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Database: UniProt
Entry: Q13363
LinkDB: Q13363
Original site: Q13363 
ID   CTBP1_HUMAN             Reviewed;         440 AA.
AC   Q13363; Q4W5N3; Q7Z2Q5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   29-SEP-2021, entry version 226.
DE   RecName: Full=C-terminal-binding protein 1;
DE            Short=CtBP1;
DE            EC=1.1.1.-;
GN   Name=CTBP1; Synonyms=CTBP;
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), PROTEIN SEQUENCE OF 98-108, AND
RP   INTERACTION WITH RBBP8 AND ADENOVIRUS E1A.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, AND FUNCTION.
RX   PubMed=9858600; DOI=10.1128/mcb.19.1.777;
RA   Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E., Otte A.P.;
RT   "C-terminal binding protein is a transcriptional repressor that interacts
RT   with a specific class of vertebrate polycomb proteins.";
RL   Mol. Cell. Biol. 19:777-787(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Lung;
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   [6]
RP   PROTEIN SEQUENCE OF 410-415, INTERACTION WITH SIMC1, PROTEOLYTIC CLEAVAGE
RP   SITES, AND MUTAGENESIS OF ALA-52; VAL-66; GLY-183; GLY-186 AND ASP-204.
RX   PubMed=23707407; DOI=10.1016/j.jmb.2013.05.009;
RA   Ono Y., Iemura S., Novak S.M., Doi N., Kitamura F., Natsume T.,
RA   Gregorio C.C., Sorimachi H.;
RT   "PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-
RT   specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.";
RL   J. Mol. Biol. 425:2955-2972(2013).
RN   [7]
RP   INTERACTION WITH ADENOVIRUS E1A (MICROBIAL INFECTION), AND PHOSPHORYLATION.
RX   PubMed=8440238; DOI=10.1002/j.1460-2075.1993.tb05679.x;
RA   Boyd J.M., Subramanian T., Schaeper U., la Regina M., Bayley S.,
RA   Chinnadurai G.;
RT   "A region in the C-terminus of adenovirus 2/5 E1a protein is required for
RT   association with a cellular phosphoprotein and important for the negative
RT   modulation of T24-ras mediated transformation, tumorigenesis and
RT   metastasis.";
RL   EMBO J. 12:469-478(1993).
RN   [8]
RP   INTERACTION WITH MECOM.
RX   PubMed=11568182; DOI=10.1074/jbc.m106733200;
RA   Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT   "Interaction of EVI1 with cAMP-responsive element-binding protein-binding
RT   protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible
RT   acetylation of EVI1 and in co-localization in nuclear speckles.";
RL   J. Biol. Chem. 276:44936-44943(2001).
RN   [9]
RP   INTERACTION WITH EPSTEIN-BARR VIRUS/EBV PROTEIN EBNA6 (MICROBIAL
RP   INFECTION).
RX   PubMed=11462050; DOI=10.1128/jvi.75.16.7749-7755.2001;
RA   Touitou R., Hickabottom M., Parker G., Crook T., Allday M.J.;
RT   "Physical and functional interactions between the corepressor CtBP and the
RT   Epstein-Barr virus nuclear antigen EBNA3C.";
RL   J. Virol. 75:7749-7755(2001).
RN   [10]
RP   INTERACTION WITH NRIP1.
RX   PubMed=11509661; DOI=10.1128/mcb.21.18.6181-6188.2001;
RA   Vo N., Fjeld C., Goodman R.H.;
RT   "Acetylation of nuclear hormone receptor-interacting protein RIP140
RT   regulates binding of the transcriptional corepressor CtBP.";
RL   Mol. Cell. Biol. 21:6181-6188(2001).
RN   [11]
RP   INTERACTION WITH EPSTEIN-BARR VIRUS/EBV PROTEIN EBNA3 (MICROBIAL
RP   INFECTION).
