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Database: UniProt
Entry: Q9YHU0
LinkDB: Q9YHU0
Original site: Q9YHU0 
ID   CTBP1_XENLA             Reviewed;         440 AA.
AC   Q9YHU0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JAN-2019, entry version 91.
DE   RecName: Full=C-terminal-binding protein 1;
DE            Short=CtBP1;
DE            EC=1.1.1.-;
DE   AltName: Full=C-terminal-binding protein A;
GN   Name=ctbp1; Synonyms=ctbp-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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.,
RA   Otte A.P.;
RT   "C-terminal binding protein is a transcriptional repressor that
RT   interacts with a specific class of vertebrate polycomb proteins.";
RL   Mol. Cell. Biol. 19:777-787(1999).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC       Has dehydrogenase activity.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AF091554; AAD14596.1; -; mRNA.
DR   RefSeq; NP_001079151.1; NM_001085682.1.
DR   RefSeq; XP_018110260.1; XM_018254771.1.
DR   UniGene; Xl.447; -.
DR   ProteinModelPortal; Q9YHU0; -.
DR   SMR; Q9YHU0; -.
DR   PRIDE; Q9YHU0; -.
DR   GeneID; 373701; -.
DR   KEGG; xla:373701; -.
DR   CTD; 373701; -.
DR   Xenbase; XB-GENE-864974; ctbp1.
DR   HOVERGEN; HBG001898; -.
DR   KO; K04496; -.
DR   OrthoDB; 700058at2759; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   NAD; Nucleus; Oxidoreductase.
FT   CHAIN         1    440       C-terminal-binding protein 1.
FT                                /FTId=PRO_0000076046.
FT   NP_BIND     180    185       NAD. {ECO:0000250}.
FT   NP_BIND     237    243       NAD. {ECO:0000250}.
FT   NP_BIND     264    266       NAD. {ECO:0000250}.
FT   NP_BIND     315    318       NAD. {ECO:0000250}.
FT   ACT_SITE    266    266       {ECO:0000250}.
FT   ACT_SITE    295    295       {ECO:0000250}.
FT   ACT_SITE    315    315       Proton donor. {ECO:0000250}.
FT   BINDING     100    100       NAD. {ECO:0000250}.
FT   BINDING     204    204       NAD. {ECO:0000250}.
FT   BINDING     290    290       NAD. {ECO:0000250}.
SQ   SEQUENCE   440 AA;  47777 MW;  E1AB044901A00116 CRC64;
     MGSSHLLNKG LPLGIRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
     EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
     PAASVEETAD STMCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
     GLGRVGQAVA LRAKTFGFNV FFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN
     EHNHHLINDF TIKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFT
     QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
     HWASMDPGVV HPELNGGAYR YPQGVVSVAP AGLPAAVEGI VPSAMSLSHA HPAVAHPPHA
     PSPGQTIKPE ADRDHPSDQL
//
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