ1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=11856312; DOI=10.1046/j.0014-2956.2001.02681.x;
Whitehouse C., Chambers J., Howe K., Cobourne M., Sharpe P.,
Solomon E.;
"NBR1 interacts with fasciculation and elongation protein zeta-1
(FEZ1) and calcium and integrin binding protein (CIB) and shows
developmentally restricted expression in the neural tube.";
Eur. J. Biochem. 269:538-545(2002).
[14]
FUNCTION, INTERACTION WITH RAC3, AND SUBCELLULAR LOCATION.
PubMed=11756406; DOI=10.1074/jbc.M105363200;
Haataja L., Kaartinen V., Groffen J., Heisterkamp N.;
"The small GTPase Rac3 interacts with the integrin-binding protein CIB
and promotes integrin alpha(IIb)beta(3)-mediated adhesion and
spreading.";
J. Biol. Chem. 277:8321-8328(2002).
[15]
INTERACTION WITH UBR5.
PubMed=12011095; DOI=10.1074/jbc.M203527200;
Henderson M.J., Russell A.J., Hird S., Munoz M., Clancy J.L.,
Lehrbach G.M., Calanni S.T., Jans D.A., Sutherland R.L., Watts C.K.;
"EDD, the human hyperplastic discs protein, has a role in progesterone
receptor coactivation and potential involvement in DNA damage
response.";
J. Biol. Chem. 277:26468-26478(2002).
[16]
INTERACTION WITH ITGA2B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PHE-115; LEU-131; ILE-153 AND PHE-173.
PubMed=12023286; DOI=10.1074/jbc.M202983200;
Barry W.T., Boudignon-Proudhon C., Shock D.D., McFadden A.,
Weiss J.M., Sondek J., Parise L.V.;
"Molecular basis of CIB binding to the integrin alpha IIb cytoplasmic
domain.";
J. Biol. Chem. 277:28877-28883(2002).
[17]
FUNCTION.
PubMed=12714504; DOI=10.1182/blood-2003-02-0591;
Naik U.P., Naik M.U.;
"Association of CIB with GPIIb/IIIa during outside-in signaling is
required for platelet spreading on fibrinogen.";
Blood 102:1355-1362(2003).
[18]
INTERACTION WITH ITGA2B, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
PubMed=14992593; DOI=10.1021/bi035432b;
Yamniuk A.P., Nguyen L.T., Hoang T.T., Vogel H.J.;
"Metal ion binding properties and conformational states of
calcium- and integrin-binding protein.";
Biochemistry 43:2558-2568(2004).
[19]
SUBCELLULAR LOCATION, INTERACTION WITH PSEN2, AND MUTAGENESIS OF
ASP-127 AND GLU-172.
PubMed=15475008; DOI=10.1016/j.yexcr.2004.07.020;
Zhu J., Stabler S.M., Ames J.B., Baskakov I., Monteiro M.J.;
"Calcium binding sequences in calmyrin regulates interaction with
presenilin-2.";
Exp. Cell Res. 300:440-454(2004).
[20]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTK2/FAK1.
PubMed=12881299; DOI=10.1182/blood-2003-05-1703;
Naik M.U., Naik U.P.;
"Calcium-and integrin-binding protein regulates focal adhesion kinase
activity during platelet spreading on immobilized fibrinogen.";
Blood 102:3629-3636(2003).
[21]
SUBUNIT.
PubMed=15933764;
Sobczak A., Blazejczyk M., Piszczek G., Zhao G., Kuznicki J.,
Wojda U.;
"Calcium-binding calmyrin forms stable covalent dimers in vitro, but
in vivo is found in monomeric form.";
Acta Biochim. Pol. 52:469-476(2005).
[22]
FUNCTION, AND INTERACTION WITH IFI6 AND BCL2.
