CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear receptor corepressor 2 
Protein Synonyms/Alias
 N-CoR2; CTG repeat protein 26; SMAP270; Silencing mediator of retinoic acid and thyroid hormone receptor; SMRT; T3 receptor-associating factor; TRAC; Thyroid-, retinoic-acid-receptor-associated corepressor 
Gene Name
 NCOR2 
Gene Synonyms/Alias
 CTG26 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
137AGSEDLTKDRSLTGKubiquitination[1]
878EEGPAKGKDAEAAEAacetylation[2]
959RANASPQKPLDLKQLacetylation[2]
1218VPGGSITKGIPSTRVacetylation[2]
1248TPADVLYKGTITRIIacetylation[2]
1517ACYEESLKSRPGTASubiquitination[1]
1586EGSLSSSKASQDRKLubiquitination[1]
1795GGPTHLTKPTTTSSSacetylation[2]
1970TGHAFLAKPPARSGLacetylation[2]
2033ASDPHREKTQSKPFSacetylation[2]
2037HREKTQSKPFSIQELacetylation[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Transcriptional corepressor of NR4A2/NURR1 and acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state (By similarity). Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. 
Sequence Annotation
 DOMAIN 427 478 SANT 1.
 DOMAIN 610 661 SANT 2.
 REGION 254 312 Interaction with SIN3A/B (By similarity).
 REGION 2139 2142 Required for interaction with RARA in the
 MOTIF 2147 2151 CORNR box of ID1.
 MOTIF 2350 2354 CORNR box of ID2.
 MOD_RES 54 54 Phosphoserine.
 MOD_RES 67 67 Phosphoserine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 152 152 Phosphoserine.
 MOD_RES 156 156 Phosphothreonine.
 MOD_RES 215 215 Phosphoserine.
 MOD_RES 553 553 Phosphothreonine.
 MOD_RES 554 554 Phosphoserine.
 MOD_RES 750 750 Phosphoserine.
 MOD_RES 753 753 Phosphoserine.
 MOD_RES 864 864 Phosphoserine (By similarity).
 MOD_RES 878 878 N6-acetyllysine.
 MOD_RES 939 939 Phosphoserine.
 MOD_RES 956 956 Phosphoserine.
 MOD_RES 959 959 N6-acetyllysine.
 MOD_RES 1218 1218 N6-acetyllysine.
 MOD_RES 1248 1248 N6-acetyllysine.
 MOD_RES 1259 1259 Phosphoserine.
 MOD_RES 1331 1331 Phosphoserine.
 MOD_RES 1391 1391 Phosphothreonine.
 MOD_RES 1444 1444 Phosphothreonine (By similarity).
 MOD_RES 1487 1487 Phosphoserine.
 MOD_RES 1786 1786 Phosphoserine.
 MOD_RES 1872 1872 Phosphoserine.
 MOD_RES 1970 1970 N6-acetyllysine.
 MOD_RES 2016 2016 Phosphoserine.
 MOD_RES 2037 2037 N6-acetyllysine.
 MOD_RES 2057 2057 Phosphoserine.
 MOD_RES 2065 2065 Phosphoserine.
 MOD_RES 2068 2068 Phosphoserine.
 MOD_RES 2069 2069 Phosphoserine.
 MOD_RES 2073 2073 Phosphothreonine.
 MOD_RES 2214 2214 Phosphoserine.
 MOD_RES 2234 2234 Phosphoserine.
 MOD_RES 2269 2269 Phosphoserine.
