GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Cell cycle and apoptosis regulator protein 2 (Cell division cycle and apoptosis regulator protein 2) (DBIRD complex subunit KIAA1967) (Deleted in breast cancer gene 1 protein) (DBC-1) (DBC.1) (NET35) (p30 DBC)

 CCAR2_HUMAN             Reviewed;         923 AA.
Q8N163; A6NL03; B2RB79; D3DSR6; Q6P0Q9; Q8N3G7; Q8N8M1; Q8TF34; Q9H9Q9;
Q9HD12; Q9NT55;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 2.
12-AUG-2020, entry version 175.
RecName: Full=Cell cycle and apoptosis regulator protein 2;
AltName: Full=Cell division cycle and apoptosis regulator protein 2;
AltName: Full=DBIRD complex subunit KIAA1967;
AltName: Full=Deleted in breast cancer gene 1 protein;
Short=DBC-1;
Short=DBC.1;
AltName: Full=NET35;
AltName: Full=p30 DBC;
Name=CCAR2; Synonyms=DBC1, KIAA1967;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
Platzer M., Shimizu N., Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Placenta;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-923 (ISOFORM 2).
TISSUE=Brain;
PubMed=11853319; DOI=10.1093/dnares/8.6.319;
Nagase T., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XXII. The
complete sequences of 50 new cDNA clones which code for large proteins.";
DNA Res. 8:319-327(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 439-845, AND TISSUE SPECIFICITY.
PubMed=12370419; DOI=10.1073/pnas.212516099;
Hamaguchi M., Meth J.L., von Klitzing C., Wei W., Esposito D., Rodgers L.,
Walsh T., Welcsh P., King M.C., Wigler M.H.;
"DBC2, a candidate for a tumor suppressor gene involved in breast cancer.";
Proc. Natl. Acad. Sci. U.S.A. 99:13647-13652(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-678 AND SER-681, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[9]
FUNCTION AS SIRT1 INHIBITOR, INTERACTION WITH SIRT1, MUTAGENESIS OF
243-LEU--LEU-264, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18235501; DOI=10.1038/nature06500;
Kim J.-E., Chen J., Lou Z.;
"DBC1 is a negative regulator of SIRT1.";
Nature 451:583-586(2008).
[10]
FUNCTION IN APOPTOSIS, AND INTERACTION WITH SIRT1.
PubMed=18235502; DOI=10.1038/nature06515;
Zhao W., Kruse J.-P., Tang Y., Jung S.Y., Qin J., Gu W.;
"Negative regulation of the deacetylase SIRT1 by DBC1.";
Nature 451:587-590(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-675; SER-678 AND
SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
FUNCTION, IDENTIFICATION IN A NUCLEAR RECEPTOR HORMONE COMPLEX, AND
INTERACTION WITH ZNF335; ASH2L; EMSY.
PubMed=19131338; DOI=10.1074/jbc.m805872200;
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
"Identification and characterization of a novel nuclear protein complex
involved in nuclear hormone receptor-mediated gene regulation.";
J. Biol. Chem. 284:7542-7552(2009).
[14]
FUNCTION AS SUV39H1 INHIBITOR, AND INTERACTION WITH SUV39H1.
PubMed=19218236; DOI=10.1074/jbc.m900956200;
Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.;
"Inhibition of SUV39H1 methyltransferase activity by DBC1.";
J. Biol. Chem. 284:10361-10366(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-675; SER-678 AND
SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ESR1 AND ESR2.
PubMed=20074560; DOI=10.1016/j.bbrc.2010.01.025;
Koyama S., Wada-Hiraike O., Nakagawa S., Tanikawa M., Hiraike H.,
Miyamoto Y., Sone K., Oda K., Fukuhara H., Nakagawa K., Kato S., Yano T.,
Taketani Y.;
"Repression of estrogen receptor beta function by putative tumor suppressor
DBC1.";
Biochem. Biophys. Res. Commun. 392:357-362(2010).
[18]
FUNCTION, INTERACTION WITH BRCA1, AND SUBCELLULAR LOCATION.
