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 13-NOV-2007, entry version 35. DE C-terminal-binding protein 2 (CtBP2). GN Name=Ctbp2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX MEDLINE=21094490; 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., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA 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., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA 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., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). CC -!- FUNCTION: Corepressor targeting diverse transcription regulators. CC Isoform 2 probably acts as a scaffold for specialized synapses (By CC similarity). CC -!- SUBUNIT: Interacts with HIPK2 and PNN (By similarity). Interacts CC with the transcription factors BKLF, delta EF1/AREB6/ZEB, EVI-1 CC 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 CC oligonucleotide. Can form homodimers or heterodimers of CTBP1 and CC CTBP2. Interacts with NRIP1 and WIZ (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). Cell junction, synapse CC (By similarity). 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 Note=Contains a phosphothreonine at position 171 (By CC similarity). Contains a phosphoserine at position 177 (By CC similarity); CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically localized in CC synaptic ribbon (at protein level). CC -!- PTM: Isoform 2 is phosphorylated upon DNA damage, probably by ATM CC or ATR at Thr-171 and Ser-177. Phosphorylation by HIPK2 on Ser-428 CC induces proteasomal degradation (By similarity). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. 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; -. DR UniGene; Rn.138124; -. DR HSSP; Q13363; 1MX3. DR SMR; Q9EQH5; 576-905. DR Ensembl; ENSRNOG00000017326; Rattus norvegicus. DR GeneID; 81717; -. DR KEGG; rno:81717; -. DR RGD; 68372; Ctbp2. DR InterPro; IPR006139; 2_Hacid_DH. DR InterPro; IPR006140; 2hydac_DH_NAD_bd. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; NAD; Nucleus; Oxidoreductase; KW Phosphoprotein; Synapse. FT CHAIN 1 445 C-terminal-binding protein 2. FT /FTId=PRO_0000299356. FT ACT_SITE 272 272 Potential. FT ACT_SITE 301 301 Potential. FT ACT_SITE 321 321 Potential. FT MOD_RES 428 428 Phosphoserine; by HIPK2 (By similarity). FT VAR_SEQ 1 20 MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWD FT AAGWYEGPWENAGPPGRRSSLTYGPGEGVWCELVNHRAQDT FT ESCLSREAFYNSLASRKGSVPDFTFYDSRQAVMSGRGSVLP FT QDYYGDPSRGTRVPKEPPFYRDPGTSRPVPSYGVLGSRIPW FT EQVQGQLPALQDAGHLYRESGSKTVLHGQRTHCRAPSPGRY FT GREQPDSRLGIEVPTYSPNSSQVYNDICERPVDSTHARQVA FT PTCLVVDPSSTAPTENSTGVAPGSLNRGYGPTRESIHSKLA FT YENYEADLSTFQGPGGKRTVYPEFLALLRAEGVAEATLAAL FT LQQGFDSPAVLATLEDADIKSVAPNLGQARVLSRLVSSCRT FT EMQFRRQDRTGPPPRHRSSSFSHRSELLPNDTASLGTTALQ FT FHPAGPLQTPSPRGGDLGRRPSSAPSQHLLETAATYSAPVV FT GSQTPHLPSNSGYSSPTPCALTARLASSYPSQAGVALTANP FT GPSVPLHSSPRTAYSTSYTVPMELLKRERSVTASPLPSPHA FT SPQLLRKPGAAPVEPAALPPVRQSLHTPHPPYQKVARRTGA FT PIIVSTMLTPEPS (in isoform 2). FT /FTId=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 //