CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012591
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear receptor coactivator 2 
Protein Synonyms/Alias
 NCoA-2; Class E basic helix-loop-helix protein 75; bHLHe75; Transcriptional intermediary factor 2; hTIF2 
Gene Name
 NCOA2 
Gene Synonyms/Alias
 BHLHE75; TIF2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
239VSQPKSIKEEGEDLQsumoylation[1]
636QSRLHDSKGQTKLLQacetylation[2]
640HDSKGQTKLLQLLTTacetylation[2]
640HDSKGQTKLLQLLTTubiquitination[3]
731PGSEVTIKQEPVSPKsumoylation[1]
780TDPASNTKLIAMKTEacetylation[2, 4]
785NTKLIAMKTEKEEMSacetylation[2, 4]
788LIAMKTEKEEMSFEPsumoylation[1]
Reference
 [1] The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1.
 Kotaja N, Karvonen U, Jänne OA, Palvimo JJ.
 J Biol Chem. 2002 Aug 16;277(33):30283-8. [PMID: 12060666]
 [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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF- 2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. 
Sequence Annotation
 DOMAIN 26 83 bHLH.
 DOMAIN 119 183 PAS.
 REGION 691 743 CASP8AP2-binding (By similarity).
 MOTIF 641 645 LXXLL motif 1.
 MOTIF 690 694 LXXLL motif 2.
 MOTIF 745 749 LXXLL motif 3.
 MOTIF 878 882 LXXLL motif 4.
 MOTIF 1079 1087 LLXXLXXXL motif.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 487 487 Phosphoserine.
 MOD_RES 493 493 Phosphoserine.
 MOD_RES 499 499 Phosphoserine.
 MOD_RES 640 640 N6-acetyllysine.
 MOD_RES 699 699 Phosphoserine (By similarity).
 MOD_RES 716 716 Phosphoserine (By similarity).
 MOD_RES 780 780 N6-acetyllysine.
 MOD_RES 785 785 N6-acetyllysine.
 MOD_RES 851 851 Phosphoserine.
 MOD_RES 854 854 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Activator; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1464 AA 
Protein Sequence
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA ELIFANFNDI 60
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML 120
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSI 180
VNGGSWSGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE 240
EGEDLQSCLI CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV 300
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT 360
TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS NSPAHQALCS GNPGQDMTLS 420
SNINFPINGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG 480
QPTSMLSPRH RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL 540
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA 600
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD QMEPSPLASS 660
LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKDLSQESS 720
STAPGSEVTI KQEPVSPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK 780
LIAMKTEKEE MSFEPGDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII 840
NDLMQLTAEN SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG 900
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP SGEWAPQSSA 960
VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ TLQSQVMNIG PSELEMNMGG 1020
PQYSQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL 1080
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ 1140
AQMAQGSYSP MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ 1200
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ 1260
RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT 1320
PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN 1380
TSMYSNNMNI NVSMATNTGG MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG 1440
NLFPNQLPGM DMIKQEGDTT RKYC 1464 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:BHF-UCL.
 GO:0004871; F:signal transducer activity; IEA:InterPro.
 GO:0030375; F:thyroid hormone receptor coactivator activity; IEA:Compara.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0016573; P:histone acetylation; IEA:GOC.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011598; bHLH_dom.
 IPR010011; DUF1518.
 IPR009110; Nuc_rcpt_coact.
 IPR014920; Nuc_rcpt_coact_Ncoa-typ.
 IPR017426; Nuclear_rcpt_coactivator.
 IPR001610; PAC.
 IPR000014; PAS.
 IPR013767; PAS_fold.
 IPR014935; SRC-1.
 IPR008955; Src1_rcpt_coact. 
Pfam
 PF07469; DUF1518
 PF08815; Nuc_rec_co-act
 PF00989; PAS
 PF08832; SRC-1 
SMART
 SM00353; HLH
 SM00086; PAC
 SM00091; PAS 
PROSITE
 PS50888; BHLH
 PS50112; PAS 
PRINTS