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; Q9H2T8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   29-SEP-2021, entry version 207.
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=3; 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; 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}. Cell junction, synapse
CC       {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   SMR; P56545; -.
DR   BioGRID; 107870; 300.
DR   CORUM; P56545; -.
DR   DIP; DIP-42104N; -.
DR   IntAct; P56545; 125.
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; 377 antibodies.
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   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; INGGYYA; -.
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; 122 hits in 1015 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 thoracic mammary gland and 250 other tissues.
DR   ExpressionAtlas; P56545; baseline and differential.
DR   Genevisible; P56545; HS.
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:0042802; F:identical protein binding; IPI:IntAct.
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; TAS:ARUK-UCL.
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: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; Cell junction; 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   NP_BIND         186..191
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|Ref.20"
FT   NP_BIND         243..249
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|Ref.20"
FT   NP_BIND         270..272
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|Ref.20"
FT   NP_BIND         321..324
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|Ref.20"
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                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /note="NAD"
FT                   /evidence="ECO:0000269|Ref.20"
FT   BINDING         296
FT                   /note="NAD"
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
//
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