CTBP2_HUMAN
ID CTBP2_HUMAN Reviewed; 445 AA.
AC P56545; A8K2X5; D3DRF5; O43449; Q5SQP7; Q69YI3; Q86SV0; Q8IY44; Q9H2T8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=C-terminal-binding protein 2;
DE Short=CtBP2;
GN Name=CTBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9479502; DOI=10.1006/geno.1997.5115;
RA Katsanis N., Fisher E.M.C.;
RT "A novel C-terminal binding protein (CTBP2) is closely related to CTBP1, an
RT adenovirus E1A-binding protein, and maps to human chromosome 21q21.3.";
RL Genomics 47:294-299(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11163272; DOI=10.1016/s0896-6273(00)00159-8;
RA Schmitz F., Koenigstorfer A., Suedhof T.C.;
RT "RIBEYE, a component of synaptic ribbons: a protein's journey through
RT evolution provides insight into synaptic ribbon function.";
RL Neuron 28:857-872(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Colon, Kidney, Pancreas, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 263-272, AND PHOSPHORYLATION.
RC TISSUE=B-cell, and Cervix carcinoma;
RX PubMed=7479821; DOI=10.1073/pnas.92.23.10467;
RA Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T.,
RA Chinnadurai G.;
RT "Molecular cloning and characterization of a cellular phosphoprotein that
RT interacts with a conserved C-terminal domain of adenovirus E1A involved in
RT negative modulation of oncogenic transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995).
RN [11]
RP INTERACTION WITH PNN.
RX PubMed=15542832; DOI=10.1128/mcb.24.23.10223-10235.2004;
RA Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E.,
RA Sugrue S.P.;
RT "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional
RT corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin
RT gene.";
RL Mol. Cell. Biol. 24:10223-10235(2004).
RN [12]
RP INTERACTION WITH NRIP1.
RX PubMed=15060175; DOI=10.1093/nar/gkh524;
RA Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F.,
RA Khochbin S., Jalaguier S., Cavailles V.;
RT "Multiple domains of the receptor-interacting protein 140 contribute to
RT transcription inhibition.";
RL Nucleic Acids Res. 32:1957-1966(2004).
RN [13]
RP INTERACTION WITH WIZ.
RX PubMed=16702210; DOI=10.1074/jbc.m603087200;
RA Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the
RT co-repressor molecule CtBP.";
RL J. Biol. Chem. 281:20120-20128(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=23747199; DOI=10.1016/j.virol.2013.05.018;
RA Subramanian T., Zhao L.J., Chinnadurai G.;
RT "Interaction of CtBP with adenovirus E1A suppresses immortalization of
RT primary epithelial cells and enhances virus replication during productive
RT infection.";
RL Virology 443:313-320(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP INTERACTION WITH MCRIP1.
RX PubMed=25728771; DOI=10.1016/j.molcel.2015.01.023;
RA Ichikawa K., Kubota Y., Nakamura T., Weng J.S., Tomida T., Saito H.,
RA Takekawa M.;
RT "MCRIP1, an ERK substrate, mediates ERK-induced gene silencing during
RT epithelial-mesenchymal transition by regulating the co-repressor CtBP.";
RL Mol. Cell 58:35-46(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 31-364 IN COMPLEX WITH NAD.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human CTBP2 dehydrogenase complexed with NAD(H).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC Functions in brown adipose tissue (BAT) differentiation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform 2 probably acts as a scaffold for specialized
CC synapses.
CC -!- SUBUNIT: Can form homodimers or heterodimers of CTBP1 and CTBP2.
CC Interacts with HIPK2 and ZNF217. Interacts with PRDM16; represses white
CC adipose tissue (WAT)-specific genes expression (By similarity).
CC Interacts with PNN, NRIP1 and WIZ. Interacts with MCRIP1
CC (PubMed:25728771). {ECO:0000250, ECO:0000269|PubMed:15060175,
CC ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:16702210,
CC ECO:0000269|PubMed:25728771, ECO:0000269|Ref.20}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1A
CC protein; this interaction seems to potentiate viral replication.
