CTBP2_RAT
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 03-AUG-2022, entry version 138.
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}. Synapse {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}.
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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 AlphaFoldDB; Q9EQH5; -.
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; ENSRNOT00000114061; ENSRNOP00000090411; 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 GeneTree; ENSGT00940000154430; -.
DR HOGENOM; CLU_012460_0_0_1; -.
DR InParanoid; Q9EQH5; -.
DR OMA; MLAPEPX; -.
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 ovary and 20 other tissues.
DR Genevisible; Q9EQH5; RN.
DR GO; GO:0070161; C:anchoring 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:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:RGD.
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:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
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; Differentiation; Methylation; NAD; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repressor; Synapse;
KW Transcription; Transcription regulation.
FT CHAIN 1..445
FT /note="C-terminal-binding protein 2"
FT /id="PRO_0000299356"
FT REGION 414..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 321..324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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