PubMed=15685448; DOI=10.1007/s00262-004-0645-2;
Tahara E. Jr., Tahara H., Kanno M., Naka K., Takeda Y., Matsuzaki T.,
Yamazaki R., Ishihara H., Yasui W., Barrett J.C., Ide T., Tahara E.;
"G1P3, an interferon inducible gene 6-16, is expressed in gastric
cancers and inhibits mitochondrial-mediated apoptosis in gastric
cancer cell line TMK-1 cell.";
Cancer Immunol. Immunother. 54:729-740(2005).
[23]
FUNCTION, AND INTERACTION WITH PAK1.
PubMed=16061695; DOI=10.1083/jcb.200502090;
Leisner T.M., Liu M., Jaffer Z.M., Chernoff J., Parise L.V.;
"Essential role of CIB1 in regulating PAK1 activation and cell
migration.";
J. Cell Biol. 170:465-476(2005).
[24]
INTERACTION WITH ITGA2B, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
PubMed=15883187; DOI=10.1110/ps.041312805;
Yamniuk A.P., Vogel H.J.;
"Calcium- and magnesium-dependent interactions between calcium- and
integrin-binding protein and the integrin alphaIIb cytoplasmic
domain.";
Protein Sci. 14:1429-1437(2005).
[25]
INTERACTION WITH ITPR3.
PubMed=16723353; DOI=10.1074/jbc.M602175200;
White C., Yang J., Monteiro M.J., Foskett J.K.;
"CIB1, a ubiquitously expressed Ca2+-binding protein ligand of the
InsP3 receptor Ca2+ release channel.";
J. Biol. Chem. 281:20825-20833(2006).
[26]
FUNCTION, INTERACTION WITH PAK1, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF PHE-173.
PubMed=16418530; DOI=10.1083/jcb.200505131;
Yuan W., Leisner T.M., McFadden A.W., Wang Z., Larson M.K., Clark S.,
Boudignon-Proudhon C., Lam S.C., Parise L.V.;
"CIB1 is an endogenous inhibitor of agonist-induced integrin
alphaIIbbeta3 activation.";
J. Cell Biol. 172:169-175(2006).
[27]
FUNCTION, INTERACTION WITH TAS1R2, AND SUBCELLULAR LOCATION.
PubMed=18627437; DOI=10.1111/j.1471-4159.2008.05563.x;
Hennigs J.K., Burhenne N., Staehler F., Winnig M., Walter B.,
Meyerhof W., Schmale H.;
"Sweet taste receptor interacting protein CIB1 is a general inhibitor
of InsP3-dependent Ca2+ release in vivo.";
J. Neurochem. 106:2249-2262(2008).
[28]
FUNCTION, AND INTERACTION WITH MAP3K5.
PubMed=19805025; DOI=10.1073/pnas.0812259106;
Yoon K.W., Cho J.H., Lee J.K., Kang Y.H., Chae J.S., Kim Y.M., Kim J.,
Kim E.K., Kim S.E., Baik J.H., Naik U.P., Cho S.G., Choi E.J.;
"CIB1 functions as a Ca(2+)-sensitive modulator of stress-induced
signaling by targeting ASK1.";
Proc. Natl. Acad. Sci. U.S.A. 106:17389-17394(2009).
[29]
SUBUNIT, AND CALCIUM-BINDING.
PubMed=19388079; DOI=10.1002/pro.104;
Yamniuk A.P., Anderson K.L., Fraser M.E., Vogel H.J.;
"Auxiliary Ca2+ binding sites can influence the structure of CIB1.";
Protein Sci. 18:1128-1134(2009).
[30]
INTERACTION WITH SPHK1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-2.
PubMed=19854831; DOI=10.1074/jbc.M109.068395;
Jarman K.E., Moretti P.A., Zebol J.R., Pitson S.M.;
"Translocation of sphingosine kinase 1 to the plasma membrane is
mediated by calcium- and integrin-binding protein 1.";
J. Biol. Chem. 285:483-492(2010).
[31]
SUBCELLULAR LOCATION.