RX   PubMed=12372828; DOI=10.1074/jbc.m208116200;
RA   Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.;
RT   "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A
RT   cooperate to bind the co-repressor carboxyl-terminal-binding protein
RT   (CtBP).";
RL   J. Biol. Chem. 277:47197-47204(2002).
RN   [12]
RP   SUMOYLATION AT LYS-428, AND SUBCELLULAR LOCATION.
RX   PubMed=12679040; DOI=10.1016/s0092-8674(03)00159-4;
RA   Kagey M.H., Melhuish T.A., Wotton D.;
RT   "The polycomb protein Pc2 is a SUMO E3.";
RL   Cell 113:127-137(2003).
RN   [13]
RP   INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-422, AND MUTAGENESIS OF
RP   SER-422.
RX   PubMed=14567915; DOI=10.1016/s0092-8674(03)00802-x;
RA   Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
RT   "Homeodomain interacting protein kinase 2 promotes apoptosis by
RT   downregulating the transcriptional corepressor CtBP.";
RL   Cell 115:177-186(2003).
RN   [14]
RP   FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND 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   [15]
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   [16]
RP   INTERACTION WITH ZFHX1B.
RX   PubMed=16061479; DOI=10.1074/jbc.m504477200;
RA   Long J., Zuo D., Park M.;
RT   "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT   transcriptional repression of E-cadherin.";
RL   J. Biol. Chem. 280:35477-35489(2005).
RN   [17]
RP   INTERACTION WITH MECOM.
RX   PubMed=15897867; DOI=10.1038/sj.onc.1208754;
RA   Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S.,
RA   Kurokawa M., Hirai H.;
RT   "Oligomerization of Evi-1 regulated by the PR domain contributes to
RT   recruitment of corepressor CtBP.";
RL   Oncogene 24:6165-6173(2005).
RN   [18]
RP   INTERACTION WITH FOXP1.
RX   PubMed=16609867; DOI=10.1007/s00427-006-0073-8;
RA   Schoen C., Wochnik A., Roessner A., Donow C., Knoechel W.;
RT   "The FoxP subclass in Xenopus laevis development.";
RL   Dev. Genes Evol. 216:641-646(2006).
RN   [19]
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   [20]
RP   INTERACTION WITH ZNF366.
RX   PubMed=16393996; DOI=10.4049/jimmunol.176.2.1081;
RA   Triantis V., Trancikova D.E., Looman M.W., Hartgers F.C., Janssen R.A.,
RA   Adema G.J.;
RT   "Identification and characterization of DC-SCRIPT, a novel dendritic cell-
RT   expressed member of the zinc finger family of transcriptional regulators.";
RL   J. Immunol. 176:1081-1089(2006).
RN   [21]
RP   INTERACTION WITH ZNF366.
RX   PubMed=17085477; DOI=10.1093/nar/gkl875;
RA   Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P.,
RA   Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.;
RT   "ZNF366 is an estrogen receptor corepressor that acts through CtBP and
RT   histone deacetylases.";
RL   Nucleic Acids Res. 34:6126-6136(2006).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [23]
RP   FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, AND TISSUE SPECIFICITY.
RX   PubMed=18212045; DOI=10.1128/mcb.01400-07;
RA   Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
RA   Ye B.H.;
RT   "CtBP is an essential corepressor for BCL6 autoregulation.";
RL   Mol. Cell. Biol. 28:2175-2186(2008).
RN   [24]
RP   FUNCTION, AND INTERACTION WITH SATB1.
RX   PubMed=19103759; DOI=10.1128/mcb.00822-08;
RA   Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT   "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT   transcriptional repression by SATB1.";
RL   Mol. Cell. Biol. 29:1321-1337(2009).
RN   [25]
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   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [27]
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   [28]
RP   IDENTIFICATION 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., 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   [29]
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   [30]
RP   INVOLVEMENT IN HADDTS, AND VARIANT HADDTS TRP-342.
