GenomeNet

Database: UniProt
Entry: P56545
LinkDB: P56545
Original site: P56545 
ID   CTBP2_HUMAN             Reviewed;         445 AA.
AC   P56545; A8K2X5; D3DRF5; O43449; Q5SQP7; Q69YI3; Q86SV0; Q8IY44;
AC   Q9H2T8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   13-FEB-2019, entry version 190.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   CTBP1, an adenovirus E1A-binding protein, and maps to human chromosome
RT   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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   that interacts with a conserved C-terminal domain of adenovirus E1A
RT   involved in 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.,
RA   Hunt M.E., Sugrue S.P.;
RT   "Nuclear speckle-associated protein Pnn/DRS binds to the
RT   transcriptional corepressor CtBP and relieves CtBP-mediated repression
RT   of the E-cadherin 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.,
RA   Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
RT   "Multiple domains of the receptor-interacting protein 140 contribute
RT   to 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
RT   the 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.,
RA   Buerckstuemmer T., 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
RT   productive infection.";
RL   Virology 443:313-320(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
RP   BY 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., 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
RT   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
RT   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
CC       white adipose tissue (WAT)-specific genes expression (By
CC       similarity). Interacts with PNN, NRIP1 and WIZ. Interacts with
CC       MCRIP1 (PubMed:25728771). {ECO:0000250,
CC       ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15542832,
CC       ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:25728771,
CC       ECO:0000269|Ref.20}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5
CC       E1A protein; this interaction seems to potentiate viral
CC       replication. {ECO:0000269|PubMed:23747199}.
CC   -!- INTERACTION:
CC       Q9UIF8-2:BAZ2B; NbExp=3; IntAct=EBI-10171902, EBI-10321972;
CC       Q9H6U6:BCAS3; NbExp=3; IntAct=EBI-10171902, EBI-6083685;
CC       P20749:BCL3; NbExp=2; IntAct=EBI-741533, EBI-958997;
CC       P54284:CACNB3; NbExp=4; IntAct=EBI-10171902, EBI-1184651;
CC       P51946:CCNH; NbExp=5; IntAct=EBI-741533, EBI-741406;
CC       Q13363-2:CTBP1; NbExp=3; IntAct=EBI-741533, EBI-10171858;
CC       A0A0S2Z5I3:DMRTB1; NbExp=3; IntAct=EBI-741533, EBI-16431245;
CC       I6L9A0:DMRTB1; NbExp=3; IntAct=EBI-10171902, EBI-10178554;
CC       Q01543:FLI1; NbExp=3; IntAct=EBI-10171902, EBI-2271018;
CC       O15409:FOXP2; NbExp=3; IntAct=EBI-741533, EBI-983612;
CC       Q8IVP5:FUNDC1; NbExp=3; IntAct=EBI-741533, EBI-3059266;
CC       Q14526:HIC1; NbExp=2; IntAct=EBI-741533, EBI-2507362;
CC       P09067:HOXB5; NbExp=5; IntAct=EBI-10171902, EBI-3893317;
CC       Q13422:IKZF1; NbExp=5; IntAct=EBI-741533, EBI-745305;
CC       Q9UKS7:IKZF2; NbExp=3; IntAct=EBI-741533, EBI-3893057;
