CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036880
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Double-stranded RNA-specific adenosine deaminase 
Protein Synonyms/Alias
  
Gene Name
 ADAR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
91LKQIEFLKGQLPEAPubiquitination[1, 2, 3]
207TAHDLSGKLGTPKKEubiquitination[3]
225VLYSLAKKGKLQKEAubiquitination[2]
369AKNIGLTKARDINAVubiquitination[2]
427PAAIPETKRNAEFLTubiquitination[2]
486VHYNGPSKAGYVDFEubiquitination[4]
538PRCSPYKKLTECQLKubiquitination[2]
607AKQDAAMKAMTILLEubiquitination[2]
617TILLEEAKAKDSGKSubiquitination[2]
634SSHYSTEKESEKTAEubiquitination[3]
638STEKESEKTAESQTPubiquitination[5]
656ATSFFSGKSPVTTLLubiquitination[2]
668TLLECMHKLGNSCEFubiquitination[2, 6]
680CEFRLLSKEGPAHEPubiquitination[2, 3]
708PSVSAPSKKVAKQMAubiquitination[5]
709SVSAPSKKVAKQMAAubiquitination[2]
712APSKKVAKQMAAEEAubiquitination[1, 2]
758MMPNKVRKIGELVRYubiquitination[2]
800SGPPHEPKFVYQAKVacetylation[3]
800SGPPHEPKFVYQAKVubiquitination[2, 3, 4, 7]
806PKFVYQAKVGGRWFPubiquitination[2, 3]
821AVCAHSKKQGKQEAAubiquitination[2]
824AHSKKQGKQEAADAAubiquitination[2]
841VLIGENEKAERMGFTacetylation[3]
841VLIGENEKAERMGFTubiquitination[1, 2, 3]
874RSPEAQPKTLPLTGSubiquitination[7]
945KGDSLSLKGETVNDCacetylation[3]
979KYNSQTAKDSIFEPAubiquitination[3]
1039YPVFENPKQGKLRTKubiquitination[2]
1158RVSIYDSKRQSGKTKubiquitination[1, 2]
1202ELSRVSKKNIFLLFKacetylation[3]
1209KNIFLLFKKLCSFRYubiquitination[2]
1210NIFLLFKKLCSFRYRubiquitination[2]
1262ISKPQEEKNFYLCPVubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1269 AA 
Protein Sequence
MMSPICDQTI DSRLKVEKAT WWGRVGGGSR PHWQSPGVRP CPEEVQDPGY SLSGYYTHPF 60
QGYEHRQLRY QQPGPGSSPS SFLLKQIEFL KGQLPEAPVI GKQTPSLPPS LPGLRPRFPV 120
LLASSTRGRQ VDIRGVPRGV HLRSQGLQRG FQHPSPRGRS LPQRGVDCLS SHFQELSIYQ 180
DQEQRILKFL EELGEGKATT AHDLSGKLGT PKKEINRVLY SLAKKGKLQK EAGTPPLWKI 240
AVSTQAWNQH SGVVRPDGHS QGAPNSDPSL EPEDRNSTSV SEDLLEPFIA VSAQAWNQHS 300
GVVRPDSHSQ GSPNSDPGLE PEDSNSTSAL EDPLEFLDMA EIKEKICDYL FNVSDSSALN 360
LAKNIGLTKA RDINAVLIDM ERQGDVYRQG TTPPIWHLTD KKRERMQIKR NTNSVPETAP 420
AAIPETKRNA EFLTCNIPTS NASNNMVTTE KVENGQEPVI KLENRQEARP EPARLKPPVH 480
YNGPSKAGYV DFENGQWATD DIPDDLNSIR AAPGEFRAIM EMPSFYSHGL PRCSPYKKLT 540
ECQLKNPISG LLEYAQFASQ TCEFNMIEQS GPPHEPRFKF QVVINGREFP PAEAGSKKVA 600
KQDAAMKAMT ILLEEAKAKD SGKSEESSHY STEKESEKTA ESQTPTPSAT SFFSGKSPVT 660
TLLECMHKLG NSCEFRLLSK EGPAHEPKFQ YCVAVGAQTF PSVSAPSKKV AKQMAAEEAM 720
KALHGEATNS MASDNQPEGM ISESLDNLES MMPNKVRKIG ELVRYLNTNP VGGLLEYARS 780
HGFAAEFKLV DQSGPPHEPK FVYQAKVGGR WFPAVCAHSK KQGKQEAADA ALRVLIGENE 840
KAERMGFTEV TPVTGASLRR TMLLLSRSPE AQPKTLPLTG STFHDQIAML SHRCFNTLTN 900
SFQPSLLGRK ILAAIIMKKD SEDMGVVVSL GTGNRCVKGD SLSLKGETVN DCHAEIISRR 960
GFIRFLYSEL MKYNSQTAKD SIFEPAKGGE KLQIKKTVSF HLYISTAPCG DGALFDKSCS 1020
DRAMESTESR HYPVFENPKQ GKLRTKVENG EGTIPVESSD IVPTWDGIRL GERLRTMSCS 1080
DKILRWNVLG LQGALLTHFL QPIYLKSVTL GYLFSQGHLT RAICCRVTRD GSAFEDGLRH 1140
PFIVNHPKVG RVSIYDSKRQ SGKTKETSVN WCLADGYDLE ILDGTRGTVD GPRNELSRVS 1200
KKNIFLLFKK LCSFRYRRDL LRLSYGEAKK AARDYETAKN YFKKGLKDMG YGNWISKPQE 1260
EKNFYLCPV 1269 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003726; F:double-stranded RNA adenosine deaminase activity; IEA:InterPro.
 GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR002466; A_deamin.
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR000607; dsRNA_A_deaminase.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF02137; A_deamin
 PF00035; dsrm
 PF02295; z-alpha 
SMART
 SM00552; ADEAMc
 SM00358; DSRM
 SM00550; Zalpha 
PROSITE
 PS50141; A_DEAMIN_EDITASE
 PS50139; DRADA_REPEAT
 PS50137; DS_RBD 
PRINTS