CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043231
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 ubiquitin-protein ligase RNF213 
Protein Synonyms/Alias
  
Gene Name
 RNF213 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44AGHYRVPKQTLSAAAubiquitination[1]
71SERAGVGKSLYVKRLubiquitination[1, 2]
83KRLHDKMKMQLNVKNubiquitination[1]
89MKMQLNVKNVPLKTIubiquitination[1, 2, 3]
94NVKNVPLKTIRLIDPubiquitination[1, 2]
202SFLDIFPKVTCRPPKubiquitination[1]
209KVTCRPPKEVIDMELubiquitination[1, 2, 3, 4]
440PFNVDFDKLPRHKKLubiquitination[1, 2, 3]
499MGETGCGKTRLIKFLubiquitination[1]
504CGKTRLIKFLSDLRRubiquitination[1]
520GTNADTIKLVKVHGGubiquitination[1, 2]
523ADTIKLVKVHGGTTAubiquitination[1]
602AACNPYRKHSEEMICubiquitination[1]
701ASQGFMRKTEDECSFubiquitination[1]
786AIARFFPKPYDDSRLubiquitination[1]
843IPLFLVGKPGSSKSLubiquitination[1]
852GSSKSLAKTIVADAMubiquitination[1]
873SDLFRSLKQVHLVSFubiquitination[1]
931DSPKMPLKTLHPLLEubiquitination[1]
950EDDPAPHKKVGFVGIacetylation[2]
950EDDPAPHKKVGFVGIubiquitination[1]
951DDPAPHKKVGFVGISubiquitination[1, 2, 3]
966NWALDPAKMNRGIFVubiquitination[1, 3]
988TELIESAKGICSSDIubiquitination[1, 2]
1010GYFASFAKAYETVCKubiquitination[1]
1017KAYETVCKRQDKEFFubiquitination[2]
1021TVCKRQDKEFFGLRDubiquitination[1]
1041KMVFAAAKASNRKPSubiquitination[1]
1046AAKASNRKPSPQDIAubiquitination[1]
1063VLRNFSGKDDIQALDubiquitination[1]
1092VSPMQLIKQNIFGPSubiquitination[1, 3]
1101NIFGPSQKVPGGEQEubiquitination[1, 5]
1232EEKDVVYKHFPIPLIubiquitination[1, 2]
1255DINTVLEKWQKSIVEubiquitination[1]
1322LTEELHQKVSEEAKSubiquitination[1, 2]
1328QKVSEEAKSILLNCAubiquitination[1, 2, 5]
1444NCLTNTAKCKILIFQubiquitination[1]
1590ESSEKVGKETSELGGubiquitination[1, 2]
1665RLSVFLKKQEESQFHubiquitination[1]
1811DAEGLPKKFVDIFQQubiquitination[1, 2, 3]
1872WSCTRKLKAASEAPEubiquitination[1]
1949MLTRNTLKPSPQAWLubiquitination[1, 2]
2030EHVFLLDKCLRENSDubiquitination[1]
2039LRENSDVKTHGPFEAubiquitination[1]
2055MRTLCECKETASKTLubiquitination[1, 2]
2060ECKETASKTLSRFGIubiquitination[1]
2078SICLGDAKDPVCLPCubiquitination[1]
2188QRHCEHTKSLSPFNDubiquitination[1]
2199PFNDVVDKTPVIRSVubiquitination[1]
2279EEEGRFLKAYSPASRubiquitination[1, 2, 3]
2329GPEMAKEKQCYLQQVubiquitination[1]
2337QCYLQQVKQFCIRVEubiquitination[1]
2370EFVQGLSKPGRPHQWubiquitination[1]
2385VFPKDVVKQQGLRQDubiquitination[1, 2]
2408LVYGDEYKALRDAVAubiquitination[1, 3]
2416ALRDAVAKAVLECKPubiquitination[1]
2422AKAVLECKPLGIKTAubiquitination[1, 3]
2427ECKPLGIKTALKACKubiquitination[1]
2475EQCEAVSKFIGECKIubiquitination[1]
2481SKFIGECKILSPPDIubiquitination[1, 3]