PubMed=20639889; DOI=10.1038/nm.2181;
Heineke J., Auger-Messier M., Correll R.N., Xu J., Benard M.J.,
Yuan W., Drexler H., Parise L.V., Molkentin J.D.;
"CIB1 is a regulator of pathological cardiac hypertrophy.";
Nat. Med. 16:872-879(2010).
[32]
INTERACTION WITH STMN2, AND SUBCELLULAR LOCATION.
PubMed=21215777; DOI=10.1016/j.bbamcr.2010.12.023;
Sobczak A., Debowska K., Blazejczyk M., Kreutz M.R., Kuznicki J.,
Wojda U.;
"Calmyrin1 binds to SCG10 protein (stathmin2) to modulate neurite
outgrowth.";
Biochim. Biophys. Acta 1813:1025-1037(2011).
[33]
FUNCTION, INTERACTION WITH PLK3, AND SUBCELLULAR LOCATION (ISOFORM 1).
PubMed=20951827; DOI=10.1016/j.biocel.2010.10.003;
Naik M.U., Naik U.P.;
"Calcium- and integrin-binding protein 1 regulates microtubule
organization and centrosome segregation through polo like kinase 3
during cell cycle progression.";
Int. J. Biochem. Cell Biol. 43:120-129(2011).
[34]
INTERACTION WITH PLK3.
PubMed=20473878; DOI=10.1002/ijc.25388;
Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P.;
"Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1
in breast cancer cells.";
Int. J. Cancer 128:587-596(2011).
[35]
FUNCTION, AND SUBCELLULAR LOCATION (ISOFORM 1).
PubMed=21748785; DOI=10.1002/jcb.23255;
Naik M.U., Naik U.P.;
"Contra-regulation of calcium- and integrin-binding protein 1-induced
cell migration on fibronectin by PAK1 and MAP kinase signaling.";
J. Cell. Biochem. 112:3289-3299(2011).
[36]
FUNCTION, AND INTERACTION WITH PLK3.
PubMed=21264284; DOI=10.1371/journal.pone.0014513;
Kostyak J.C., Naik U.P.;
"Calcium- and integrin-binding protein 1 regulates endomitosis and its
interaction with Polo-like kinase 3 is enhanced in endomitotic Dami
cells.";
PLoS ONE 6:E14513-E14513(2011).
[37]
INTERACTION WITH ITGA2B.
PubMed=22779914; DOI=10.1139/o2012-021;
Huang H., Bogstie J.N., Vogel H.J.;
"Biophysical and structural studies of the human calcium- and
integrin-binding protein family: understanding their functional
similarities and differences.";
Biochem. Cell Biol. 90:646-656(2012).
[38]
INTERACTION WITH ITGA5 AND ITGAV, AND MUTAGENESIS OF 114-ILE--PHE-117;
152-LEU-ILE-153 AND PHE-173.
PubMed=24011356; DOI=10.1021/bi400678y;
Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I.,
Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.;
"Identification of novel integrin binding partners for calcium and
integrin binding protein 1 (CIB1): structural and thermodynamic basis
of CIB1 promiscuity.";
Biochemistry 52:7082-7090(2013).
[39]
FUNCTION.
PubMed=22964641; DOI=10.1038/onc.2012.408;
Leisner T.M., Moran C., Holly S.P., Parise L.V.;
"CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell
death via AKT and ERK signaling.";
Oncogene 32:4017-4027(2013).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[41]
STRUCTURE BY NMR OF 9-191.
PubMed=10822252;
DOI=10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.3.CO;2-1;
Hwang P.M., Vogel H.J.;
"Structures of the platelet calcium- and integrin-binding protein and
the alphaIIb-integrin cytoplasmic domain suggest a mechanism for
calcium-regulated recognition; homology modelling and NMR studies.";
J. Mol. Recognit. 13:83-92(2000).
[42]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 9-191 IN COMPLEX WITH
CALCIUM IONS, AND SUBUNIT.
