CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015170
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear factor related to kappa-B-binding protein 
Protein Synonyms/Alias
 DNA-binding protein R kappa-B; INO80 complex subunit G 
Gene Name
 NFRKB 
Gene Synonyms/Alias
 INO80G 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
122HFNPEVVKYRQLCFKubiquitination[1]
148QYFHRLLKQILASRSacetylation[2]
148QYFHRLLKQILASRSubiquitination[3]
982DMMATLAKSQVTTVKubiquitination[4]
1004TGGNTTGKGISATLHubiquitination[4]
1049VKVTPDLKPTEASSSacetylation[5, 6]
1049VKVTPDLKPTEASSSubiquitination[4]
1083TVASSEAKPAATIRIacetylation[5, 6]
1198ISQPMKGKSVVTAPIubiquitination[4]
1207VVTAPIIKGNLGANLubiquitination[4, 6]
1237TKLIAGNKPVSFLTAacetylation[5, 6, 7, 8, 9]
1237TKLIAGNKPVSFLTAubiquitination[4]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] 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]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'. 
Sequence Annotation
 REGION 370 495 Winged-helix like domain.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 1022 1022 Phosphoserine.
 MOD_RES 1237 1237 N6-acetyllysine.
 MOD_RES 1291 1291 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1299 AA 
Protein Sequence
MDSLDHMLTD PLELGPCGDG HGTRIMEDCL LGGTRVSLPE DLLEDPEIFF DVVSLSTWQE 60
VLSDSQREHL QQFLPQFPED SAEQQNELIL ALFSGENFRF GNPLHIAQKL FRDGHFNPEV 120
VKYRQLCFKS QYKRYLNSQQ QYFHRLLKQI LASRSDLLEM ARRSGPALPF RQKRPSPSRT 180
PEEREWRTQQ RYLKVLREVK EECGDTALSS DEEDLSSWLP SSPARSPSPA VPLRVVPTLS 240
TTDMKTADKV ELGDSDLKIM LKKHHEKRKH QPDHPDLLTG DLTLNDIMTR VNAGRKGSLA 300
ALYDLAVLKK KVKEKEEKKK KKIKTIKSEA EDLAEPLSST EGVAPLSQAP SPLAIPAIKE 360
EPLEDLKPCL GINEISSSFF SLLLEILLLE SQASLPMLEE RVLDWQSSPA SSLNSWFSAA 420
PNWAELVLPA LQYLAGESRA VPSSFSPFVE FKEKTQQWKL LGQSQDNEKE LAALFQLWLE 480
TKDQAFCKQE NEDSSDATTP VPRVRTDYVV RPSTGEEKRV FQEQERYRYS QPHKAFTFRM 540
HGFESVVGPV KGVFDKETSL NKAREHSLLR SDRPAYVTIL SLVRDAAARL PNGEGTRAEI 600
CELLKDSQFL APDVTSTQVN TVVSGALDRL HYEKDPCVKY DIGRKLWIYL HRDRSEEEFE 660
RIHQAQAAAA KARKALQQKP KPPSKVKSSS KESSIKVLSS GPSEQSQMSL SDSSMPPTPV 720
TPVTPTTPAL PAIPISPPPV SAVNKSGPST VSEPAKSSSG VLLVSSPTMP HLGTMLSPAS 780
SQTAPSSQAA ARVVSHSGSA GLSQVRVVAQ PSLPAVPQQS GGPAQTLPQM PAGPQIRVPA 840
TATQTKVVPQ TVMATVPVKA QTTAATVQRP GPGQTGLTVT SLPATASPVS KPATSSPGTS 900
APSASTAAVI QNVTGQNIIK QVAITGQLGV KPQTGNSIPL TATNFRIQGK DVLRLPPSSI 960
TTDAKGQTVL RITPDMMATL AKSQVTTVKL TQDLFGTGGN TTGKGISATL HVTSNPVHAA 1020
DSPAKASSAS APSSTPTGTT VVKVTPDLKP TEASSSAFRL MPALGVSVAD QKGKSTVASS 1080
EAKPAATIRI VQGLGVMPPK AGQTITVATH AKQGASVASG SGTVHTSAVS LPSMNAAVSK 1140
TVAVASGAAS TPISISTGAP TVRQVPVSTT VVSTSQAGKL PTRITVPLSV ISQPMKGKSV 1200
VTAPIIKGNL GANLSGLGRN IILTTMPAGT KLIAGNKPVS FLTAQQLQQL QQQGQATQVR 1260
IQTVPASHLQ QGTASGSSKA VSTVVVTTAP SPKQAPEQQ 1299 
Gene Ontology
 GO:0031011; C:Ino80 complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0006954; P:inflammatory response; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR024867; NFRKB.
 IPR025220; NFRKB_winged_dom. 
Pfam
 PF14465; NFRKB_winged 
SMART
  
PROSITE
  
PRINTS