2568LAQARRWKGLERVHWubiquitination[1]
2620RDGFHLVKDKADRTQubiquitination[1]
2744FDTELSTKEMRNNWEubiquitination[1, 3]
2752EMRNNWEKEIAAVISubiquitination[1]
2767PELEHLDKTLPTMNNubiquitination[1]
2780NNLISQDKRISSNPVubiquitination[1]
2789ISSNPVAKIIYGDPVubiquitination[1, 3]
2847ILWHFLQKEAELRLVubiquitination[1]
2855EAELRLVKFLPEILAubiquitination[1]
2869ALQRDLVKQFQNVQQubiquitination[1]
2888SIRGFLSKHSSDGLRubiquitination[1]
2926NGEINLPKDYCSTDLubiquitination[5]
2973EIVYAVEKLSKENNSubiquitination[1]
2976YAVEKLSKENNSYSVubiquitination[1]
3028VQEFDLEKIQRQIVSubiquitination[1]
3041VSRFLQGKPRLSLKGubiquitination[1]
3047GKPRLSLKGIPTLVYubiquitination[1, 2]
3070LFMDIKNKMAQDSLPubiquitination[1]
3168EQLLRLHKEPFGEISubiquitination[1]
3179GEISSRYKADLSPENubiquitination[1]
3215EMIILKLKNPQTQTEubiquitination[1]
3274WKTAAVLKWNREMR*ubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Metal-binding; Nucleotide-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3280 AA 
Protein Sequence
MVCDGDWEHC YLPSAFSQHK VFVTPQAPLE AIQAYLAGHY RVPKQTLSAA AVFNDRLCVG 60
IVASERAGVG KSLYVKRLHD KMKMQLNVKN VPLKTIRLID PQVDESRVLG ALLPFLDAQY 120
QKVPVLFHLD VTSSVQTGIW VFLFKLLILQ YLMDINGKMW LRNPCHLYIV EILERRTSVP 180
SRSSSALRTR VPQFSFLDIF PKVTCRPPKE VIDMELSALR SDTEPGMDLW EFCSETFQRP 240
YQYLRRFNQN QDLDTFQYQE GSVEGTPEEC LQHFLFHCGV INPSWSELRN FARFLNYQLR 300
DCEASLFCNP SFIGDTLRGF KKFVVTFMIF MARDFATPSL HTSDQSPGKH MVTMDGVREE 360
DLAPFSLRKR WESEPHPYVF FNDDHTTMTF IGFHLQPNIN GSVDAISHLT GKVIKRDVMT 420
RDLYQGLLLQ RVPFNVDFDK LPRHKKLERL CLTLGIPQAT DPDKTYELTT DNMLKILAIE 480
MRFRCGIPVI IMGETGCGKT RLIKFLSDLR RGGTNADTIK LVKVHGGTTA DMIYSRVREA 540
ENVAFANKDQ HQLDTILFFD EANTTEAISC IKEVLCDHMV DGQPLAEDSG LHIIAACNPY 600
RKHSEEMICR LESAGLGYRV SMEETADRLG SIPLRQLVYR VHALPPSLIP LVWDFGQLSD 660
VAEKLYIQQI VQRLVESISL DENGTRVITE VLCASQGFMR KTEDECSFVS LRDVERCVKV 720
FRWFHEHSAM LLAQLNAFLS KSSVSKNHTE RDPVLWSLML AIGVCYHASL EKKDSYRKAI 780
ARFFPKPYDD SRLLLDEITR AQDLFLDGVP LRKTIAKNLA LKENVFMMVV CIELKIPLFL 840
VGKPGSSKSL AKTIVADAMQ GPAAYSDLFR SLKQVHLVSF QCSPHSTPQG IISTFRQCAR 900
FQQGKDLQQY VSVVVLDEVG LAEDSPKMPL KTLHPLLEDG CIEDDPAPHK KVGFVGISNW 960
ALDPAKMNRG IFVSRGSPNE TELIESAKGI CSSDILVQDR VQGYFASFAK AYETVCKRQD 1020
KEFFGLRDYY SLIKMVFAAA KASNRKPSPQ DIAQAVLRNF SGKDDIQALD IFLANLPEAK 1080
CSEEVSPMQL IKQNIFGPSQ KVPGGEQEDA ESRYLLVLTK NYVALQILQQ TFFEGDQQPE 1140
IIFGSGFPKD QEYTQLCRNI NRVKICMETG KMVLLLNLQN LYESLYDALN QYYVHLGGQK 1200
YVDLGLGTHR VKCRVHPNFR LIVIEEKDVV YKHFPIPLIN RLEKHYLDIN TVLEKWQKSI 1260
VEELCAWVEK FINVKAHHFQ KRHKYSPSDV FIGYHSDACA SVVLQVIERQ GPRALTEELH 1320