CC       Q96JN0:LCOR; NbExp=4; IntAct=EBI-741533, EBI-746045;
CC       O94818-2:NOL4; NbExp=3; IntAct=EBI-10171902, EBI-10190763;
CC       Q96MY1:NOL4L; NbExp=3; IntAct=EBI-10171902, EBI-6660790;
CC       Q9NQ66:PLCB1; NbExp=3; IntAct=EBI-10171902, EBI-3396023;
CC       O75807:PPP1R15A; NbExp=2; IntAct=EBI-741533, EBI-714746;
CC       Q92786:PROX1; NbExp=2; IntAct=EBI-741533, EBI-3912635;
CC       Q9Y5P3:RAI2; NbExp=4; IntAct=EBI-741533, EBI-746228;
CC       Q9UFD9:RIMBP3; NbExp=3; IntAct=EBI-10171902, EBI-10182375;
CC       Q9UN79:SOX13; NbExp=2; IntAct=EBI-741533, EBI-3928516;
CC       Q15583:TGIF1; NbExp=5; IntAct=EBI-741533, EBI-714215;
CC       Q15583-2:TGIF1; NbExp=3; IntAct=EBI-741533, EBI-12691451;
CC       Q63HK5:TSHZ3; NbExp=5; IntAct=EBI-10171902, EBI-9053916;
CC       A2APF7:Zbp1 (xeno); NbExp=2; IntAct=EBI-741533, EBI-6115394;
CC       Q99592:ZBTB18; NbExp=5; IntAct=EBI-10171902, EBI-3232046;
CC       B2RXF5:ZBTB42; NbExp=4; IntAct=EBI-10171902, EBI-12287587;
CC       Q32MQ0:ZNF750; NbExp=3; IntAct=EBI-741533, EBI-10240029;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction,
CC       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         Note=Ref.2 (AAG45951) sequence is in conflict in position:
CC         455:Y->H. Ref.2 (AAG45951) sequence is in conflict in position:
CC         539:Q->E. {ECO:0000305};
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}.
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_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   UniGene; Hs.501345; -.
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   PDBsum; 2OME; -.
DR   PDBsum; 4LCJ; -.
DR   ProteinModelPortal; P56545; -.
DR   SMR; P56545; -.
DR   BioGrid; 107870; 118.
DR   CORUM; P56545; -.
DR   DIP; DIP-42104N; -.
DR   IntAct; P56545; 109.
DR   MINT; P56545; -.
DR   STRING; 9606.ENSP00000311825; -.
DR   BindingDB; P56545; -.
DR   ChEMBL; CHEMBL3797016; -.
DR   iPTMnet; P56545; -.
DR   PhosphoSitePlus; P56545; -.
DR   BioMuta; CTBP2; -.
DR   DMDM; 3182976; -.
DR   EPD; P56545; -.
DR   jPOST; P56545; -.
DR   MaxQB; P56545; -.
DR   PaxDb; P56545; -.
DR   PeptideAtlas; P56545; -.
DR   PRIDE; P56545; -.
DR   ProteomicsDB; 56923; -.
DR   ProteomicsDB; 56924; -. [P56545-2]
DR   DNASU; 1488; -.
DR   Ensembl; ENST00000309035; ENSP00000311825; ENSG00000175029. [P56545-2]
DR   Ensembl; ENST00000334808; ENSP00000357816; ENSG00000175029. [P56545-3]
DR   Ensembl; ENST00000337195; ENSP00000338615; ENSG00000175029. [P56545-1]
DR   Ensembl; ENST00000411419; ENSP00000410474; ENSG00000175029. [P56545-1]
DR   Ensembl; ENST00000494626; ENSP00000436285; ENSG00000175029. [P56545-1]
DR   Ensembl; ENST00000531469; ENSP00000434630; ENSG00000175029. [P56545-1]
DR   GeneID; 1488; -.
DR   KEGG; hsa:1488; -.
DR   UCSC; uc001lie.5; human. [P56545-1]
DR   CTD; 1488; -.
DR   DisGeNET; 1488; -.
DR   EuPathDB; HostDB:ENSG00000175029.16; -.
DR   GeneCards; CTBP2; -.
DR   HGNC; HGNC:2495; CTBP2.
DR   HPA; CAB031916; -.
DR   HPA; CAB079018; -.
DR   HPA; HPA023559; -.
DR   HPA; HPA023564; -.
DR   HPA; HPA044971; -.
DR   MIM; 602619; gene.
DR   neXtProt; NX_P56545; -.