RX   PubMed=27094857; DOI=10.1007/s10048-016-0482-4;
RA   Beck D.B., Cho M.T., Millan F., Yates C., Hannibal M., O'Connor B.,
RA   Shinawi M., Connolly A.M., Waggoner D., Halbach S., Angle B., Sanders V.,
RA   Shen Y., Retterer K., Begtrup A., Bai R., Chung W.K.;
RT   "A recurrent de novo CTBP1 mutation is associated with developmental delay,
RT   hypotonia, ataxia, and tooth enamel defects.";
RL   Neurogenetics 17:173-178(2016).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-353 IN COMPLEX WITH NAD,
RP   FUNCTION, COFACTOR, MUTAGENESIS OF CYS-134; ASN-138; ARG-141;
RP   141-ARG-ARG-142; LEU-150; ARG-163; ARG-171; GLY-181; GLY-183; ASP-204;
RP   ARG-266; ASP-290; GLU-295 AND HIS-315, AND DIMERIZATION.
RX   PubMed=12419229; DOI=10.1016/s1097-2765(02)00650-0;
RA   Kumar V., Carlson J.E., Ohgi K.A., Edwards T.A., Rose D.W., Escalante C.R.,
RA   Rosenfeld M.G., Aggarwal A.K.;
RT   "Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase.";
RL   Mol. Cell 10:857-869(2002).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators such
CC       as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling
CC       the equilibrium between tubular and stacked structures in the Golgi
CC       complex. Functions in brown adipose tissue (BAT) differentiation.
CC       {ECO:0000269|PubMed:12419229, ECO:0000269|PubMed:15542832,
CC       ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19103759,
CC       ECO:0000269|PubMed:9858600}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:12419229};
CC       Note=NAD is required for efficient interaction with E1A. Cofactor
CC       binding induces a conformation change. {ECO:0000269|PubMed:12419229};
CC   -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts with
CC       PRDM16; the interaction represses white adipose tissue (WAT)-specific
CC       genes expression. Interacts with GLIS2, FOXP2, HDAC4, HDAC5, HDAC9 and
CC       ZNF217. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8
CC       (via its PXDLS motif); the interaction is disrupted by binding to
CC       adenovirus E1A. Interacts with FOXP1, HIPK2, PNN, NRIP1, MECOM, ZFHX1B
CC       and WIZ. Interacts with ZNF366 (via PXDLS motif) (PubMed:16393996,
CC       PubMed:17085477). Interaction with SATB1 (non-acetylated form); the
CC       interaction stabilizes its attachment to DNA and promotes transcription
CC       repression. Interacts with BCL6; the interaction is required for BCL6
CC       transcriptional autoinhibition and inhibition of some BCL6 target
CC       genes. Interacts with IKZF4 (By similarity). Interacts with MCRIP1
CC       (unphosphorylated form, via the PXDLS motif); competitively inhibiting
CC       CTBP-ZEB1 interaction (PubMed:25728771). Interacts with Bassoon/BSN;
CC       this interaction targets and anchors CTBP1 to presynapses (By
CC       similarity). Interacts with SIMC1 (PubMed:23707407).
CC       {ECO:0000250|UniProtKB:O88712, ECO:0000269|PubMed:11509661,
CC       ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:12419229,
CC       ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:15060175,
CC       ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15897867,
CC       ECO:0000269|PubMed:16061479, ECO:0000269|PubMed:16393996,
CC       ECO:0000269|PubMed:16609867, ECO:0000269|PubMed:16702210,
CC       ECO:0000269|PubMed:17085477, ECO:0000269|PubMed:18212045,
CC       ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:23707407,
CC       ECO:0000269|PubMed:25728771, ECO:0000269|PubMed:7479821}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA3
CC       and EBNA6. {ECO:0000269|PubMed:11462050, ECO:0000269|PubMed:12372828}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1A protein
CC       (via its C-terminus); the interaction disrupts the interaction of CTBP1
CC       with RBBP8. {ECO:0000269|PubMed:8440238}.