PubMed=20160719; DOI=10.1038/sj.bjc.6605577;
Hiraike H., Wada-Hiraike O., Nakagawa S., Koyama S., Miyamoto Y., Sone K.,
Tanikawa M., Tsuruga T., Nagasaka K., Matsumoto Y., Oda K., Shoji K.,
Fukuhara H., Saji S., Nakagawa K., Kato S., Yano T., Taketani Y.;
"Identification of DBC1 as a transcriptional repressor for BRCA1.";
Br. J. Cancer 102:1061-1067(2010).
[19]
FUNCTION, AND INTERACTION WITH HDAC1; HDAC3; SIRT1 AND MEF2D.
PubMed=21030595; DOI=10.1074/jbc.m110.153270;
Chini C.C., Escande C., Nin V., Chini E.N.;
"HDAC3 is negatively regulated by the nuclear protein DBC1.";
J. Biol. Chem. 285:40830-40837(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-124; SER-675; SER-678
AND SER-681, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION AT THR-454, MUTAGENESIS OF THR-454, AND INTERACTION WITH
SIRT1.
PubMed=22735644; DOI=10.1093/jmcb/mjs035;
Zannini L., Buscemi G., Kim J.E., Fontanella E., Delia D.;
"DBC1 phosphorylation by ATM/ATR inhibits SIRT1 deacetylase in response to
DNA damage.";
J. Mol. Cell Biol. 4:294-303(2012).
[24]
IDENTIFICATION IN THE DBIRD COMPLEX, FUNCTION, AND INTERACTION WITH ZNF326.
PubMed=22446626; DOI=10.1038/nature10925;
Close P., East P., Dirac-Svejstrup A.B., Hartmann H., Heron M., Maslen S.,
Chariot A., Soding J., Skehel M., Svejstrup J.Q.;
"DBIRD complex integrates alternative mRNA splicing with RNA polymerase II
transcript elongation.";
Nature 484:386-389(2012).
[25]
FUNCTION, AND INTERACTION WITH NR1D1.
PubMed=23398316; DOI=10.1042/bj20121085;
Chini C.C., Escande C., Nin V., Chini E.N.;
"DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of
the nuclear receptor Rev-erbalpha.";
Biochem. J. 451:453-461(2013).
[26]
REVIEW.
PubMed=23841676; DOI=10.1042/bsr20130062;
Chini E.N., Chini C.C., Nin V., Escande C.;
"Deleted in breast cancer-1 (DBC-1) in the interface between metabolism,
aging and cancer.";
Biosci. Rep. 33:0-0(2013).
[27]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SIRT1.
PubMed=23352644; DOI=10.1016/j.canlet.2013.01.026;
Kim W., Kim J.E.;
"Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of
breast cancer cells through impaired responses to UV-induced DNA damage.";
Cancer Lett. 333:180-186(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; THR-454; SER-569;
SER-675; SER-678; SER-681; SER-687; SER-808 AND THR-897, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
REVIEW.
PubMed=24273392;
Joshi P., Quach O.L., Giguere S.S., Cristea I.M.;
"A functional proteomics perspective of dbc1 as a regulator of
transcription.";
J. Proteomics Bioinform. 0:0-0(2013).
[30]
ACETYLATION AT LYS-112 AND LYS-215, AND INTERACTION WITH SIRT1.
PubMed=24126058; DOI=10.1128/mcb.00874-13;
Zheng H., Yang L., Peng L., Izumi V., Koomen J., Seto E., Chen J.;
"hMOF acetylation of DBC1/CCAR2 prevents binding and inhibition of SirT1.";
Mol. Cell. Biol. 33:4960-4970(2013).
[31]
FUNCTION.
PubMed=24415752; DOI=10.1074/jbc.m113.512913;
Nin V., Chini C.C., Escande C., Capellini V., Chini E.N.;
"Deleted in breast cancer 1 (DBC1) protein regulates hepatic
gluconeogenesis.";
J. Biol. Chem. 289:5518-5527(2014).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-484; SER-569; SER-627 AND
SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND ARG-180, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[34]
SUMOYLATION AT LYS-591, DESUMOYLATION, PHOSPHORYLATION AT THR-454,
MUTAGENESIS OF THR-454; LYS-591; LYS-667 AND LYS-839, AND INTERACTION WITH
SIRT1; PSIA3 AND SENP1.
PubMed=25406032; DOI=10.1038/ncomms6483;
Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W., Ka S.H.,
Oh K.H., Jeon Y.J., Chung C.H.;
"Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in
response to DNA damage.";
Nat. Commun. 5:5483-5483(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-591, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[36]
FUNCTION, AND INTERACTION WITH CHEK2 AND PSEM3.