PubMed=15574431; DOI=10.1074/jbc.M411515200;
Gentry H.R., Singer A.U., Betts L., Yang C., Ferrara J.D., Sondek J.,
Parise L.V.;
"Structural and biochemical characterization of CIB1 delineates a new
family of EF-hand-containing proteins.";
J. Biol. Chem. 280:8407-8415(2005).
[43]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 9-191.
PubMed=15840829; DOI=10.1110/ps.041270805;
Blamey C.J., Ceccarelli C., Naik U.P., Bahnson B.J.;
"The crystal structure of calcium- and integrin-binding protein 1:
insights into redox regulated functions.";
Protein Sci. 14:1214-1221(2005).
[44]
STRUCTURE BY NMR OF 1-191 IN COMPLEXES WITH CALCIUM IONS AND MAGNESIUM
ION, AND INTERACTION WITH ITGA2B.
PubMed=21388953; DOI=10.1074/jbc.M110.179028;
Huang H., Ishida H., Yamniuk A.P., Vogel H.J.;
"Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions
with the platelet integrin alphaIIb cytoplasmic domain.";
J. Biol. Chem. 286:17181-17192(2011).
[45]
STRUCTURE BY NMR OF 1-191 IN COMPLEX WITH ITGA2B PEPTIDE AND CALCIUM
IONS, AND INTERACTION WITH ITGA2B.
PubMed=22283712; DOI=10.1021/ja2111306;
Huang H., Vogel H.J.;
"Structural basis for the activation of platelet integrin
alphaIIbbeta3 by calcium- and integrin-binding protein 1.";
J. Am. Chem. Soc. 134:3864-3872(2012).
-!- FUNCTION: Calcium-binding protein that plays a role in the
regulation of numerous cellular processes, such as cell
differentiation, cell division, cell proliferation, cell
migration, thrombosis, angiogenesis, cardiac hypertrophy and
apoptosis. Involved in bone marrow megakaryocyte differentiation
by negatively regulating thrombopoietin-mediated signaling
pathway. Participates in the endomitotic cell cycle of
megakaryocyte, a form of mitosis in which both karyokinesis and
cytokinesis are interrupted. Plays a role in integrin signaling by
negatively regulating alpha-IIb/beta3 activation in thrombin-
stimulated megakaryocytes preventing platelet aggregation. Up-
regulates PTK2/FAK1 activity, and is also needed for the
recruitment of PTK2/FAK1 to focal adhesions; it thus appears to
play an important role in focal adhesion formation. Positively
regulates cell migration on fibronectin in a CDC42-dependent
manner, the effect being negatively regulated by PAK1. Functions
as a negative regulator of stress activated MAP kinase (MAPK)
signaling pathways. Down-regulates inositol 1,4,5-trisphosphate
receptor-dependent calcium signaling. Involved in sphingosine
kinase SPHK1 translocation to the plasma membrane in a N-
myristoylation-dependent manner preventing TNF-alpha-induced
apoptosis. Regulates serine/threonine-protein kinase PLK3 activity
for proper completion of cell division progression. Plays a role
in microtubule (MT) dynamics during neuronal development; disrupts
the MT depolymerization activity of STMN2 attenuating NGF-induced
neurite outgrowth and the MT reorganization at the edge of
lamellipodia. Promotes cardiomyocyte hypertrophy via activation of
the calcineurin/NFAT signaling pathway. Stimulates calcineurin
PPP3R1 activity by mediating its anchoring to the sarcolemma. In
ischemia-induced (pathological or adaptive) angiogenesis,
stimulates endothelial cell proliferation, migration and
microvessel formation by activating the PAK1 and ERK1/ERK2
signaling pathway. Promotes also cancer cell survival and
proliferation. May regulate cell cycle and differentiation of
spermatogenic germ cells, and/or differentiation of supporting
Sertoli cells.