CC {ECO:0000269|PubMed:23747199}.
CC -!- INTERACTION:
CC P56545; P20749: BCL3; NbExp=2; IntAct=EBI-741533, EBI-958997;
CC P56545; P51946: CCNH; NbExp=5; IntAct=EBI-741533, EBI-741406;
CC P56545; Q13363: CTBP1; NbExp=13; IntAct=EBI-741533, EBI-908846;
CC P56545; Q13363-2: CTBP1; NbExp=5; IntAct=EBI-741533, EBI-10171858;
CC P56545; A0A0S2Z5I3: DMRTB1; NbExp=3; IntAct=EBI-741533, EBI-16431245;
CC P56545; Q13643: FHL3; NbExp=4; IntAct=EBI-741533, EBI-741101;
CC P56545; O15409: FOXP2; NbExp=4; IntAct=EBI-741533, EBI-983612;
CC P56545; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-741533, EBI-3059266;
CC P56545; Q14526: HIC1; NbExp=2; IntAct=EBI-741533, EBI-2507362;
CC P56545; Q13422: IKZF1; NbExp=5; IntAct=EBI-741533, EBI-745305;
CC P56545; Q9UKS7: IKZF2; NbExp=3; IntAct=EBI-741533, EBI-3893057;
CC P56545; Q96JN0: LCOR; NbExp=5; IntAct=EBI-741533, EBI-746045;
CC P56545; O94818-2: NOL4; NbExp=3; IntAct=EBI-741533, EBI-10190763;
CC P56545; Q96MY1: NOL4L; NbExp=3; IntAct=EBI-741533, EBI-6660790;
CC P56545; Q9NQ66: PLCB1; NbExp=3; IntAct=EBI-741533, EBI-3396023;
CC P56545; O75807: PPP1R15A; NbExp=2; IntAct=EBI-741533, EBI-714746;
CC P56545; Q92786: PROX1; NbExp=2; IntAct=EBI-741533, EBI-3912635;
CC P56545; Q9Y5P3: RAI2; NbExp=4; IntAct=EBI-741533, EBI-746228;
CC P56545; Q9UN79: SOX13; NbExp=2; IntAct=EBI-741533, EBI-3928516;
CC P56545; Q15583: TGIF1; NbExp=5; IntAct=EBI-741533, EBI-714215;
CC P56545; Q15583-2: TGIF1; NbExp=3; IntAct=EBI-741533, EBI-12691451;
CC P56545; Q92618: ZNF516; NbExp=6; IntAct=EBI-741533, EBI-2799490;
CC P56545; Q32MQ0: ZNF750; NbExp=3; IntAct=EBI-741533, EBI-10240029;
CC P56545; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-741533, EBI-6115394;
CC P56545-3; P54253: ATXN1; NbExp=3; IntAct=EBI-10171902, EBI-930964;
CC P56545-3; A0A0A0MR97: BAZ2B; NbExp=5; IntAct=EBI-10171902, EBI-11985607;
CC P56545-3; Q9UIF8-2: BAZ2B; NbExp=3; IntAct=EBI-10171902, EBI-10321972;
CC P56545-3; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-10171902, EBI-6083685;
CC P56545-3; Q02641: CACNB1; NbExp=3; IntAct=EBI-10171902, EBI-947514;
CC P56545-3; Q08289: CACNB2; NbExp=5; IntAct=EBI-10171902, EBI-2874501;
CC P56545-3; P54284: CACNB3; NbExp=8; IntAct=EBI-10171902, EBI-1184651;
CC P56545-3; O00305: CACNB4; NbExp=3; IntAct=EBI-10171902, EBI-714838;
CC P56545-3; Q9Y6W3: CAPN7; NbExp=3; IntAct=EBI-10171902, EBI-1765641;
CC P56545-3; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-10171902, EBI-744545;
CC P56545-3; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-10171902, EBI-744556;
CC P56545-3; Q76N32-2: CEP68; NbExp=3; IntAct=EBI-10171902, EBI-11975967;
CC P56545-3; P33240: CSTF2; NbExp=3; IntAct=EBI-10171902, EBI-711360;