PubMed=25361978; DOI=10.1093/nar/gku1065;
Magni M., Ruscica V., Buscemi G., Kim J.E., Nachimuthu B.T., Fontanella E.,
Delia D., Zannini L.;
"Chk2 and REGgamma-dependent DBC1 regulation in DNA damage induced
apoptosis.";
Nucleic Acids Res. 42:13150-13160(2014).
[37]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=25732823; DOI=10.1016/j.celrep.2015.01.066;
Qin B., Minter-Dykhouse K., Yu J., Zhang J., Liu T., Zhang H., Lee S.,
Kim J., Wang L., Lou Z.;
"DBC1 functions as a tumor suppressor by regulating p53 stability.";
Cell Rep. 10:1324-1334(2015).
[38]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MCC.
PubMed=24824780; DOI=10.1002/ijc.28967;
Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N.,
Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R.;
"MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in
the cytoplasm.";
Int. J. Cancer 136:55-64(2015).
[39]
PHOSPHORYLATION AT THR-454, MUTAGENESIS OF THR-454, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND INTERACTION WITH CSNK2A1.
PubMed=24962073; DOI=10.1002/ijc.29043;
Bae J.S., Park S.H., Kim K.M., Kwon K.S., Kim C.Y., Lee H.K., Park B.H.,
Park H.S., Lee H., Moon W.S., Chung M.J., Sylvester K.G., Jang K.Y.;
"CK2alpha phosphorylates DBC1 and is involved in the progression of gastric
carcinoma and predicts poor survival of gastric carcinoma patients.";
Int. J. Cancer 136:797-809(2015).
[40]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NR1H2 AND NR1H3.
PubMed=25661920; DOI=10.1016/j.jsbmb.2015.02.001;
Sakurabashi A., Wada-Hiraike O., Hirano M., Fu H., Isono W., Fukuda T.,
Morita Y., Tanikawa M., Miyamoto Y., Oda K., Kawana K., Osuga Y., Fujii T.;
"CCAR2 negatively regulates nuclear receptor LXRalpha by competing with
SIRT1 deacetylase.";
J. Steroid Biochem. Mol. Biol. 149:80-88(2015).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-591, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Core component of the DBIRD complex, a multiprotein complex
that acts at the interface between core mRNP particles and RNA
polymerase II (RNAPII) and integrates transcript elongation with the
regulation of alternative splicing: the DBIRD complex affects local
transcript elongation rates and alternative splicing of a large set of
exons embedded in (A + T)-rich DNA regions (PubMed:22446626). Inhibits
SIRT1 deacetylase activity leading to increasing levels of p53/TP53
acetylation and p53-mediated apoptosis (PubMed:18235501,
PubMed:18235502, PubMed:23352644). Inhibits SUV39H1 methyltransferase
activity (PubMed:19218236). Mediates ligand-dependent transcriptional
activation by nuclear hormone receptors (PubMed:19131338). Plays a
critical role in maintaining genomic stability and cellular integrity
following UV-induced genotoxic stress (PubMed:23398316). Regulates the
circadian expression of the core clock components NR1D1 and ARNTL/BMAL1
(PubMed:23398316). Enhances the transcriptional repressor activity of
NR1D1 through stabilization of NR1D1 protein levels by preventing its
ubiquitination and subsequent degradation (PubMed:23398316). Represses
the ligand-dependent transcriptional activation function of ESR2
(PubMed:20074560). Acts as a regulator of PCK1 expression and
gluconeogenesis by a mechanism that involves, at least in part, both
NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase
activity of HDAC3 and can alter its subcellular localization
(PubMed:21030595). Positively regulates the beta-catenin pathway
(canonical Wnt signaling pathway) and is required for MCC-mediated
repression of the beta-catenin pathway (PubMed:24824780). Represses
ligand-dependent transcriptional activation function of NR1H2 and NR1H3
and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920).