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       Q13363; O00257: CBX4; NbExp=4; IntAct=EBI-908846, EBI-722425;
CC       Q13363; Q13363: CTBP1; NbExp=4; IntAct=EBI-908846, EBI-908846;
CC       Q13363; P56545: CTBP2; NbExp=3; IntAct=EBI-908846, EBI-741533;
CC       Q13363; Q9BXL5: HEMGN; NbExp=2; IntAct=EBI-908846, EBI-3916399;
CC       Q13363; Q14526: HIC1; NbExp=2; IntAct=EBI-908846, EBI-2507362;
CC       Q13363; O43474: KLF4; NbExp=4; IntAct=EBI-908846, EBI-7232405;
CC       Q13363; Q96JN0: LCOR; NbExp=3; IntAct=EBI-908846, EBI-746045;
CC       Q13363; Q8N3X6: LCORL; NbExp=3; IntAct=EBI-908846, EBI-7138654;
CC       Q13363; P48552: NRIP1; NbExp=2; IntAct=EBI-908846, EBI-746484;
CC       Q13363; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-908846, EBI-750109;
CC       Q13363; Q96EK4: THAP11; NbExp=2; IntAct=EBI-908846, EBI-1790529;
CC       Q13363; Q8N895: ZNF366; NbExp=5; IntAct=EBI-908846, EBI-2813661;
CC       Q13363; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-908846, EBI-6115394;
CC       Q13363-2; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-10171858, EBI-6083685;
CC       Q13363-2; P55273: CDKN2D; NbExp=3; IntAct=EBI-10171858, EBI-745859;
CC       Q13363-2; Q76N32: CEP68; NbExp=3; IntAct=EBI-10171858, EBI-9051024;
CC       Q13363-2; Q49AN0: CRY2; NbExp=3; IntAct=EBI-10171858, EBI-2212355;
CC       Q13363-2; Q13363-2: CTBP1; NbExp=5; IntAct=EBI-10171858, EBI-10171858;
CC       Q13363-2; P56545: CTBP2; NbExp=5; IntAct=EBI-10171858, EBI-741533;
CC       Q13363-2; P56545-3: CTBP2; NbExp=4; IntAct=EBI-10171858, EBI-10171902;
CC       Q13363-2; A0A0S2Z5I3: DMRTB1; NbExp=3; IntAct=EBI-10171858, EBI-16431245;
CC       Q13363-2; I6L9A0: DMRTB1; NbExp=3; IntAct=EBI-10171858, EBI-10178554;
CC       Q13363-2; O15409: FOXP2; NbExp=7; IntAct=EBI-10171858, EBI-983612;
CC       Q13363-2; P09067: HOXB5; NbExp=3; IntAct=EBI-10171858, EBI-3893317;
CC       Q13363-2; Q13422: IKZF1; NbExp=3; IntAct=EBI-10171858, EBI-745305;
CC       Q13363-2; Q13422-7: IKZF1; NbExp=5; IntAct=EBI-10171858, EBI-11522367;
CC       Q13363-2; Q9Y4X4: KLF12; NbExp=6; IntAct=EBI-10171858, EBI-750750;
CC       Q13363-2; P57682: KLF3; NbExp=3; IntAct=EBI-10171858, EBI-8472267;
CC       Q13363-2; P45984: MAPK9; NbExp=3; IntAct=EBI-10171858, EBI-713568;
CC       Q13363-2; O94818-2: NOL4; NbExp=4; IntAct=EBI-10171858, EBI-10190763;
CC       Q13363-2; Q96MY1: NOL4L; NbExp=3; IntAct=EBI-10171858, EBI-6660790;
CC       Q13363-2; Q9NQ66: PLCB1; NbExp=3; IntAct=EBI-10171858, EBI-3396023;
CC       Q13363-2; Q13131: PRKAA1; NbExp=3; IntAct=EBI-10171858, EBI-1181405;
CC       Q13363-2; Q15583: TGIF1; NbExp=3; IntAct=EBI-10171858, EBI-714215;
CC       Q13363-2; Q15583-2: TGIF1; NbExp=3; IntAct=EBI-10171858, EBI-12691451;
CC       Q13363-2; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-10171858, EBI-9053916;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12679040}. Nucleus
CC       {ECO:0000269|PubMed:12679040}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13363-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13363-2; Sequence=VSP_043305;
CC   -!- TISSUE SPECIFICITY: Expressed in germinal center B-cells.