DR   OpenTargets; ENSG00000175029; -.
DR   PharmGKB; PA26996; -.
DR   eggNOG; KOG0067; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000154430; -.
DR   HOVERGEN; HBG001898; -.
DR   InParanoid; P56545; -.
DR   KO; K04496; -.
DR   OMA; EYTIKQM; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; P56545; -.
DR   TreeFam; TF313593; -.
DR   Reactome; R-HSA-4641265; Repression of WNT target genes.
DR   Reactome; R-HSA-5339700; TCF7L2 mutants don't bind CTBP.
DR   SignaLink; P56545; -.
DR   SIGNOR; P56545; -.
DR   ChiTaRS; CTBP2; human.
DR   EvolutionaryTrace; P56545; -.
DR   GeneWiki; CTBP2; -.
DR   GenomeRNAi; 1488; -.
DR   PRO; PR:P56545; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000175029; Expressed in 238 organ(s), highest expression level in thoracic mammary gland.
DR   ExpressionAtlas; P56545; baseline and differential.
DR   Genevisible; P56545; HS.
DR   GO; GO:0030054; C:cell 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:transcriptional repressor complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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:0042974; F:retinoic acid receptor binding; IEA:Ensembl.
DR   GO; GO:0098882; F:structural constituent of presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
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: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: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   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; Cell junction; Complete proteome;
KW   Differentiation; Direct protein sequencing; Host-virus interaction;
KW   Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Repressor; Synapse; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    445       C-terminal-binding protein 2.
FT                                /FTId=PRO_0000076044.
FT   NP_BIND     186    191       NAD. {ECO:0000269|Ref.20}.
FT   NP_BIND     243    249       NAD. {ECO:0000269|Ref.20}.
FT   NP_BIND     270    272       NAD. {ECO:0000269|Ref.20}.
FT   NP_BIND     321    324       NAD. {ECO:0000269|Ref.20}.
FT   ACT_SITE    272    272       {ECO:0000250}.
FT   ACT_SITE    301    301       {ECO:0000250}.
FT   ACT_SITE    321    321       Proton donor. {ECO:0000250}.
FT   BINDING     106    106       NAD. {ECO:0000250}.
FT   BINDING     210    210       NAD. {ECO:0000269|Ref.20}.
FT   BINDING     296    296       NAD. {ECO:0000269|Ref.20}.
FT   MOD_RES      22     22       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     428    428       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ       1     20       MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWD
FT                                AAGWYEGPWENAESLRPLGRRSSLTYGTAEGTWFEPNHRPQ
FT                                DAALPVAAEPYLYREAVYNSVAARKGSTPDFTFYDSRQAVM
FT                                SGRSPLLPREYYSDPSGAARVPKEPPLYRDPGVSRPVPSYG
FT                                VLGSRTSWDPMQGRSPALQDAGHLYRDPGGKMIPQGRQTQS
FT                                RAASPGRYGREQPDTRYGAEVPAYPLSQVFSDISERPIDPA
FT                                PARQVAPTCLVVDPSSAAAPEGSTGVAPGALNRGYGPARES
FT                                IPSKMAYETYEADLSTFQGPGGKRTVLPEFLAFLRAEGLAE
FT                                ATLGALLQQGFDSPAVLATLEDADIKSVAPNLGQARVLSRL
FT                                ANSCRTEMQLRRQDRGGPLPRARSSSFSHRSELLHGDLASL
FT                                GAAAPLQTASPRAGDPARRPSSAPSQHLLETAATYSAPGVG
FT                                THAPHFPSNSGYSSPTPCALTARLSPTYPLQAGVALTNPGP
FT                                SNPLHPGPRTAYSTAYTVPMELLKRERNVAASPLPSPHGSP
FT                                QVLRKPGAPLGPSTLPPASQSLHTPHSPYQKVARRTGAPII
FT                                VSTMLAPEPS (in isoform 2).