Plays an important role in tumor suppression through p53/TP53
regulation; stabilizes p53/TP53 by affecting its interaction with
ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional
activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a
CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in
vitro (PubMed:25361978). {ECO:0000269|PubMed:18235501,
ECO:0000269|PubMed:18235502, ECO:0000269|PubMed:19131338,
ECO:0000269|PubMed:19218236, ECO:0000269|PubMed:20074560,
ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:21030595,
ECO:0000269|PubMed:22446626, ECO:0000269|PubMed:23352644,
ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24415752,
ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:25361978,
ECO:0000269|PubMed:25661920, ECO:0000269|PubMed:25732823}.
-!- SUBUNIT: Component of the DBIRD complex (PubMed:22446626). Interacts
with ZNF326/ZIRD; the interaction is direct (PubMed:22446626).
Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation
of substrates (PubMed:18235501, PubMed:18235502, PubMed:21030595,
PubMed:22735644, PubMed:23352644, PubMed:24126058, PubMed:25406032).
Interacts (via N-terminus) with SUV39H1; this interaction abolishes the
interaction with SIRT1 (PubMed:19218236). Component of a nuclear
receptor-mediated transcription complex composed of at least ZNF335,
CCAR2 and EMSY; the complex stimulates the transcription of nuclear
receptor target genes such as SOX9 and HOXA1 (PubMed:19131338). Within
the complex interacts with EMSY and interacts with ZNF335 (via C-
terminus) (PubMed:19131338). Components of this complex may associate
with components of a histone methylation complex to form a complex at
least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and
WDR5 (PubMed:19131338). Within this complex, interacts with ASH2L
(PubMed:19131338). Interacts with NR1D1 (PubMed:23398316). Interacts
(via N-terminus) with ESR1 and ESR2 (PubMed:20074560). Interacts (via
N-terminus) with HDAC3 (via C-terminus) (PubMed:21030595). Interacts
with HDAC1 and MED2F (PubMed:21030595). Interacts with MCC
(PubMed:24824780). Interacts (via N-terminus) with NR1H2 and NR1H3 in a
ligand-independent manner (PubMed:25661920). Interacts with CSNK2A1
(PubMed:24962073). Interacts (via N-terminus) with p53/TP53
(PubMed:25732823). Interacts (via N-terminus) with BRCA1 (via the BRCT
domains) (PubMed:20160719). Interacts (via N-terminus) with CHEK2 (via
protein kinase domain) (PubMed:25361978). Interacts with PSEM3
(PubMed:25361978). Interacts (via N-terminus) with PSIA3 and SENP1
(PubMed:25406032). The sumoylated form shows a preferential interaction
with SIRT1 as compared to its unmodified form (PubMed:25406032).
{ECO:0000269|PubMed:18235501, ECO:0000269|PubMed:18235502,
ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:19218236,
ECO:0000269|PubMed:20074560, ECO:0000269|PubMed:20160719,
ECO:0000269|PubMed:21030595, ECO:0000269|PubMed:22446626,
ECO:0000269|PubMed:22735644, ECO:0000269|PubMed:23352644,
ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:24126058,
ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:24962073,
ECO:0000269|PubMed:25361978, ECO:0000269|PubMed:25406032,
ECO:0000269|PubMed:25661920, ECO:0000269|PubMed:25732823}.
-!- INTERACTION:
Q8N163; P01106: MYC; NbExp=8; IntAct=EBI-355410, EBI-447544;
Q8N163; Q96EB6: SIRT1; NbExp=16; IntAct=EBI-355410, EBI-1802965;
Q8N163; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-355410, EBI-6248094;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20074560,
ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:23352644,
ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:24962073,
ECO:0000269|PubMed:25661920}. Cytoplasm {ECO:0000269|PubMed:20160719,
ECO:0000269|PubMed:24824780}. Note=Recruited to chromatin, post-UV
irradiation. Sequestered to the cytoplasm in the presence of MCC.
Translocated to the cytoplasm during UV-induced apoptosis.
{ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:24824780}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N163-1; Sequence=Displayed;
Name=2;
IsoId=Q8N163-2; Sequence=VSP_017092;
-!- TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the
expression gradually increases with the progression of the carcinoma
(at protein level). Expressed ubiquitously in normal tissues. Expressed
in 84 to 100% of neoplastic breast, lung, and colon tissues.
{ECO:0000269|PubMed:12370419, ECO:0000269|PubMed:24962073}.