CC       {ECO:0000269|PubMed:18212045}.
CC   -!- PTM: The level of phosphorylation appears to be regulated during the
CC       cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal
CC       degradation. {ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:8440238}.
CC   -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC       {ECO:0000250}.
CC   -!- PTM: Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase
CC       CBX4. {ECO:0000269|PubMed:12679040}.
CC   -!- DISEASE: Hypotonia, ataxia, developmental delay, and tooth enamel
CC       defect syndrome (HADDTS) [MIM:617915]: An autosomal dominant disorder
CC       characterized by delayed motor development, intellectual disability,
CC       failure to thrive, hypotonia, ataxia, and tooth enamel defects.
CC       {ECO:0000269|PubMed:27094857}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U37408; AAC62822.1; -; mRNA.
DR   EMBL; AF091555; AAD14597.1; -; mRNA.
DR   EMBL; AC092535; AAY40989.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82599.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82600.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82601.1; -; Genomic_DNA.
DR   EMBL; BC011655; AAH11655.1; -; mRNA.
DR   EMBL; BC053320; AAH53320.1; -; mRNA.
DR   CCDS; CCDS3348.1; -. [Q13363-1]
DR   CCDS; CCDS43203.1; -. [Q13363-2]
DR   RefSeq; NP_001012632.1; NM_001012614.1. [Q13363-2]
DR   RefSeq; NP_001319.1; NM_001328.2. [Q13363-1]
DR   RefSeq; XP_016863253.1; XM_017007764.1. [Q13363-2]
DR   RefSeq; XP_016863254.1; XM_017007765.1.
DR   RefSeq; XP_016863255.1; XM_017007766.1.
DR   RefSeq; XP_016863256.1; XM_017007767.1.
DR   PDB; 1MX3; X-ray; 1.95 A; A=28-353.
DR   PDB; 4LCE; X-ray; 2.38 A; A=28-353.
DR   PDB; 4U6Q; X-ray; 2.30 A; A=28-353.
DR   PDB; 4U6S; X-ray; 2.10 A; A=28-353.
DR   PDB; 6CDF; X-ray; 2.60 A; A=28-379.
DR   PDB; 6CDR; X-ray; 2.40 A; A=28-379.
DR   PDB; 6V89; X-ray; 2.45 A; A=28-375.
DR   PDB; 6V8A; X-ray; 2.35 A; A=28-375.
DR   PDB; 7KWM; X-ray; 2.30 A; A=28-356.
DR   PDBsum; 1MX3; -.
DR   PDBsum; 4LCE; -.
DR   PDBsum; 4U6Q; -.
DR   PDBsum; 4U6S; -.
DR   PDBsum; 6CDF; -.
DR   PDBsum; 6CDR; -.
DR   PDBsum; 6V89; -.
DR   PDBsum; 6V8A; -.
DR   PDBsum; 7KWM; -.
DR   SMR; Q13363; -.
DR   BioGRID; 107869; 250.
DR   CORUM; Q13363; -.
DR   DIP; DIP-24245N; -.
DR   ELM; Q13363; -.
DR   IntAct; Q13363; 102.
DR   MINT; Q13363; -.
DR   STRING; 9606.ENSP00000290921; -.
DR   BindingDB; Q13363; -.
DR   DrugBank; DB01942; Formic acid.
DR   iPTMnet; Q13363; -.
DR   PhosphoSitePlus; Q13363; -.
DR   SwissPalm; Q13363; -.
DR   BioMuta; CTBP1; -.
DR   DMDM; 6014741; -.
DR   EPD; Q13363; -.
DR   jPOST; Q13363; -.