CC P56545-3; Q13363-2: CTBP1; NbExp=4; IntAct=EBI-10171902, EBI-10171858;
CC P56545-3; P56545-3: CTBP2; NbExp=3; IntAct=EBI-10171902, EBI-10171902;
CC P56545-3; I6L9A0: DMRTB1; NbExp=3; IntAct=EBI-10171902, EBI-10178554;
CC P56545-3; O60941-5: DTNB; NbExp=5; IntAct=EBI-10171902, EBI-11984733;
CC P56545-3; Q9H596: DUSP21; NbExp=3; IntAct=EBI-10171902, EBI-7357329;
CC P56545-3; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-10171902, EBI-1175354;
CC P56545-3; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-10171902, EBI-12012124;
CC P56545-3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10171902, EBI-744099;
CC P56545-3; Q01543: FLI1; NbExp=3; IntAct=EBI-10171902, EBI-2271018;
CC P56545-3; O15409: FOXP2; NbExp=3; IntAct=EBI-10171902, EBI-983612;
CC P56545-3; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-10171902, EBI-7251368;
CC P56545-3; P20719: HOXA5; NbExp=5; IntAct=EBI-10171902, EBI-8470697;
CC P56545-3; P09067: HOXB5; NbExp=8; IntAct=EBI-10171902, EBI-3893317;
CC P56545-3; Q00444: HOXC5; NbExp=3; IntAct=EBI-10171902, EBI-11955357;
CC P56545-3; P42858: HTT; NbExp=3; IntAct=EBI-10171902, EBI-466029;
CC P56545-3; Q13422: IKZF1; NbExp=3; IntAct=EBI-10171902, EBI-745305;
CC P56545-3; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-10171902, EBI-11522367;
CC P56545-3; Q9UKS7: IKZF2; NbExp=3; IntAct=EBI-10171902, EBI-3893057;
CC P56545-3; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-10171902, EBI-747204;
CC P56545-3; P57682: KLF3; NbExp=3; IntAct=EBI-10171902, EBI-8472267;
CC P56545-3; Q16719-2: KYNU; NbExp=3; IntAct=EBI-10171902, EBI-12351611;
CC P56545-3; Q96JN0: LCOR; NbExp=3; IntAct=EBI-10171902, EBI-746045;
CC P56545-3; Q8N3X6-3: LCORL; NbExp=3; IntAct=EBI-10171902, EBI-12111580;
CC P56545-3; P61968: LMO4; NbExp=3; IntAct=EBI-10171902, EBI-2798728;
CC P56545-3; Q8IXL7-2: MSRB3; NbExp=5; IntAct=EBI-10171902, EBI-10699187;
CC P56545-3; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-10171902, EBI-11750983;
CC P56545-3; O94818-2: NOL4; NbExp=3; IntAct=EBI-10171902, EBI-10190763;
CC P56545-3; Q96MY1: NOL4L; NbExp=3; IntAct=EBI-10171902, EBI-6660790;
CC P56545-3; Q9NQ66: PLCB1; NbExp=3; IntAct=EBI-10171902, EBI-3396023;
CC P56545-3; P47897: QARS1; NbExp=3; IntAct=EBI-10171902, EBI-347462;
CC P56545-3; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-10171902, EBI-746228;
CC P56545-3; Q8NC74: RBBP8NL; NbExp=3; IntAct=EBI-10171902, EBI-11322432;
CC P56545-3; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-10171902, EBI-10182375;
CC P56545-3; Q8IUD6: RNF135; NbExp=3; IntAct=EBI-10171902, EBI-9916363;
CC P56545-3; O00560: SDCBP; NbExp=3; IntAct=EBI-10171902, EBI-727004;