-!- PTM: ATM/ATR-mediated phosphorylation at Thr-454 upon DNA damage
promotes binding to SIRT1. Phosphorylation at Thr-454 promotes its
sumoylation by switching the binding partner of CCAR2 from SENP1 to
PIAS3. {ECO:0000269|PubMed:22735644, ECO:0000269|PubMed:25406032}.
-!- PTM: Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory
binding to SIRT1 and increases its deacetylase activity.
{ECO:0000269|PubMed:24126058}.
-!- PTM: Genotoxic stress induces its sumoylation and sumoylation promotes
the SIRT1-CCAR2 interaction which in turn inhibits SIRT1-mediated
deacetylation of p53/TP53. Sumoylation leads to transcriptional
activation of p53/TP53 by sequestering SIRT1 from p53/TP53.
Desumoylated by SENP1. {ECO:0000269|PubMed:25406032}.
-!- SEQUENCE CAUTION:
Sequence=AAG02472.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=BAB85553.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KIAA1967ID46056ch8p21.html";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AK096547; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK314535; BAG37126.1; -; mRNA.
EMBL; AL834162; CAD38866.1; -; mRNA.
EMBL; AL834351; CAD39016.1; -; mRNA.
EMBL; AL834352; CAD39017.1; -; mRNA.
EMBL; BX640952; CAE45976.1; -; mRNA.
EMBL; AL137523; CAB70788.3; -; mRNA.
EMBL; AC037459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63658.1; -; Genomic_DNA.
EMBL; CH471080; EAW63661.1; -; Genomic_DNA.
EMBL; BC018269; AAH18269.2; -; mRNA.
EMBL; BC065495; AAH65495.1; -; mRNA.
EMBL; AB075847; BAB85553.1; ALT_INIT; mRNA.
EMBL; AF293335; AAG02472.1; ALT_FRAME; mRNA.
CCDS; CCDS34863.1; -. [Q8N163-1]
PIR; T46368; T46368.
RefSeq; NP_066997.3; NM_021174.5. [Q8N163-1]
SMR; Q8N163; -.
BioGRID; 121775; 155.
CORUM; Q8N163; -.
DIP; DIP-38122N; -.
IntAct; Q8N163; 92.
MINT; Q8N163; -.
STRING; 9606.ENSP00000310670; -.
iPTMnet; Q8N163; -.
PhosphoSitePlus; Q8N163; -.
SwissPalm; Q8N163; -.
BioMuta; CCAR2; -.
DMDM; 85701135; -.
EPD; Q8N163; -.
jPOST; Q8N163; -.
MassIVE; Q8N163; -.
MaxQB; Q8N163; -.
PaxDb; Q8N163; -.
PeptideAtlas; Q8N163; -.
PRIDE; Q8N163; -.
ProteomicsDB; 71566; -. [Q8N163-1]
ProteomicsDB; 71567; -. [Q8N163-2]
Antibodypedia; 9629; 282 antibodies.
DNASU; 57805; -.
Ensembl; ENST00000308511; ENSP00000310670; ENSG00000158941. [Q8N163-1]
Ensembl; ENST00000389279; ENSP00000373930; ENSG00000158941. [Q8N163-1]
GeneID; 57805; -.
KEGG; hsa:57805; -.
UCSC; uc003xch.4; human. [Q8N163-1]
CTD; 57805; -.
DisGeNET; 57805; -.
EuPathDB; HostDB:ENSG00000158941.16; -.
GeneCards; CCAR2; -.
HGNC; HGNC:23360; CCAR2.
HPA; ENSG00000158941; Low tissue specificity.
MIM; 607359; gene.
neXtProt; NX_Q8N163; -.
OpenTargets; ENSG00000158941; -.
PharmGKB; PA134993792; -.
eggNOG; KOG4246; Eukaryota.
GeneTree; ENSGT00530000063672; -.
HOGENOM; CLU_008030_2_0_1; -.
InParanoid; Q8N163; -.
OMA; LEMQRMV; -.
OrthoDB; 614048at2759; -.
PhylomeDB; Q8N163; -.
TreeFam; TF316387; -.
PathwayCommons; Q8N163; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
BioGRID-ORCS; 57805; 17 hits in 861 CRISPR screens.
ChiTaRS; CCAR2; human.
GeneWiki; KIAA1967; -.
GenomeRNAi; 57805; -.
Pharos; Q8N163; Tbio.
PRO; PR:Q8N163; -.
Proteomes; UP000005640; Chromosome 8.