DR   MassIVE; Q13363; -.
DR   PaxDb; Q13363; -.
DR   PeptideAtlas; Q13363; -.
DR   PRIDE; Q13363; -.
DR   ProteomicsDB; 59349; -. [Q13363-1]
DR   ProteomicsDB; 59350; -. [Q13363-2]
DR   Antibodypedia; 3783; 686 antibodies.
DR   DNASU; 1487; -.
DR   Ensembl; ENST00000290921; ENSP00000290921; ENSG00000159692. [Q13363-1]
DR   Ensembl; ENST00000382952; ENSP00000372411; ENSG00000159692. [Q13363-2]
DR   GeneID; 1487; -.
DR   KEGG; hsa:1487; -.
DR   UCSC; uc003gcu.2; human. [Q13363-1]
DR   CTD; 1487; -.
DR   DisGeNET; 1487; -.
DR   GeneCards; CTBP1; -.
DR   HGNC; HGNC:2494; CTBP1.
DR   HPA; ENSG00000159692; Low tissue specificity.
DR   MalaCards; CTBP1; -.
DR   MIM; 602618; gene.
DR   MIM; 617915; phenotype.
DR   neXtProt; NX_Q13363; -.
DR   OpenTargets; ENSG00000159692; -.
DR   Orphanet; 280; Wolf-Hirschhorn syndrome.
DR   PharmGKB; PA26995; -.
DR   VEuPathDB; HostDB:ENSG00000159692; -.
DR   eggNOG; KOG0067; Eukaryota.
DR   GeneTree; ENSGT00940000157061; -.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   InParanoid; Q13363; -.
DR   OMA; TCHTAFY; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; Q13363; -.
DR   TreeFam; TF313593; -.
DR   PathwayCommons; Q13363; -.
DR   Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-HSA-4641265; Repression of WNT target genes.
DR   Reactome; R-HSA-5339700; Signaling by TCF7L2 mutants.
DR   SignaLink; Q13363; -.
DR   SIGNOR; Q13363; -.
DR   BioGRID-ORCS; 1487; 21 hits in 1025 CRISPR screens.
DR   ChiTaRS; CTBP1; human.
DR   EvolutionaryTrace; Q13363; -.
DR   GeneWiki; CTBP1; -.
DR   GenomeRNAi; 1487; -.
DR   Pharos; Q13363; Tbio.
DR   PRO; PR:Q13363; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q13363; protein.
DR   Bgee; ENSG00000159692; Expressed in oviduct epithelium and 255 other tissues.
DR   ExpressionAtlas; Q13363; baseline and differential.
DR   Genevisible; Q13363; HS.
DR   GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
DR   GO; GO:0017053; C:transcription repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
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:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:BHF-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR   GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0006342; P:chromatin silencing; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IMP:BHF-UCL.
DR   GO; GO:0090241; P:negative regulation of histone H4 acetylation; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL.
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   IDEAL; IID00469; -.
DR   InterPro; IPR043322; CtBP.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Alternative splicing; Cytoplasm;
KW   Differentiation; Direct protein sequencing; Disease variant;
KW   Host-virus interaction; Isopeptide bond; Mental retardation; NAD; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..440
FT                   /note="C-terminal-binding protein 1"
FT                   /id="PRO_0000076041"
FT   NP_BIND         180..185
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         237..243
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         264..266
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         315..318
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   REGION          1..70
FT                   /note="Interaction with GLIS2 1"
FT                   /evidence="ECO:0000250"
FT   REGION          288..360
FT                   /note="Interaction with GLIS2 2"
FT                   /evidence="ECO:0000250"
FT   REGION          408..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        315
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   SITE            375..376
FT                   /note="Cleavage; by CAPN1"
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   SITE            387..388
FT                   /note="Cleavage; by CAPN1"
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   SITE            409..410
FT                   /note="Cleavage; by CAPN1 and CAPN3"
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         422
FT                   /note="Phosphoserine; by HIPK2"
FT                   /evidence="ECO:0000269|PubMed:14567915"
FT   CROSSLNK        428
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:12679040"
FT   VAR_SEQ         1..13
FT                   /note="MGSSHLLNKGLPL -> MS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043305"
FT   VARIANT         342
FT                   /note="R -> W (in HADDTS; dbSNP:rs869320802)"
FT                   /evidence="ECO:0000269|PubMed:27094857"
FT                   /id="VAR_080622"
FT   MUTAGEN         52
FT                   /note="A->E: Loss of interaction with SIMC1. No effect on
FT                   its proteolytic processing mediated by CAPN3."
