GENTAUR Molecular Products.

 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.
 07-NOV-2018, entry version 161.
 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";
 -----------------------------------------------------------------------
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 Distributed under the Creative Commons Attribution (CC BY 4.0) License
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 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; 110.
 CORUM; Q8N163; -.
 DIP; DIP-38122N; -.
 IntAct; Q8N163; 66.
 MINT; Q8N163; -.
 STRING; 9606.ENSP00000310670; -.
 iPTMnet; Q8N163; -.
 PhosphoSitePlus; Q8N163; -.
 SwissPalm; Q8N163; -.
 BioMuta; KIAA1967; -.
 DMDM; 85701135; -.
 EPD; Q8N163; -.
 MaxQB; Q8N163; -.
 PaxDb; Q8N163; -.
 PeptideAtlas; Q8N163; -.
 PRIDE; Q8N163; -.
 ProteomicsDB; 71566; -.
 ProteomicsDB; 71567; -. [Q8N163-2]
 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; PLQLEMQ; -.
 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; Expressed in 190 organ(s), highest expression level in right testis.
 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: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; 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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