CC P56545-3; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-10171902, EBI-12037847;
CC P56545-3; Q9UN79: SOX13; NbExp=3; IntAct=EBI-10171902, EBI-3928516;
CC P56545-3; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10171902, EBI-11741437;
CC P56545-3; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-10171902, EBI-11059915;
CC P56545-3; Q63HK5: TSHZ3; NbExp=6; IntAct=EBI-10171902, EBI-9053916;
CC P56545-3; Q9H8Y1: VRTN; NbExp=5; IntAct=EBI-10171902, EBI-12894399;
CC P56545-3; Q99592: ZBTB18; NbExp=6; IntAct=EBI-10171902, EBI-3232046;
CC P56545-3; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-10171902, EBI-12287587;
CC P56545-3; Q8NAM6: ZSCAN4; NbExp=3; IntAct=EBI-10171902, EBI-7252920;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P56545-1; Sequence=Displayed;
CC Name=2; Synonyms=Ribeye;
CC IsoId=P56545-2; Sequence=VSP_027615;
CC Name=3;
CC IsoId=P56545-3; Sequence=VSP_058946;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in heart, skeletal
CC muscle, and pancreas.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF016507; AAC39603.1; -; mRNA.
DR EMBL; AF222711; AAG45951.1; -; mRNA.
DR EMBL; BT007012; AAP35658.1; -; mRNA.
DR EMBL; AK290390; BAF83079.1; -; mRNA.
DR EMBL; AL833398; CAH10590.1; -; mRNA.
DR EMBL; AL596261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49247.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49250.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49249.1; -; Genomic_DNA.
DR EMBL; BC002486; AAH02486.1; -; mRNA.
DR EMBL; BC037900; AAH37900.1; -; mRNA.
DR EMBL; BC047018; AAH47018.1; -; mRNA.
DR EMBL; BC052276; AAH52276.1; -; mRNA.
DR EMBL; BC072020; AAH72020.1; -; mRNA.
DR CCDS; CCDS7643.1; -. [P56545-1]
DR CCDS; CCDS7644.1; -. [P56545-2]
DR CCDS; CCDS86154.1; -. [P56545-3]
DR RefSeq; NP_001077383.1; NM_001083914.2. [P56545-1]
DR RefSeq; NP_001277143.1; NM_001290214.2. [P56545-1]
DR RefSeq; NP_001277144.1; NM_001290215.2. [P56545-1]
DR RefSeq; NP_001307941.1; NM_001321012.1. [P56545-1]
DR RefSeq; NP_001307942.1; NM_001321013.1. [P56545-1]
DR RefSeq; NP_001307943.1; NM_001321014.1. [P56545-1]
DR RefSeq; NP_001320.1; NM_001329.3. [P56545-1]
DR RefSeq; NP_073713.2; NM_022802.2. [P56545-2]
DR RefSeq; XP_005269618.1; XM_005269561.2. [P56545-1]
DR RefSeq; XP_005269621.1; XM_005269564.2. [P56545-1]
DR RefSeq; XP_005269624.1; XM_005269567.2. [P56545-1]
DR RefSeq; XP_005269625.1; XM_005269568.4. [P56545-1]
DR RefSeq; XP_005269626.1; XM_005269569.2. [P56545-1]
DR RefSeq; XP_005269628.1; XM_005269571.2. [P56545-1]
DR RefSeq; XP_005269629.1; XM_005269572.3. [P56545-1]
DR RefSeq; XP_006717705.1; XM_006717642.2. [P56545-1]
DR RefSeq; XP_011537651.1; XM_011539349.2.