RNAct; Q8N163; protein.
Bgee; ENSG00000158941; Expressed in cortical plate and 203 other tissues.
ExpressionAtlas; Q8N163; baseline and differential.
Genevisible; Q8N163; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0044609; C:DBIRD complex; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
GO; GO:0030374; F:nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0043086; P:negative regulation of catalytic activity; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:2000003; P:positive regulation of DNA damage checkpoint; IMP:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
GO; GO:0090311; P:regulation of protein deacetylation; IDA:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0009411; P:response to UV; IMP:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR025224; CCAR1/CCAR2.
InterPro; IPR028811; CCAR2.
InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR025223; S1-like_RNA-bd_dom.
PANTHER; PTHR14304; PTHR14304; 1.
PANTHER; PTHR14304:SF12; PTHR14304:SF12; 1.
Pfam; PF14443; DBC1; 1.
Pfam; PF14444; S1-like; 1.
SMART; SM01122; DBC1; 1.
SUPFAM; SSF47473; SSF47473; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Apoptosis;
Biological rhythms; Cell cycle; Coiled coil; Cytoplasm; DNA damage;
Isopeptide bond; Metalloenzyme inhibitor; Methylation; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Transcription; Transcription regulation; Tumor suppressor; Ubl conjugation;
Wnt signaling pathway.
CHAIN 1..923
/note="Cell cycle and apoptosis regulator protein 2"
/id="PRO_0000050813"
REGION 610..670
/note="Interaction with MCC"
/evidence="ECO:0000269|PubMed:24824780"
REGION 704..923
/note="Interaction with NR1D1"
/evidence="ECO:0000269|PubMed:23398316"
COILED 829..909
/evidence="ECO:0000255"
MOD_RES 35
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231"
MOD_RES 112
/note="N6-acetyllysine; by KAT8"
/evidence="ECO:0000269|PubMed:24126058"
MOD_RES 123
/note="N6-methyllysine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 124
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 180
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 215
/note="N6-acetyllysine; by KAT8"
/evidence="ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:24126058"
MOD_RES 454
/note="Phosphothreonine; by ATM, ATR and CK2"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22735644, ECO:0000269|PubMed:24962073"
MOD_RES 484
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 569
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 627
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 675
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 678
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 681
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 687
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 808
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 897
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
CROSSLNK 591
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2 and SUMO3); alternate"
/evidence="ECO:0000269|PubMed:25406032"
CROSSLNK 591
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733"
VAR_SEQ 910..923
/note="ADSWVEKEEPAPSN -> VRWGWTRRQHSSFP (in isoform 2)"
/evidence="ECO:0000303|PubMed:11853319"
/id="VSP_017092"
MUTAGEN 243..264
/note="Missing: Abolishes binding to SIRT1."
/evidence="ECO:0000269|PubMed:18235501"
MUTAGEN 454
/note="T->A: Significantly reduces association with SIRT1.
Decreases sumoylation and the interaction of the sumoylated
form with SIRT1. Inhibits CCAR2-PSIA3 interaction.
Increases CCAR2-SENP1 interaction. Down-regulation of the
signals related with the epithelial-mesenchymal transition
of gastric cancer cells."
/evidence="ECO:0000269|PubMed:22735644,
ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:25406032"
MUTAGEN 454
/note="T->D: Significantly increases association with SIRT1
and induces p53 acetylation and apoptosis. Increases
sumoylation and the interaction of the sumoylated form with
SIRT1. Promotes CCAR2-PSIA3 interaction. Decreases CCAR2-
SENP1 interaction."
/evidence="ECO:0000269|PubMed:22735644,
ECO:0000269|PubMed:25406032"
MUTAGEN 591
/note="K->R: Loss of sumoylation."
/evidence="ECO:0000269|PubMed:25406032"
MUTAGEN 667
/note="K->R: No effect on sumoylation."
/evidence="ECO:0000269|PubMed:25406032"
MUTAGEN 839
/note="K->R: No effect on sumoylation."