QKVSEEAKSI LLNCATPDAV VRLSAYSLGG FAAEWLSQEY FHRQRHNSFA DFLQAHLHTA 1380
DLERHAIFTE ITTFSRLLTS HDCEILESEV TGRAPKPTLL WLQQFDTEYS FLKEVRNCLT 1440
NTAKCKILIF QTDFEDGIRS AQLIASAKYS VINEINKIRE NEDRIFVYFI TKLSRVGRGT 1500
AYVGFHGGLW QSVHIDDLRR STLMVSDVTR LQHVTISQLF APGDLPELGL EHRAEDGHEE 1560
AMETEASTSG EVAEVAEEAM ETESSEKVGK ETSELGGSDV SILDTTRLLR SCVQSAVGML 1620
RDQNESCTRN MRRVVLLLGL LNEDDACHAS FLRVSKMRLS VFLKKQEESQ FHPLEWLARE 1680
ACNQDALQEA GTFRHTLWKR VQGAVTPLLA SMISFIDRDG NLELLTRPDT PPWARDLWMF 1740
IFSDTMLLNI PLVMNNERHK GEMAYIVVQN HMNLSENASN NVPFSWKIKD YLEELWVQAQ 1800
YITDAEGLPK KFVDIFQQTP LGRFLAQLHG EPQQELLQCY LKDFILLTMR VSTEEELKFL 1860
QMALWSCTRK LKAASEAPEE EVSLPWVHLA YQRFRSRLQN FSRILTIYPQ VLHSLMEARW 1920
NHELAGCEMT LDAFAAMACT EMLTRNTLKP SPQAWLQLVK NLSMPLELIC SDEHMQGSGS 1980
LAQAVIREVR AQWSRIFSTA LFVEHVLLGT ESRVPELQGL VTEHVFLLDK CLRENSDVKT 2040
HGPFEAVMRT LCECKETASK TLSRFGIQPC SICLGDAKDP VCLPCDHVHC LRCLRAWFAS 2100
EQMICPYCLT ALPDEFSPAV SQAHREAIEK HARFRQMCNS FFVDLVSTIC FKDNAPPEKE 2160
VIESLLSLLF VQKGRLRDAA QRHCEHTKSL SPFNDVVDKT PVIRSVILKL LLKYSFHDVK 2220
DYIQEYLTLL KKKAFITEDK TELYMLFINC LEDSILEKTS AYSRNDELNH LEEEGRFLKA 2280
YSPASRGREP ANEASVEYLQ EVARIRLCLD RAADFLSEPE GGPEMAKEKQ CYLQQVKQFC 2340
IRVENDWHRV YLVRKLSSQR GMEFVQGLSK PGRPHQWVFP KDVVKQQGLR QDHPGQMDRY 2400
LVYGDEYKAL RDAVAKAVLE CKPLGIKTAL KACKTPQSQQ SAYFLLTLFR EVAILYRSHN 2460
ASLHPTPEQC EAVSKFIGEC KILSPPDISR FATSLVDNSV PLLRAGPSDS NLDGTVTEMA 2520
IHAAAVLLCG QNELLEPLKN LAFSPATMAH AFLPTMPEDL LAQARRWKGL ERVHWYTCPN 2580
GHPCSVGECG RPMEQSICID CHAPIGGIDH KPRDGFHLVK DKADRTQTGH VLGNPQRRDV 2640
VTCDRGLPPV VFLLIRLLTH LALLLGASQS SQALINIIKP PVRDPKGFLQ QHILKDLEQL 2700
AKMLGHSADE TIGVVHLVLR RLLQEQHQLS SRRLLNFDTE LSTKEMRNNW EKEIAAVISP 2760
ELEHLDKTLP TMNNLISQDK RISSNPVAKI IYGDPVTFLP HLPRKSVVHC SKIWSCRKRI 2820
TVEYLQHIVE QKNGKERVPI LWHFLQKEAE LRLVKFLPEI LALQRDLVKQ FQNVQQVEYS 2880
SIRGFLSKHS SDGLRQLLHN RITVFLSTWN KLRRSLETNG EINLPKDYCS TDLDLDTEFE 2940
ILLPRRRGLG LCATALVSYL IRLHNEIVYA VEKLSKENNS YSVDAAEVTE LHVISYEVER 3000
DLTPLILSNC QYQVEEGRET VQEFDLEKIQ RQIVSRFLQG KPRLSLKGIP TLVYRHDWNY 3060
EHLFMDIKNK MAQDSLPSSV ISAISGQLQS YSDACEVLSV VEVTLGFLST AGGDPNMQLN 3120
VYTQDILQMG DQTIHVLKAL NRCQLKHTIA LWQFLSAHKS EQLLRLHKEP FGEISSRYKA 3180
DLSPENAKLL STFLNQTGLD AFLLELHEMI ILKLKNPQTQ TEERFRPQWS LRDTLVSYMQ 3240
TKESEILPEM ASQFPEEILL ASCVSVWKTA AVLKWNREMR 3280 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR027417; P-loop_NTPase.
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00097; zf-C3HC4 
SMART
 SM00382; AAA
 SM00184; RING 
PROSITE
 PS50089; ZF_RING_2 
PRINTS