DR RefSeq; XP_011537653.1; XM_011539351.1. [P56545-1]
DR RefSeq; XP_011537655.1; XM_011539353.1. [P56545-1]
DR RefSeq; XP_011537656.1; XM_011539354.1. [P56545-1]
DR RefSeq; XP_011537657.1; XM_011539355.1. [P56545-1]
DR RefSeq; XP_016871245.1; XM_017015756.1. [P56545-1]
DR RefSeq; XP_016871246.1; XM_017015757.1. [P56545-1]
DR PDB; 2OME; X-ray; 2.80 A; A/B/C/D/E/F/G/H=31-364.
DR PDB; 4LCJ; X-ray; 2.86 A; A/B/C/D/E/F/G/H=31-362.
DR PDB; 6WKW; EM; 3.60 A; A/B/C/D=33-362.
DR PDBsum; 2OME; -.
DR PDBsum; 4LCJ; -.
DR PDBsum; 6WKW; -.
DR AlphaFoldDB; P56545; -.
DR SMR; P56545; -.
DR BioGRID; 107870; 327.
DR CORUM; P56545; -.
DR DIP; DIP-42104N; -.
DR IntAct; P56545; 131.
DR MINT; P56545; -.
DR STRING; 9606.ENSP00000311825; -.
DR BindingDB; P56545; -.
DR ChEMBL; CHEMBL3797016; -.
DR GlyGen; P56545; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56545; -.
DR PhosphoSitePlus; P56545; -.
DR BioMuta; CTBP2; -.
DR DMDM; 3182976; -.
DR EPD; P56545; -.
DR jPOST; P56545; -.
DR MassIVE; P56545; -.
DR MaxQB; P56545; -.
DR PaxDb; P56545; -.
DR PeptideAtlas; P56545; -.
DR PRIDE; P56545; -.
DR ProteomicsDB; 56923; -. [P56545-1]
DR ProteomicsDB; 56924; -. [P56545-2]
DR Antibodypedia; 19137; 393 antibodies from 37 providers.
DR DNASU; 1488; -.
DR Ensembl; ENST00000309035.11; ENSP00000311825.6; ENSG00000175029.17. [P56545-2]
DR Ensembl; ENST00000334808.10; ENSP00000357816.5; ENSG00000175029.17. [P56545-3]
DR Ensembl; ENST00000337195.9; ENSP00000338615.5; ENSG00000175029.17. [P56545-1]
DR Ensembl; ENST00000411419.6; ENSP00000410474.2; ENSG00000175029.17. [P56545-1]
DR Ensembl; ENST00000494626.6; ENSP00000436285.1; ENSG00000175029.17. [P56545-1]
DR Ensembl; ENST00000531469.5; ENSP00000434630.1; ENSG00000175029.17. [P56545-1]
DR GeneID; 1488; -.
DR KEGG; hsa:1488; -.
DR MANE-Select; ENST00000309035.11; ENSP00000311825.6; NM_022802.3; NP_073713.2. [P56545-2]
DR UCSC; uc001lie.5; human. [P56545-1]
DR CTD; 1488; -.
DR DisGeNET; 1488; -.
DR GeneCards; CTBP2; -.
DR HGNC; HGNC:2495; CTBP2.
DR HPA; ENSG00000175029; Low tissue specificity.
DR MIM; 602619; gene.
DR neXtProt; NX_P56545; -.
DR OpenTargets; ENSG00000175029; -.
DR PharmGKB; PA26996; -.
DR VEuPathDB; HostDB:ENSG00000175029; -.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000154430; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR InParanoid; P56545; -.
DR OMA; TCHTAFY; -.
DR OrthoDB; 700058at2759; -.
DR PhylomeDB; P56545; -.
DR TreeFam; TF313593; -.
DR PathwayCommons; P56545; -.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR Reactome; R-HSA-5339700; Signaling by TCF7L2 mutants.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. [P56545-2]
DR SignaLink; P56545; -.
DR SIGNOR; P56545; -.
DR BioGRID-ORCS; 1488; 128 hits in 1073 CRISPR screens.
DR ChiTaRS; CTBP2; human.
DR EvolutionaryTrace; P56545; -.
