GenomeNet

Database: UniProt
Entry: P56546
LinkDB: P56546
Original site: P56546 
ID   CTBP2_MOUSE             Reviewed;         445 AA.
AC   P56546; O54855; O88462;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   13-FEB-2019, entry version 162.
DE   RecName: Full=C-terminal-binding protein 2;
DE            Short=CtBP2;
GN   Name=Ctbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
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 1).
RX   PubMed=9724649; DOI=10.1093/emboj/17.17.5129;
RA   Turner J., Crossley M.;
RT   "Cloning and characterization of mCtBP2, a co-repressor that
RT   associates with basic krueppel-like factor and other mammalian
RT   transcriptional regulators.";
RL   EMBO J. 17:5129-5140(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR;
RX   PubMed=10567582; DOI=10.1128/MCB.19.12.8581;
RA   Furusawa T., Moribe H., Kondoh H., Higashi Y.;
RT   "Identification of CtBP1 and CtBP2 as corepressors of zinc finger-
RT   homeodomain factor deltaEF1.";
RL   Mol. Cell. Biol. 19:8581-8590(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   INTERACTION WITH NRIP1.
RX   PubMed=14736873; DOI=10.1074/jbc.M313906200;
RA   Christian M., Tullet J.M.A., Parker M.G.;
RT   "Characterization of four autonomous repression domains in the
RT   corepressor receptor interacting protein 140.";
RL   J. Biol. Chem. 279:15645-15651(2004).
RN   [6]
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   [7]
RP   INTERACTION WITH ZNF217.
RX   PubMed=16940172; DOI=10.1128/MCB.00680-06;
RA   Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P.,
RA   Corda D., Bolognesi M., Crossley M.;
RT   "Specific recognition of ZNF217 and other zinc finger proteins at a
RT   surface groove of C-terminal binding proteins.";
RL   Mol. Cell. Biol. 26:8159-8172(2006).
RN   [8]
RP   FUNCTION, INTERACTION WITH PRDM16, AND SUBCELLULAR LOCATION.
RX   PubMed=18483224; DOI=10.1101/gad.1666108;
RA   Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA   Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT   "Regulation of the brown and white fat gene programs through a
RT   PRDM16/CtBP transcriptional complex.";
RL   Genes Dev. 22:1397-1409(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC       Isoform 2 probably acts as a scaffold for specialized synapses (By
CC       similarity). Functions in brown adipose tissue (BAT)
CC       differentiation. {ECO:0000250, ECO:0000269|PubMed:18483224}.
CC   -!- SUBUNIT: Interacts with HIPK2 and PNN (By similarity). Interacts
CC       with the transcription factors ZNF217, BKLF, delta EF1/AREB6/ZEB,
CC       EVI-1 and Friend of GATA (FOG) via the consensus motif P-X-[DNS]-
CC       L-[STVA]. Interacts also with the C-terminus of adenovirus E1A
CC       protein. Can form a complex with BKLF on a CACCC-box
CC       oligonucleotide. Can form homodimers or heterodimers of CTBP1 and
CC       CTBP2. Interacts with NRIP1 and WIZ. Interacts with PRDM16;
CC       represses white adipose tissue (WAT)-specific genes expression.
CC       Interacts with MCRIP1 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P56545, ECO:0000269|PubMed:14736873,
CC       ECO:0000269|PubMed:16702210, ECO:0000269|PubMed:16940172,
CC       ECO:0000269|PubMed:18483224}.
CC   -!- INTERACTION:
CC       Q14526:HIC1 (xeno); NbExp=2; IntAct=EBI-1384883, EBI-2507362;
CC       Q03112:MECOM (xeno); NbExp=3; IntAct=EBI-1384883, EBI-1384862;
CC       Q9HAZ2-2:PRDM16 (xeno); NbExp=2; IntAct=EBI-1384883, EBI-5282871;
CC       Q9HAZ2-4:PRDM16 (xeno); NbExp=2; IntAct=EBI-1384883, EBI-4566658;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction,
CC       synapse {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P56546-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ribeye;
CC         IsoId=P56546-2; Sequence=VSP_027616;
CC   -!- TISSUE SPECIFICITY: Found in all tissues except spleen and liver.
CC   -!- DEVELOPMENTAL STAGE: Strong expression confined to the embryonic
CC       stages.
CC   -!- PTM: Phosphorylation by HIPK2 on Ser-428 induces proteasomal
CC       degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC40043.1; Type=Frameshift; Positions=12; Evidence={ECO:0000305};
DR   EMBL; AF016508; AAC40043.1; ALT_FRAME; mRNA.
DR   EMBL; AF059735; AAC33873.1; -; mRNA.
DR   EMBL; AB033123; BAA85181.1; -; mRNA.
DR   EMBL; AC119806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS21930.1; -. [P56546-1]
DR   CCDS; CCDS52417.1; -. [P56546-2]
DR   RefSeq; NP_001164215.1; NM_001170744.1. [P56546-2]
DR   RefSeq; NP_034110.1; NM_009980.4. [P56546-1]
DR   RefSeq; XP_006507371.1; XM_006507308.3. [P56546-1]
DR   RefSeq; XP_006507372.1; XM_006507309.3. [P56546-1]
DR   RefSeq; XP_006507373.1; XM_006507310.3. [P56546-1]
DR   RefSeq; XP_006507374.1; XM_006507311.3. [P56546-1]
DR   RefSeq; XP_006507375.1; XM_006507312.3. [P56546-1]
DR   UniGene; Mm.246240; -.