/evidence="ECO:0000269|PubMed:25406032"
CONFLICT 47
/note="R -> S (in Ref. 2; CAD38866/CAD39017)"
/evidence="ECO:0000305"
CONFLICT 850
/note="T -> S (in Ref. 5; AAH65495)"
/evidence="ECO:0000305"
CONFLICT 908
/note="E -> G (in Ref. 2; CAD38866/CAD39017)"
/evidence="ECO:0000305"
SEQUENCE 923 AA; 102902 MW; 1733934377E35D21 CRC64;
MSQFKRQRIN PLPGGRNFSG TASTSLLGPP PGLLTPPVAT ELSQNARHLQ GGEKQRVFTG
IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP
LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR
FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LPPYRVHLTP YTVDSPICDF
LELQRRYRSL LVPSDFLSVH LSWLSAFPLS QPFSLHHPSR IQVSSEKEAA PDAGAEPITA
DSDPAYSSKV LLLSSPGLEE LYRCCMLFVD DMAEPRETPE HPLKQIKFLL GRKEEEAVLV
GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSGCT KWWRFAEFQY LQPGPPRRLQ
TVVVYLPDVW TIMPTLEEWE ALCQQKAAEA APPTQEAQGE TEPTEQAPDA LEQAADTSRR
NAETPEATTQ QETDTDLPEA PPPPLEPAVI ARPGCVNLSL HGIVEDRRPK ERISFEVMVL
AELFLEMLQR DFGYRVYKML LSLPEKVVSP PEPEKEEAAK EEATKEEEAI KEEVVKEPKD
EAQNEGPATE SEAPLKEDGL LPKPLSSGGE EEEKPRGEAS EDLCEMALDP ELLLLRDDGE
EEFAGAKLED SEVRSVASNQ SEMEFSSLQD MPKELDPSAV LPLDCLLAFV FFDANWCGYL
HRRDLERILL TLGIRLSAEQ AKQLVSRVVT QNICQYRSLQ YSRQEGLDGG LPEEVLFGNL
DLLPPPGKST KPGAAPTEHK ALVSHNGSLI NVGSLLQRAE QQDSGRLYLE NKIHTLELKL
EESHNRFSAT EVTNKTLAAE MQELRVRLAE AEETARTAER QKSQLQRLLQ ELRRRLTPLQ
LEIQRVVEKA DSWVEKEEPA PSN


Related products :

Catalog number Product name Quantity
EIAAB05873 CARP1,CARP-1,CCAR1,Cell cycle and apoptosis regulatory protein 1,Cell division cycle and apoptosis regulator protein 1,Death inducer with SAP domain,DIS,Homo sapiens,Human
EIAAB05874 Carp1,CARP-1,Ccar1,Cell cycle and apoptosis regulatory protein 1,Cell division cycle and apoptosis regulator protein 1,Mouse,Mus musculus
CCAR1_MOUSE ELISA Kit FOR Cell division cycle and apoptosis regulator protein 1; organism: Mouse; gene name: Ccar1 96T
CCAR1_HUMAN ELISA Kit FOR Cell division cycle and apoptosis regulator protein 1; organism: Human; gene name: CCAR1 96T
CSB-EL004614HU Human Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit 96T
CSB-EL004614MO Mouse Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit 96T
CSB-EL004614MO Mouse Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit SpeciesMouse 96T
CSB-EL004614HU Human Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit SpeciesHuman 96T
CCBL1 CCAR1 Gene cell division cycle and apoptosis regulator 1
E14065h Human Cell Division Cycle And Apoptosis Regulator 96T
CSB-EL004614MO Mouse cell division cycle and apoptosis regulator 1 (CCAR1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL004614HU Human cell division cycle and apoptosis regulator 1 (CCAR1) ELISA kit, Species Human, Sample Type serum, plasma 96T
27-305 In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. CHEK2 is a cell cycle checkpoint regulator and putative tumor 0.05 mg
30-841 HUS1Bis most closely related to HUS1, a component of a cell cycle checkpoint protein complex involved in cell cycle arrest in response to DNA damage. HUS1B can interact with the check point protein RA 0.05 mg
EIAAB06429 Anaphase-promoting complex subunit CDC26,Cdc26,Cell division cycle protein 26 homolog,Protein BWK-2,Rat,Rattus norvegicus
EIAAB06420 Anapc6,Anaphase-promoting complex subunit 6,APC6,Cdc16,Cell division cycle protein 16 homolog,Cyclosome subunit 6,Mouse,Mus musculus
E1771b ELISA ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
E1771m ELISA Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
E1771m ELISA kit Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
E1771b ELISA kit ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
U1771m CLIA Anapc8,Anaphase-promoting complex subunit 8,APC8,Cdc23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Mouse,Mus musculus 96T
U1771b CLIA ANAPC8,Anaphase-promoting complex subunit 8,APC8,Bos taurus,Bovine,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8 96T