-!- FUNCTION: Isoform 2: Plays a regulatory role in angiogenesis and
tumor growth by mediating PKD/PRKD2-induced vascular endothelial
growth factor A (VEGFA) secretion. {ECO:0000269|PubMed:23503467}.
-!- SUBUNIT: Monomer. Interacts with MYO1C. Interacts (via C-terminal
region) with PPP3R1 and CACNA1C; the interactions increase upon
cardiomyocytes hypertrophy (By similarity). Interacts with the
heterodimeric integrin alpha-IIb/beta3 (ITGA2B-ITGB3). Interacts
with ITGA2B (via cytoplasmic domain); the interaction is direct
and calcium-dependent. Interacts with the protein kinases PLK2/SNK
and PRKDC (via the region immediately upstream of the kinase
domain). Interacts with PLK3; the interaction inhibits PLK3 kinase
activity. Interacts with PSEN2. Interacts (via C-terminus) with
F8. Interacts with NBR1 (via C-terminus). Interacts with FEZ1 (via
C-terminus). Interacts with UBR5 (via C-terminus); the interaction
is sensitive to DNA damage, and may target CIB1 for ubiquitin-
mediated degradation. Interacts with IFI6. Interacts with BCL2.
Interacts with ITPR3; the interaction occurs in a calcium-
dependent manner. Interacts with PTK2/FAK1. Interacts with MAP3K5;
the interaction inhibits MAP3K5 activation by phosphorylation, and
its subsequent interaction with TRAF2. Isoform 2 interacts with
PRKD2 (via N-terminal AP-rich region), PTK2/FAK1 and PAK1.
Interacts with TAS1R2 (via C-terminus); the interaction is
independent of the myristoylation state of CIB1. Interacts (via C-
terminal region) with STMN2 (via the N-terminal region); the
interaction is direct, occurs in a calcium-dependent manner and
attenuates the STMN2-induced neurite outgrowth inhibition.
Interacts with SPHK1, the interaction occurs in a calcium-
dependent manner. Interacts with ITGA2B (via C-terminal
cytoplasmic tail); the interaction occurs upon platelet
aggregation and is stabilized/increased in a calcium and
magnesium-dependent manner. Interacts with PAK1 (via N-terminal
region); the interaction is direct and occurs in a calcium-
dependent manner. Interacts with RAC3 (via C-terminal region); the
interaction induces their association with the cytoskeleton upon
alpha-IIb/beta3 integrin-mediated adhesion. Interacts with ITGA5
and ITGAV. {ECO:0000250, ECO:0000269|PubMed:10366599,
ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:11323029,
ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11856312,
ECO:0000269|PubMed:12011095, ECO:0000269|PubMed:12023286,
ECO:0000269|PubMed:12881299, ECO:0000269|PubMed:14992593,
ECO:0000269|PubMed:15475008, ECO:0000269|PubMed:15574431,
ECO:0000269|PubMed:15685448, ECO:0000269|PubMed:15883187,
ECO:0000269|PubMed:15933764, ECO:0000269|PubMed:16061695,
ECO:0000269|PubMed:16418530, ECO:0000269|PubMed:16723353,
ECO:0000269|PubMed:18627437, ECO:0000269|PubMed:19388079,
ECO:0000269|PubMed:19805025, ECO:0000269|PubMed:19854831,
ECO:0000269|PubMed:20473878, ECO:0000269|PubMed:20951827,
ECO:0000269|PubMed:21215777, ECO:0000269|PubMed:21264284,
ECO:0000269|PubMed:21388953, ECO:0000269|PubMed:22283712,
ECO:0000269|PubMed:22779914, ECO:0000269|PubMed:23503467,
ECO:0000269|PubMed:24011356, ECO:0000269|PubMed:9030514,
ECO:0000269|PubMed:9372844}.
