ID CTBP2_RAT Reviewed; 445 AA. AC Q9EQH5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 11-DEC-2019, entry version 128. DE RecName: Full=C-terminal-binding protein 2; DE Short=CtBP2; GN Name=Ctbp2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Corepressor targeting diverse transcription regulators. CC Functions in brown adipose tissue (BAT) differentiation. Isoform 2 CC probably acts as a scaffold for specialized synapses (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with HIPK2, ZNF217 and PNN (By similarity). CC Interacts with the transcription factors BKLF, delta EF1/AREB6/ZEB, CC EVI-1 and Friend of GATA (FOG) via the consensus motif P-X-[DNS]-L- CC [STVA]. Can form a complex with BKLF on a CACCC-box oligonucleotide. CC Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with CC NRIP1 and WIZ. Interacts with PRDM16; represses white adipose tissue CC (WAT)-specific genes expression (By similarity). Interacts with MCRIP1 CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P56545}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cell junction, synapse CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9EQH5-1; Sequence=Displayed; CC Name=2; Synonyms=Ribeye; CC IsoId=Q9EQH5-2; Sequence=VSP_027611; CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically localized in synaptic CC ribbon (at protein level). {ECO:0000269|PubMed:11163272}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF222712; AAG45952.1; -; mRNA. DR EMBL; AABR03001613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03000195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_445787.1; NM_053335.1. [Q9EQH5-2] DR SMR; Q9EQH5; -. DR BioGrid; 249593; 1. DR STRING; 10116.ENSRNOP00000023404; -. DR iPTMnet; Q9EQH5; -. DR PhosphoSitePlus; Q9EQH5; -. DR jPOST; Q9EQH5; -. DR PaxDb; Q9EQH5; -. DR PRIDE; Q9EQH5; -. DR Ensembl; ENSRNOT00000023404; ENSRNOP00000023404; ENSRNOG00000017326. [Q9EQH5-2] DR Ensembl; ENSRNOT00000023574; ENSRNOP00000023574; ENSRNOG00000017326. [Q9EQH5-1] DR GeneID; 81717; -. DR KEGG; rno:81717; -. DR UCSC; RGD:68372; rat. [Q9EQH5-1] DR CTD; 1488; -. DR RGD; 68372; Ctbp2. DR eggNOG; KOG0067; Eukaryota. DR eggNOG; COG0111; LUCA. DR GeneTree; ENSGT00940000154430; -. DR HOGENOM; HOG000136701; -. DR InParanoid; Q9EQH5; -. DR KO; K04496; -. DR OMA; IKCVAPN; -. DR OrthoDB; 700058at2759; -. DR PhylomeDB; Q9EQH5; -. DR TreeFam; TF313593; -. DR Reactome; R-RNO-4641265; Repression of WNT target genes. DR PRO; PR:Q9EQH5; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000017326; Expressed in 10 organ(s), highest expression level in lung. DR Genevisible; Q9EQH5; RN. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD. DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:RGD. DR GO; GO:0099523; C:presynaptic cytosol; ISO:RGD. DR GO; GO:0097470; C:ribbon synapse; ISO:RGD. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISO:RGD. 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:RGD. DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD. DR GO; GO:0042974; F:retinoic acid receptor binding; ISO:RGD. DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD. DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD. DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0035563; P:positive regulation of chromatin binding; ISO:RGD. DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD. DR GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Differentiation; 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_0000299356" FT NP_BIND 186..191 FT /note="NAD" FT /evidence="ECO:0000250" FT NP_BIND 243..249 FT /note="NAD" FT /evidence="ECO:0000250" FT NP_BIND 270..272 FT /note="NAD" FT /evidence="ECO:0000250" FT NP_BIND 321..324 FT /note="NAD" FT /evidence="ECO:0000250" 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:0000250" FT BINDING 296 FT /note="NAD" FT /evidence="ECO:0000250" FT MOD_RES 22 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P56545" FT MOD_RES 428 FT /note="Phosphoserine; by HIPK2" FT /evidence="ECO:0000250|UniProtKB:P56545" FT VAR_SEQ 1..20 FT /note="MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWDAAGWYEGPWEN FT AGPPGRRSSLTYGPGEGVWCELVNHRAQDTESCLSREAFYNSLASRKGSVPDFTFYDSR FT QAVMSGRGSVLPQDYYGDPSRGTRVPKEPPFYRDPGTSRPVPSYGVLGSRIPWEQVQGQ FT LPALQDAGHLYRESGSKTVLHGQRTHCRAPSPGRYGREQPDSRLGIEVPTYSPNSSQVY FT NDICERPVDSTHARQVAPTCLVVDPSSTAPTENSTGVAPGSLNRGYGPTRESIHSKLAY FT ENYEADLSTFQGPGGKRTVYPEFLALLRAEGVAEATLAALLQQGFDSPAVLATLEDADI FT KSVAPNLGQARVLSRLVSSCRTEMQFRRQDRTGPPPRHRSSSFSHRSELLPNDTASLGT FT TALQFHPAGPLQTPSPRGGDLGRRPSSAPSQHLLETAATYSAPVVGSQTPHLPSNSGYS FT SPTPCALTARLASSYPSQAGVALTANPGPSVPLHSSPRTAYSTSYTVPMELLKRERSVT FT ASPLPSPHASPQLLRKPGAAPVEPAALPPVRQSLHTPHPPYQKVARRTGAPIIVSTMLT FT PEPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11163272" FT /id="VSP_027611" SQ SEQUENCE 445 AA; 48987 MW; 403012CDEB2E492B 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 FFVTSTPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP PAMEGIIPGG IPVTHNLPTV AHPSQAPSPN QPTKHGDNRE HPNEQ //