DR GeneWiki; CTBP2; -.
DR GenomeRNAi; 1488; -.
DR Pharos; P56545; Tchem.
DR PRO; PR:P56545; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P56545; protein.
DR Bgee; ENSG00000175029; Expressed in pancreatic ductal cell and 207 other tissues.
DR ExpressionAtlas; P56545; baseline and differential.
DR Genevisible; P56545; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IEA:Ensembl.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:CAFA.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ARUK-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IEA:Ensembl.
DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation;
KW Direct protein sequencing; Host-virus interaction; Methylation; NAD;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Synapse; Transcription; Transcription regulation.
FT CHAIN 1..445
FT /note="C-terminal-binding protein 2"
FT /id="PRO_0000076044"
FT REGION 414..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT BINDING 243..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT BINDING 270..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT BINDING 321..324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.20"
FT MOD_RES 22
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..20
FT /note="MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWDAAGWYEGPWEN
FT AESLRPLGRRSSLTYGTAEGTWFEPNHRPQDAALPVAAEPYLYREAVYNSVAARKGSTP
FT DFTFYDSRQAVMSGRSPLLPREYYSDPSGAARVPKEPPLYRDPGVSRPVPSYGVLGSRT
FT SWDPMQGRSPALQDAGHLYRDPGGKMIPQGRQTQSRAASPGRYGREQPDTRYGAEVPAY
FT PLSQVFSDISERPIDPAPARQVAPTCLVVDPSSAAAPEGSTGVAPGALNRGYGPARESI
FT PSKMAYETYEADLSTFQGPGGKRTVLPEFLAFLRAEGLAEATLGALLQQGFDSPAVLAT
FT LEDADIKSVAPNLGQARVLSRLANSCRTEMQLRRQDRGGPLPRARSSSFSHRSELLHGD
FT LASLGAAAPLQTASPRAGDPARRPSSAPSQHLLETAATYSAPGVGTHAPHFPSNSGYSS
FT PTPCALTARLSPTYPLQAGVALTNPGPSNPLHPGPRTAYSTAYTVPMELLKRERNVAAS
FT PLPSPHGSPQVLRKPGAPLGPSTLPPASQSLHTPHSPYQKVARRTGAPIIVSTMLAPEP
FT S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11163272"
FT /id="VSP_027615"
FT VAR_SEQ 1..19
FT /note="MALVDKHKVKRQRLDRICE -> MRPGLPGPTGLCAQTSSRGQKSVLKQKES
FT CGIWQLYHFLSRKQEPRWEPCVSGSSSGDGAVADLADELRGYPALCCTLPVHSYRSWA
FT (in isoform 3)"
FT /id="VSP_058946"
FT CONFLICT 87
FT /note="L -> F (in Ref. 2; AAG45951)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="T -> N (in Ref. 2; AAG45951)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> N (in Ref. 2; AAG45951)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="G -> R (in Ref. 9; AAH37900)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> T (in Ref. 9; AAH47018)"
FT /evidence="ECO:0000305"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:2OME"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:2OME"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2OME"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:2OME"
FT HELIX 327..346
FT /evidence="ECO:0007829|PDB:2OME"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:2OME"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2OME"
FT CONFLICT P56545-2:455
FT /note="Y -> H (in Ref. 2; AAG45951)"
FT /evidence="ECO:0000305"
FT CONFLICT P56545-2:539
FT /note="Q -> E (in Ref. 2; AAG45951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 48945 MW; 0A8C21CEB36807FA CRC64;
MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC
DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG
IAVCNIPSAA VEETADSTIC HILNLYRRNT WLYQALREGT RVQSVEQIRE VASGAARIRG
ETLGLIGFGR TGQAVAVRAK AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS
LHCNLNEHNH HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES
EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP ESLRNCVNKE
FFVTSAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP AAMEGIIPGG IPVTHNLPTV
AHPSQAPSPN QPTKHGDNRE HPNEQ