-!- INTERACTION:
P48449:LSS; NbExp=4; IntAct=EBI-372594, EBI-3930711;
O00401:WASL; NbExp=7; IntAct=EBI-372594, EBI-957615;
-!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell membrane,
sarcolemma. Cell membrane. Apical cell membrane. Cell projection,
ruffle membrane. Cell projection, filopodium tip. Cell projection,
growth cone. Cell projection, lamellipodium. Cytoplasm. Cytoplasm,
cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome. Cytoplasm, perinuclear region. Nucleus.
Note=Colocalized with PPP3R1 at the cell membrane of
cardiomyocytes in the hypertrophic heart (By similarity).
Colocalized with NBR1 to the perinuclear region. Colocalizes with
TAS1R2 in apical regions of taste receptor cells. Colocalized with
RAC3 in the perinuclear area and at the cell periphery.
Colocalized with PAK1 within membrane ruffles during cell
spreading upon readhesion to fibronectin. Redistributed to the
cytoskeleton upon platelet aggregation. Translocates from the
cytosol to the plasma membrane in a calcium-dependent manner.
Colocalized with STMN2 in the cell body, neurites and growth cones
of neurons. Colocalized with STMN2 to the leading edge of
lamellipodia. Colocalized with PLK3 at centrosomes in ductal
breast carcinoma cells. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:23503467}. Golgi apparatus, trans-Golgi
network {ECO:0000269|PubMed:23503467}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99828-1; Sequence=Displayed;
Name=2; Synonyms=CIB1a;
IsoId=Q99828-2; Sequence=VSP_053740;
Note=Contains a phosphoserine at position 118.
{ECO:0000269|PubMed:23503467};
-!- TISSUE SPECIFICITY: Detected in platelets and in cell lines of
megakaryocytic and erythrocytic lineages. Both isoform 1 and
isoform 2 are detected in various cancer cell lines, with isoform
2 being the predominant form (at protein level). Ubiquitously
expressed. {ECO:0000269|PubMed:10477286,
ECO:0000269|PubMed:11856312, ECO:0000269|PubMed:23503467,
ECO:0000269|PubMed:9030514, ECO:0000269|PubMed:9372844}.
-!- INDUCTION: Up-regulated during breast cancer progression.
-!- DOMAIN: The EF-hands may also bind magnesium ions in the presence
of high Mg(2+) levels and low Ca(2+) levels.
-!- PTM: Phosphorylation of isoform 2 at Ser-118 by PRKD2 increases
its ability to stimulate tumor angiogenesis.
{ECO:0000305|PubMed:23503467}.
-!- MISCELLANEOUS: The binding of either calcium or magnesium
significantly increases the structural stability of the protein in
comparison to apo-CIB (calcium- and magnesium-free form).
{ECO:0000305|PubMed:14992593}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U82226; AAC51106.1; -; mRNA.
EMBL; U85611; AAB53387.1; -; mRNA.
EMBL; AB021866; BAA36281.1; -; Genomic_DNA.
EMBL; JQ246073; AEZ06077.1; -; mRNA.
EMBL; U83236; AAB39758.1; -; mRNA.
EMBL; CR456955; CAG33236.1; -; mRNA.
EMBL; AB451276; BAG70090.1; -; mRNA.
EMBL; AB451406; BAG70220.1; -; mRNA.
EMBL; CH471101; EAX02090.1; -; Genomic_DNA.
EMBL; BC000846; AAH00846.1; -; mRNA.
CCDS; CCDS10360.1; -. [Q99828-1]
CCDS; CCDS73781.1; -. [Q99828-2]
RefSeq; NP_001264693.1; NM_001277764.1. [Q99828-2]
RefSeq; NP_006375.2; NM_006384.3. [Q99828-1]
UniGene; Hs.715556; -.
PDB; 1DGU; NMR; -; A=9-191.
PDB; 1DGV; NMR; -; A=9-191.
PDB; 1XO5; X-ray; 1.99 A; A/B=9-191.
PDB; 1Y1A; X-ray; 2.30 A; A/B=9-191.
PDB; 2L4H; NMR; -; A=1-191.
