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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.
25-OCT-2017, entry version 153.
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 IN TRANSCRIPTIONAL REGULATION, AND IDENTIFICATION IN A
COMPLEX WITH HCFC1; MKI67; EMSY; MATR3; HSPA8; TUBB2A; ZNF335; ASCL2;
RBBP5 AND WDR5.
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.
Inhibits SIRT1 deacetylase activity leading to increasing levels
of p53/TP53 acetylation and p53-mediated apoptosis. Inhibits
SUV39H1 methyltransferase activity. As part of a histone H3-
specific methyltransferase complex may mediate ligand-dependent
transcriptional activation by nuclear hormone receptors. Plays a
critical role in maintaining genomic stability and cellular
integrity following UV-induced genotoxic stress. Regulates the
circadian expression of the core clock components NR1D1 and
ARNTL/BMAL1. Enhances the transcriptional repressor activity of
NR1D1 through stabilization of NR1D1 protein levels by preventing
its ubiquitination and subsequent degradation (PubMed:18235501,
PubMed:18235502, PubMed:19131338, PubMed:19218236,
PubMed:22446626, PubMed:23352644, 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. Interacts with
ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus)
with SIRT1, which inhibits the deacetylation of substrates.
Interacts (via N-terminus) with SUV39H1; this interaction
abolishes the interaction with SIRT1. Part of a complex composed
at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5,
TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
specific methyltransferase activity. Interacts with NR1D1.
Interacts (via N-terminus) with ESR1 and ESR2. Interacts (via N-
terminus) with HDAC3 (via C-terminus). Interacts with HDAC1 and
MED2F. Interacts with MCC. Interacts (via N-terminus) with NR1H2
and NR1H3 in a ligand-independent manner. Interacts with CSNK2A1.
Interacts (via N-terminus) with p53/TP53. Interacts (via N-
terminus) with BRCA1 (via the BRCT domains). Interacts (via N-
terminus) with CHEK2 (via protein kinase domain). Interacts with
PSEM3. Interacts (via N-terminus) with PSIA3 and SENP1. The
sumoylated form shows a preferential interaction with SIRT1 as
compared to its unmodified form. {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:
P01106:MYC; NbExp=8; IntAct=EBI-355410, EBI-447544;
Q9Q2G4:ORF (xeno); NbExp=5; IntAct=EBI-355410, EBI-6248094;
Q96EB6:SIRT1; NbExp=16; IntAct=EBI-355410, EBI-1802965;
-!- 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;
Note=No experimental confirmation available.;
-!- 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; Positions=610, 622, 794, 810; Evidence={ECO:0000305};
Sequence=BAB85553.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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 http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs 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]
UniGene; Hs.744848; -.
ProteinModelPortal; Q8N163; -.
SMR; Q8N163; -.
BioGrid; 121775; 106.
CORUM; Q8N163; -.
DIP; DIP-38122N; -.
IntAct; Q8N163; 60.
MINT; MINT-5003338; -.
STRING; 9606.ENSP00000310670; -.
iPTMnet; Q8N163; -.
PhosphoSitePlus; Q8N163; -.
SwissPalm; Q8N163; -.
BioMuta; KIAA1967; -.
DMDM; 85701135; -.
EPD; Q8N163; -.
MaxQB; Q8N163; -.
PaxDb; Q8N163; -.
PeptideAtlas; Q8N163; -.
PRIDE; Q8N163; -.
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; CAB072827; -.
HPA; CAB072828; -.
HPA; HPA019907; -.
HPA; HPA019943; -.
MIM; 607359; gene.
neXtProt; NX_Q8N163; -.
OpenTargets; ENSG00000158941; -.
PharmGKB; PA134993792; -.
eggNOG; KOG4246; Eukaryota.
eggNOG; ENOG4111FW4; LUCA.
GeneTree; ENSGT00530000063672; -.
HOVERGEN; HBG081843; -.
InParanoid; Q8N163; -.
OMA; ASNQSEM; -.
OrthoDB; EOG091G03QV; -.
PhylomeDB; Q8N163; -.
TreeFam; TF316387; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
ChiTaRS; CCAR2; human.
GeneWiki; KIAA1967; -.
GenomeRNAi; 57805; -.
PRO; PR:Q8N163; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000158941; -.
CleanEx; HS_DBC1; -.
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:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core 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: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; Complete proteome;
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 Cell cycle and apoptosis regulator
protein 2.
/FTId=PRO_0000050813.
REGION 610 670 Interaction with MCC.
{ECO:0000269|PubMed:24824780}.
REGION 704 923 Interaction with NR1D1.
{ECO:0000269|PubMed:23398316}.
COILED 829 909 {ECO:0000255}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 112 112 N6-acetyllysine; by KAT8.
{ECO:0000269|PubMed:24126058}.
MOD_RES 123 123 N6-methyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 180 180 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 215 215 N6-acetyllysine; by KAT8.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:24126058}.
MOD_RES 454 454 Phosphothreonine; by ATM, ATR and CK2.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22735644,
ECO:0000269|PubMed:24962073}.
MOD_RES 484 484 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 678 678 Phosphoserine.
{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 681 681 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 897 897 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 591 591 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2 and
SUMO3); alternate.
{ECO:0000269|PubMed:25406032}.
CROSSLNK 591 591 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 910 923 ADSWVEKEEPAPSN -> VRWGWTRRQHSSFP (in
isoform 2).
{ECO:0000303|PubMed:11853319}.
/FTId=VSP_017092.
MUTAGEN 243 264 Missing: Abolishes binding to SIRT1.
{ECO:0000269|PubMed:18235501}.
MUTAGEN 454 454 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.
{ECO:0000269|PubMed:22735644,
ECO:0000269|PubMed:24962073,
ECO:0000269|PubMed:25406032}.
MUTAGEN 454 454 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.
{ECO:0000269|PubMed:22735644,
ECO:0000269|PubMed:25406032}.
MUTAGEN 591 591 K->R: Loss of sumoylation.
{ECO:0000269|PubMed:25406032}.
MUTAGEN 667 667 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:25406032}.
MUTAGEN 839 839 K->R: No effect on sumoylation.
{ECO:0000269|PubMed:25406032}.
CONFLICT 47 47 R -> S (in Ref. 2; CAD38866/CAD39017).
{ECO:0000305}.
CONFLICT 850 850 T -> S (in Ref. 5; AAH65495).
{ECO:0000305}.
CONFLICT 908 908 E -> G (in Ref. 2; CAD38866/CAD39017).
{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


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