DR   UniGene; Mm.252063; -.
DR   UniGene; Mm.389984; -.
DR   ProteinModelPortal; P56546; -.
DR   SMR; P56546; -.
DR   BioGrid; 198962; 22.
DR   IntAct; P56546; 10.
DR   MINT; P56546; -.
DR   STRING; 10090.ENSMUSP00000130294; -.
DR   iPTMnet; P56546; -.
DR   PhosphoSitePlus; P56546; -.
DR   REPRODUCTION-2DPAGE; P56546; -.
DR   PaxDb; P56546; -.
DR   PeptideAtlas; P56546; -.
DR   PRIDE; P56546; -.
DR   Ensembl; ENSMUST00000033269; ENSMUSP00000033269; ENSMUSG00000030970. [P56546-1]
DR   Ensembl; ENSMUST00000169570; ENSMUSP00000130294; ENSMUSG00000030970. [P56546-2]
DR   GeneID; 13017; -.
DR   KEGG; mmu:13017; -.
DR   UCSC; uc009kcy.1; mouse. [P56546-1]
DR   UCSC; uc012fve.1; mouse. [P56546-2]
DR   CTD; 1488; -.
DR   MGI; MGI:1201686; Ctbp2.
DR   eggNOG; KOG0067; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000154430; -.
DR   HOGENOM; HOG000136701; -.
DR   HOVERGEN; HBG001898; -.
DR   InParanoid; P56546; -.
DR   KO; K04496; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; P56546; -.
DR   TreeFam; TF313593; -.
DR   Reactome; R-MMU-4641265; Repression of WNT target genes.
DR   ChiTaRS; Ctbp2; mouse.
DR   PRO; PR:P56546; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030970; Expressed in 301 organ(s), highest expression level in ear.
DR   ExpressionAtlas; P56546; baseline and differential.
DR   Genevisible; P56546; MM.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR   GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR   GO; GO:0097470; C:ribbon synapse; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
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; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0042974; F:retinoic acid receptor binding; IPI:MGI.
DR   GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR   GO; GO:0003713; F:transcription coactivator activity; IGI:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0035563; P:positive regulation of chromatin binding; IMP:MGI.
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; IDA:SynGO.
DR   GO; GO:0050872; P:white fat cell differentiation; IDA: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   Alternative splicing; Cell junction; Complete proteome;
KW   Differentiation; Methylation; NAD; Nucleus; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Repressor; Synapse; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    445       C-terminal-binding protein 2.
FT                                /FTId=PRO_0000076045.
FT   NP_BIND     186    191       NAD. {ECO:0000250}.
FT   NP_BIND     243    249       NAD. {ECO:0000250}.
FT   NP_BIND     270    272       NAD. {ECO:0000250}.
FT   NP_BIND     321    324       NAD. {ECO:0000250}.
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:0000250}.
FT   BINDING     296    296       NAD. {ECO:0000250}.
FT   MOD_RES      22     22       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES     428    428       Phosphoserine; by HIPK2.
FT                                {ECO:0000250|UniProtKB:P56545}.
FT   VAR_SEQ       1     20       MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWD
FT                                AAGWYEGPWENAGPPGRRSSLTYGPGEGTWCELLNHRAQDT
FT                                ESYLSREAFYNSLASRKGSVPDFTFYDSRQAVMSGRGSVLP
FT                                QDYYGDPSRGTRVPKEPPFYRDPGTSRPVPSYGMLGSRMPW
FT                                EQVQGQLPALQDTGHLYPESGGKTVPHGQRTHGRAPSPGRY
FT                                GREQPDTRLGIEVPTYSPNSSQVYNDICERPVDSTPARQVA
FT                                PTCLVVDPSSAVPTENSTGVAPGSLNRGYGPTRESIHSKLA
FT                                YENYEADLSTFQGPGGKRTMYPEFLALLRAEGVAEATLAAL
FT                                LQQGFDSPAVLATLEDADIKSVAPNLGQARVLSRLASSCRT
FT                                EMQFRRQDRTGPLPRNRSSSFSHRSELLPNDMASLGTTALQ
FT                                FHPAGPLQTPSPRAGDLGRRPSSAPSQHLLETAATYSTPVV
FT                                GSQTPHLPSNSGYSSPTPCALTARLASSYPSQAGVALTANP
FT                                GPSAPLHSNPRTAYSTSYTVPMELLKRERSMTASPLPSPHG
FT                                SPQLLRKPGAAPVEPSTLPPVSQSLHTPHSPYQKVARRTGA
FT                                PIIVSTMLTPEPS (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_027616.
FT   CONFLICT     49     49       P -> H (in Ref. 1; AAC40043).
FT                                {ECO:0000305}.
FT   CONFLICT    170    170       E -> D (in Ref. 1; AAC40043).
FT                                {ECO:0000305}.
FT   CONFLICT    288    288       G -> A (in Ref. 1; AAC40043).
FT                                {ECO:0000305}.
SQ   SEQUENCE   445 AA;  48957 MW;  5A81B9D75A9E493B CRC64;
     MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC
     DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG
     IAVCNIPSAA VEETADSTVC 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 PAMEGIIPGG IPVTHNLPTV
     AHPSQAPSPN QPTKHGDNRE HPNEQ
//
DBGET integrated database retrieval system