PDB; 2L4I; NMR; -; A=1-191.
PDB; 2LM5; NMR; -; A=1-191.
PDBsum; 1DGU; -.
PDBsum; 1DGV; -.
PDBsum; 1XO5; -.
PDBsum; 1Y1A; -.
PDBsum; 2L4H; -.
PDBsum; 2L4I; -.
PDBsum; 2LM5; -.
ProteinModelPortal; Q99828; -.
SMR; Q99828; -.
BioGrid; 115774; 21.
DIP; DIP-31260N; -.
IntAct; Q99828; 29.
MINT; MINT-95290; -.
STRING; 9606.ENSP00000333873; -.
iPTMnet; Q99828; -.
PhosphoSitePlus; Q99828; -.
BioMuta; CIB1; -.
DMDM; 134047806; -.
EPD; Q99828; -.
MaxQB; Q99828; -.
PaxDb; Q99828; -.
PeptideAtlas; Q99828; -.
PRIDE; Q99828; -.
DNASU; 10519; -.
Ensembl; ENST00000328649; ENSP00000333873; ENSG00000185043. [Q99828-1]
Ensembl; ENST00000612800; ENSP00000479860; ENSG00000185043. [Q99828-2]
GeneID; 10519; -.
KEGG; hsa:10519; -.
UCSC; uc002bpb.5; human. [Q99828-1]
CTD; 10519; -.
DisGeNET; 10519; -.
GeneCards; CIB1; -.
H-InvDB; HIX0012576; -.
HGNC; HGNC:16920; CIB1.
HPA; CAB012991; -.
HPA; HPA048825; -.
MIM; 602293; gene.
neXtProt; NX_Q99828; -.
OpenTargets; ENSG00000185043; -.
PharmGKB; PA38423; -.
eggNOG; KOG0034; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00860000133737; -.
HOVERGEN; HBG107344; -.
InParanoid; Q99828; -.
KO; K17259; -.
OMA; QDGDCTF; -.
OrthoDB; EOG091G0OJZ; -.
PhylomeDB; Q99828; -.
TreeFam; TF313865; -.
SIGNOR; Q99828; -.
ChiTaRS; CIB1; human.
EvolutionaryTrace; Q99828; -.
GeneWiki; CIB1; -.
GenomeRNAi; 10519; -.
PRO; PR:Q99828; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000185043; -.
CleanEx; HS_CIB1; -.
ExpressionAtlas; Q99828; baseline and differential.
Genevisible; Q99828; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IMP:HGNC.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:HGNC.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IMP:HGNC.
GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; IMP:CACAO.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0043495; F:protein anchor; IGI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:CACAO.
GO; GO:0017016; F:Ras GTPase binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IMP:HGNC.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:HGNC.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
GO; GO:0006302; P:double-strand break repair; TAS:ProtInc.
GO; GO:0007113; P:endomitotic cell cycle; IDA:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; TAS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IGI:BHF-UCL.
GO; GO:2000256; P:positive regulation of male germ cell proliferation; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; ISS:UniProtKB.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Apoptosis; Calcium;
Cell adhesion; Cell cycle; Cell division; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Golgi apparatus; Lipoprotein; Magnesium; Membrane;
Metal-binding; Myristate; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Spermatogenesis.
INIT_MET 1 1 Removed.
CHAIN 2 191 Calcium and integrin-binding protein 1.
/FTId=PRO_0000073531.
DOMAIN 103 138 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 148 183 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 116 127 1.
CA_BIND 161 172 2.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:10366599}.
VAR_SEQ 29 29 L -> LSVYVVLAPHLVDNEQQARSGNEHTGRPIAENTDSS
PLSTR (in isoform 2).
{ECO:0000303|PubMed:23503467}.
/FTId=VSP_053740.
VARIANT 44 44 S -> T (in dbSNP:rs3210935).