 MOD_RES 2463 2463 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2525 AA 
Protein Sequence
MSGSTQPVAQ TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA SHLSPGSIIQ 60
PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM EFIESKRPRL ELLPDPLLRP 120
SPLLATGQPA GSEDLTKDRS LTGKLEPVSP PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD 180
REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA 240
AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ 300
RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG 360
LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMADPM 420
KVYKDRQVMN MWSEQEKETF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK 480
SLVRRSYRRR GKSQQQQQQQ QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN 540
DKEDLLKEKT DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ 600
SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK NFYFNYKKRQ 660
NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV EDEEMEASGV SGNEEEMVEE 720
AEALHASGNE VPRGECSGPA TVNNSSDTES IPSPHTEAAK DTGQNGPKPP ATLGADGPPP 780
GPPTPPPEDI PAPTEPTPAS EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG 840
EEQKPPAAEE LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS 900
GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD PRANASPQKP 960
LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP PPQNLQPESD APQQPGSSPR 1020
GKSRSPAPPA DKEAEKPVFF PAFAAEAQKL PGDPPCWTSG LPFPVPPREV IKASPHAPDP 1080
SAFSYAPPGH PLPLGLHDTA RPVLPRPPTI SNPPPLISSA KHPSVLERQI GAISQGMSVQ 1140
LHVPYSEHAK APVGPVTMGL PLPMDPKKLA PFSGVKQEQL SPRGQAGPPE SLGVPTAQEA 1200
SVLRGTALGS VPGGSITKGI PSTRVPSDSA ITYRGSITHG TPADVLYKGT ITRIIGEDSP 1260
SRLDRGREDS LPKGHVIYEG KKGHVLSYEG GMSVTQCSKE DGRSSSGPPH ETAAPKRTYD 1320
MMEGRVGRAI SSASIEGLMG RAIPPERHSP HHLKEQHHIR GSITQGIPRS YVEAQEDYLR 1380
REAKLLKREG TPPPPPPSRD LTEAYKTQAL GPLKLKPAHE GLVATVKEAG RSIHEIPREE 1440
LRHTPELPLA PRPLKEGSIT QGTPLKYDTG ASTTGSKKHD VRSLIGSPGR TFPPVHPLDV 1500
MADARALERA CYEESLKSRP GTASSSGGSI ARGAPVIVPE LGKPRQSPLT YEDHGAPFAG 1560
HLPRGSPVTT REPTPRLQEG SLSSSKASQD RKLTSTPREI AKSPHSTVPE HHPHPISPYE 1620
HLLRGVSGVD LYRSHIPLAF DPTSIPRGIP LDAAAAYYLP RHLAPNPTYP HLYPPYLIRG 1680
YPDTAALENR QTIINDYITS QQMHHNAATA MAQRADMLRG LSPRESSLAL NYAAGPRGII 1740
DLSQVPHLPV LVPPTPGTPA TAMDRLAYLP TAPQPFSSRH SSSPLSPGGP THLTKPTTTS 1800
SSERERDRDR ERDRDREREK SILTSTTTVE HAPIWRPGTE QSSGSSGSSG GGGGSSSRPA 1860
SHSHAHQHSP ISPRTQDALQ QRPSVLHNTG MKGIITAVEP STPTVLRSTS TSSPVRPAAT 1920
FPPATHCPLG GTLDGVYPTL MEPVLLPKEA PRVARPERPR ADTGHAFLAK PPARSGLEPA 1980
SSPSKGSEPR PLVPPVSGHA TIARTPAKNL APHHASPDPP APPASASDPH REKTQSKPFS 2040
IQELELRSLG YHGSSYSPEG VEPVSPVSSP SLTHDKGLPK HLEELDKSHL EGELRPKQPG 2100
PVKLGGEAAH LPHLRPLPES QPSSSPLLQT APGVKGHQRV VTLAQHISEV ITQDYTRHHP 2160
QQLSAPLPAP LYSFPGASCP VLDLRRPPSD LYLPPPDHGA PARGSPHSEG GKRSPEPNKT 2220
SVLGGGEDGI EPVSPPEGMT EPGHSRSAVY PLLYRDGEQT EPSRMGSKSP GNTSQPPAFF 2280
SKLTESNSAM VKSKKQEINK KLNTHNRNEP EYNISQPGTE IFNMPAITGT GLMTYRSQAV 2340
QEHASTNMGL EAIIRKALMG KYDQWEESPP LSANAFNPLN ASASLPAAMP ITAADGRSDH 2400
TLTSPGGGGK AKVSGRPSSR KAKSPAPGLA SGDRPPSVSS VHSEGDCNRR TPLTNRVWED 2460
RPSSAGSTPF PYNPLIMRLQ AGVMASPPPP GLPAGSGPLA GPHHAWDEEP KPLLCSQYET 2520
LSDSE 2525 
Gene Ontology
 GO:0016604; C:nuclear body; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0072365; P:regulation of cellular ketone metabolic process by negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. 
Interpro
 IPR009057; Homeodomain-like.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom. 
Pfam
 PF00249; Myb_DNA-binding 
SMART
 SM00717; SANT 
PROSITE
 PS51293; SANT 
PRINTS