FT                                {ECO:0000303|PubMed:11163272}.
FT                                /FTId=VSP_027615.
FT   VAR_SEQ       1     19       MALVDKHKVKRQRLDRICE -> MRPGLPGPTGLCAQTSSR
FT                                GQKSVLKQKESCGIWQLYHFLSRKQEPRWEPCVSGSSSGDG
FT                                AVADLADELRGYPALCCTLPVHSYRSWA (in isoform
FT                                3).
FT                                /FTId=VSP_058946.
FT   CONFLICT     87     87       L -> F (in Ref. 2; AAG45951).
FT                                {ECO:0000305}.
FT   CONFLICT     88     88       T -> N (in Ref. 2; AAG45951).
FT                                {ECO:0000305}.
FT   CONFLICT    112    112       D -> N (in Ref. 2; AAG45951).
FT                                {ECO:0000305}.
FT   CONFLICT    292    292       G -> R (in Ref. 9; AAH37900).
FT                                {ECO:0000305}.
FT   CONFLICT    411    411       I -> T (in Ref. 9; AAH47018).
FT                                {ECO:0000305}.
FT   STRAND       35     38       {ECO:0000244|PDB:2OME}.
FT   HELIX        47     51       {ECO:0000244|PDB:2OME}.
FT   TURN         52     54       {ECO:0000244|PDB:2OME}.
FT   STRAND       56     59       {ECO:0000244|PDB:2OME}.
FT   HELIX        65     67       {ECO:0000244|PDB:2OME}.
FT   HELIX        70     75       {ECO:0000244|PDB:2OME}.
FT   STRAND       76     81       {ECO:0000244|PDB:2OME}.
FT   STRAND       83     85       {ECO:0000244|PDB:2OME}.
FT   HELIX        89     93       {ECO:0000244|PDB:2OME}.
FT   STRAND      100    106       {ECO:0000244|PDB:2OME}.
FT   HELIX       113    118       {ECO:0000244|PDB:2OME}.
FT   STRAND      122    124       {ECO:0000244|PDB:2OME}.
FT   STRAND      128    130       {ECO:0000244|PDB:2OME}.
FT   HELIX       131    147       {ECO:0000244|PDB:2OME}.
FT   HELIX       149    157       {ECO:0000244|PDB:2OME}.
FT   HELIX       165    171       {ECO:0000244|PDB:2OME}.
FT   TURN        172    174       {ECO:0000244|PDB:2OME}.
FT   STRAND      182    186       {ECO:0000244|PDB:2OME}.
FT   HELIX       190    199       {ECO:0000244|PDB:2OME}.
FT   HELIX       200    202       {ECO:0000244|PDB:2OME}.
FT   STRAND      205    209       {ECO:0000244|PDB:2OME}.
FT   HELIX       217    220       {ECO:0000244|PDB:2OME}.
FT   HELIX       229    235       {ECO:0000244|PDB:2OME}.
FT   STRAND      237    241       {ECO:0000244|PDB:2OME}.
FT   HELIX       255    258       {ECO:0000244|PDB:2OME}.
FT   STRAND      265    269       {ECO:0000244|PDB:2OME}.
FT   HELIX       273    275       {ECO:0000244|PDB:2OME}.
FT   HELIX       278    286       {ECO:0000244|PDB:2OME}.
FT   STRAND      289    296       {ECO:0000244|PDB:2OME}.
FT   STRAND      299    302       {ECO:0000244|PDB:2OME}.
FT   TURN        309    312       {ECO:0000244|PDB:2OME}.
FT   STRAND      314    318       {ECO:0000244|PDB:2OME}.
FT   HELIX       327    346       {ECO:0000244|PDB:2OME}.
FT   TURN        349    352       {ECO:0000244|PDB:2OME}.
FT   STRAND      354    356       {ECO:0000244|PDB:2OME}.
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
//
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