{ECO:0000269|PubMed:10826701,
ECO:0000269|PubMed:9372844,
ECO:0000269|Ref.5}.
/FTId=VAR_019565.
VARIANT 106 106 I -> T (in dbSNP:rs11551250).
/FTId=VAR_048636.
MUTAGEN 2 2 G->A: Inhibits translocation to the
plasma membrane. Show increased apoptosis
after TNF stimulation.
{ECO:0000269|PubMed:19854831}.
MUTAGEN 78 78 S->A: Loss of phosphorylation by
PKD/PRKD2; in isoform 2.
{ECO:0000269|PubMed:23503467}.
MUTAGEN 78 78 S->E: Phosphomimetic; promotes tumor
growth by an indirect mechanism; in
isoform 2. {ECO:0000269|PubMed:23503467}.
MUTAGEN 114 117 IFDF->AAAA: Loss of binding to ITGAV.
{ECO:0000269|PubMed:24011356}.
MUTAGEN 115 115 F->A: Loss of binding to ITGA2B.
{ECO:0000269|PubMed:12023286}.
MUTAGEN 127 127 D->N: Cytoplasmic localization.
{ECO:0000269|PubMed:15475008}.
MUTAGEN 131 131 L->A,T: Loss of binding to ITGA2B.
{ECO:0000269|PubMed:12023286}.
MUTAGEN 152 153 LI->AA: Loss of binding to ITGA2B.
{ECO:0000269|PubMed:24011356}.
MUTAGEN 153 153 I->A: Loss of binding to ITGA2B.
{ECO:0000269|PubMed:12023286}.
MUTAGEN 167 167 T->A: No effect on phosphorylation by
PKD/PRKD2; in isoform 2.
{ECO:0000269|PubMed:23503467}.
MUTAGEN 172 172 E->Q: Cytoplasmic localization.
{ECO:0000269|PubMed:15475008}.
MUTAGEN 173 173 F->A: Loss of binding to ITGA2B.
{ECO:0000269|PubMed:12023286,
ECO:0000269|PubMed:16418530,
ECO:0000269|PubMed:24011356}.
MUTAGEN 173 173 F->A: Loss of binding to ITGA2B. Does not
inhibit interaction with PAK1.
{ECO:0000269|PubMed:12023286,
ECO:0000269|PubMed:16418530,
ECO:0000269|PubMed:24011356}.
CONFLICT 136 136 T -> M (in Ref. 6; CAG33236).
{ECO:0000305}.
CONFLICT 171 171 S -> F (in Ref. 4; AEZ06077).
{ECO:0000305}.
HELIX 14 16 {ECO:0000244|PDB:1XO5}.
TURN 18 20 {ECO:0000244|PDB:2L4I}.
HELIX 24 35 {ECO:0000244|PDB:1XO5}.
HELIX 40 42 {ECO:0000244|PDB:1XO5}.
HELIX 45 50 {ECO:0000244|PDB:1XO5}.
HELIX 55 59 {ECO:0000244|PDB:1XO5}.
HELIX 62 65 {ECO:0000244|PDB:1XO5}.
HELIX 70 77 {ECO:0000244|PDB:1XO5}.
STRAND 81 86 {ECO:0000244|PDB:1Y1A}.
HELIX 88 98 {ECO:0000244|PDB:1XO5}.
HELIX 104 115 {ECO:0000244|PDB:1XO5}.
STRAND 120 123 {ECO:0000244|PDB:1XO5}.
HELIX 125 135 {ECO:0000244|PDB:1XO5}.
STRAND 137 139 {ECO:0000244|PDB:1Y1A}.
STRAND 145 147 {ECO:0000244|PDB:2L4I}.
HELIX 149 160 {ECO:0000244|PDB:1XO5}.
STRAND 165 168 {ECO:0000244|PDB:1XO5}.
HELIX 170 179 {ECO:0000244|PDB:1XO5}.
HELIX 181 190 {ECO:0000244|PDB:1XO5}.
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


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