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MUTAGEN         66
FT                   /note="V->R: Loss of interaction with SIMC1. Reduced
FT                   proteolytic processing mediated by CAPN3."
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MUTAGEN         134
FT                   /note="C->A: Strongly reduces E1A binding; when associated
FT                   with A-138; A-141 and A-150."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         138
FT                   /note="N->A: Strongly reduces E1A binding; when associated
FT                   with A-134; A-141 and A-150."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         141..142
FT                   /note="RR->AA: Strongly reduces E1A binding; when
FT                   associated with A-163 and A-171."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         141
FT                   /note="R->A: Strongly reduces E1A binding; when associated
FT                   with A-134; A-138 and A-150."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         150
FT                   /note="L->A: Strongly reduces E1A binding; when associated
FT                   with A-134; A-138 and A-141."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         163
FT                   /note="R->A: Strongly reduces E1A binding; when associated
FT                   with A-141; A-142 and A-171."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         171
FT                   /note="R->A: Strongly reduces E1A binding; when associated
FT                   with A-141; A-142 and A-163."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         181
FT                   /note="G->V: Strongly reduces E1A binding; when associated
FT                   with V-183 and A-204."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         183
FT                   /note="G->A: Reduced proteolytic processing mediated by
FT                   CAPN3; when associated with A-186."
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MUTAGEN         183
FT                   /note="G->V: Strongly reduces E1A binding; when associated
FT                   with V-181 and A-204."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         186
FT                   /note="G->A: Reduced proteolytic processing mediated by
FT                   CAPN3; when associated with A-183."
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MUTAGEN         204
FT                   /note="D->A: Strongly reduces E1A binding; when associated
FT                   with V-181 and V-183."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         204
FT                   /note="D->L: Reduced proteolytic processing mediated by
FT                   CAPN3."
FT                   /evidence="ECO:0000269|PubMed:23707407"
FT   MUTAGEN         266
FT                   /note="R->A: Strongly reduces E1A binding; when associated
FT                   with A-290; A-295 and A-315."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         290
FT                   /note="D->A: Strongly reduces E1A binding; when associated
FT                   with A-266; A-295 and A-315."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         295
FT                   /note="E->A: Strongly reduces E1A binding; when associated
FT                   with A-266; A-290 and A-315."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         315
FT                   /note="H->A: Strongly reduces E1A binding; when associated
FT                   with A-266; A-290 and A-295."
FT                   /evidence="ECO:0000269|PubMed:12419229"
FT   MUTAGEN         422
FT                   /note="S->A: Abolishes phosphorylation by HIPK2 and
FT                   prevents UV-induced clearance."
FT                   /evidence="ECO:0000269|PubMed:14567915"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           64..69
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           107..112
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:4U6S"
FT   HELIX           125..141
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           143..151
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           159..165
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           184..194
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           211..215
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           223..229
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          231..235
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           249..252
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:4U6S"
FT   HELIX           272..280
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          283..290
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            303..306
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   HELIX           321..340
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            343..346
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:1MX3"
FT   TURN            353..355
FT                   /evidence="ECO:0007829|PDB:7KWM"
SQ   SEQUENCE   440 AA;  47535 MW;  F071DD30B385603F CRC64;
     MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
     EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
     PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
     GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN
     EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
     QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
     HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA
     PSPGQTVKPE ADRDHASDQL
//
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