E1771h ELISA kit ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
E1771h ELISA ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
U1771h CLIA ANAPC8,Anaphase-promoting complex subunit 8,APC8,CDC23,Cell division cycle protein 23 homolog,Cyclosome subunit 8,Homo sapiens,Human 96T
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP1689: Porphyrin and chlorophyll metabolism
WP414: Cell Cycle and Cell Division
WP1694: Pyrimidine metabolism
WP964: Cell cycle
WP1782: APC/C-mediated degradation of cell cycle proteins
WP1195: G1 to S cell cycle control
WP445: G1 to S cell cycle control
WP1792: Cell Cycle, Mitotic
WP840: G1 to S cell cycle control
WP1693: Purine metabolism
WP1900: Regulation of mitotic cell cycle
WP1663: Homologous recombination
WP2414: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP1393: Cell cycle
WP1672: Mismatch repair
WP2435: Quercetin and Nf-kB/ AP-1 induced cell apoptosis
WP348: G1 to S cell cycle control
WP1775: Cell Cycle Checkpoints
WP2328: Allograft rejection
WP2152: BDNF
WP1078: G1 to S cell cycle control
WP179: Cell cycle
WP1200: Cell cycle

Related Genes :
[CCAR1 CARP1 DIS] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)
[Ccar1 Carp1] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1)
[BIRC7 KIAP LIVIN MLIAP RNF50 UNQ5800/PRO19607/PRO21344] Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Kidney inhibitor of apoptosis protein) (KIAP) (Livin) (Melanoma inhibitor of apoptosis protein) (ML-IAP) (RING finger protein 50) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30kDa subunit (Truncated livin) (p30-Livin) (tLivin)]
[BRCA1 RNF53] Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[INTS13 ASUN C12orf11 GCT1] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95)
[Taf1 Ccg1] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[SIRT1 SIR2L1] NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[CDCA7 JPO1] Cell division cycle-associated protein 7 (Protein JPO1)
[Asun IntS13 Mat89Bb ovary2 CG6814] Protein asunder (Cell cycle regulator Mat89Bb) (Integrator complex subunit 13) (Maternal transcript 89Bb) (Set apart in position or space protein)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[TAF1 BA2R CCG1 CCGS TAF2A] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)
[BIRC3 API2 MIHC RNF49] Baculoviral IAP repeat-containing protein 3 (EC 2.3.2.27) (Apoptosis inhibitor 2) (API2) (Cellular inhibitor of apoptosis 2) (C-IAP2) (IAP homolog C) (Inhibitor of apoptosis protein 1) (hIAP-1) (hIAP1) (RING finger protein 49) (RING-type E3 ubiquitin transferase BIRC3) (TNFR2-TRAF-signaling complex protein 1)
[BIRC2 API1 MIHB RNF48] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[PSME3] Proteasome activator complex subunit 3 (11S regulator complex subunit gamma) (REG-gamma) (Activator of multicatalytic protease subunit 3) (Ki nuclear autoantigen) (Proteasome activator 28 subunit gamma) (PA28g) (PA28gamma)
[CDC36 DNA19 NOT2 YDL165W] General negative regulator of transcription subunit 2 (cell division cycle protein 36)
[CDCA8 PESCRG3] Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDC43 CAL1 YGL155W G1864] Geranylgeranyl transferase type-1 subunit beta (GGTase-I-beta) (EC 2.5.1.59) (Cell division cycle protein 43) (Geranylgeranyl transferase type I subunit beta) (RAS proteins geranylgeranyltransferase subunit beta) (Type I protein geranyl-geranyltransferase subunit beta) (PGGTase I beta)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[CDK1 CDC2 CDKN1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Hmgb1 Hmg-1 Hmg1] High mobility group protein B1 (Amphoterin) (Heparin-binding protein p30) (High mobility group protein 1) (HMG-1)
[Bcl2l1 Bcl2l Bclx] Bcl-2-like protein 1 (Bcl2-L-1) (Apoptosis regulator Bcl-X)

Bibliography :