CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016323
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase DZIP3 
Protein Synonyms/Alias
 DAZ-interacting protein 3; RNA-binding ubiquitin ligase of 138 kDa; hRUL138 
Gene Name
 DZIP3 
Gene Synonyms/Alias
 KIAA0675 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
151ALTERGKKEDYTEAEubiquitination[1]
212SLQEIGDKNDHWFDIubiquitination[2]
248TTESNIMKQTICSYLubiquitination[3]
311NDQSFSGKKCLKEGCubiquitination[2]
315FSGKKCLKEGCTGDMubiquitination[3]
372TDTDIRPKISLKFNTubiquitination[2]
376IRPKISLKFNTKDEMubiquitination[2]
380ISLKFNTKDEMPIFKubiquitination[2]
485NVFPAPKKGWNMEPPubiquitination[3]
703HSVSRLIKDDASDVQubiquitination[2]
738IEQGSAGKVTTDYGEubiquitination[2]
748TDYGETEKERLARQRubiquitination[2, 3]
768HYQCEDFKRQLRTVTubiquitination[3]
786QENQMQIKKKDKIIAubiquitination[2]
821HAKDNEIKNLKEQLSubiquitination[3]
824DNEIKNLKEQLSMKRubiquitination[2, 3]
830LKEQLSMKRSQWEMEubiquitination[3]
838RSQWEMEKHNLESTMubiquitination[3]
846HNLESTMKTYVSKLNubiquitination[2, 3, 4, 5, 6]
851TMKTYVSKLNAETSRubiquitination[2, 3]
883LHLEQTEKECLNQLAubiquitination[1, 3]
936QYNEQINKVKQGFALubiquitination[2, 3]
1042ERITDRLKTAFPQQTubiquitination[2, 4, 5]
1051AFPQQTRKELTDFLRubiquitination[2, 3, 4, 5, 7]
1061TDFLRKLKDAYGKSLubiquitination[3]
1087ISQFIDPKKSQSQGKubiquitination[2, 3]
1088SQFIDPKKSQSQGKSubiquitination[3]
Reference
 [1] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [2] 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]
 [3] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [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] 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
 E3 Ubiquitin ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Able to specifically bind RNA. 
Sequence Annotation
 ZN_FING 1148 1188 RING-type; atypical.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Reference proteome; RNA-binding; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1208 AA 
Protein Sequence
MDSLPDEFFV RHPAVEDQRK EETENKLEKS SGQLNKQEND IPTDLVPVNL LLEVKKLLNA 60
INTLPKGVVP HIKKFLQEDF SFQTMQREVA ANSQNGEEIV PALTLRFLIT QLEAALRNIQ 120
AGNYTAHQIN IGYYLTLLFL YGVALTERGK KEDYTEAENK FLVMKMMIQE NEICENFMSL 180
VYFGRGLLRC AQKRYNGGLL EFHKSLQEIG DKNDHWFDID PTEDEDLPTT FKDLLNNFIK 240
TTESNIMKQT ICSYLDCERS CEADILKNTS YKGFFQLMCS KSCCVYFHKI CWKKFKNLKY 300
PGENDQSFSG KKCLKEGCTG DMVRMLQCDV PGIVKILFEV VRKDEYITIE NLGASYRKLI 360
SLKITDTDIR PKISLKFNTK DEMPIFKLDY NYFYHLLHII IISGTDIVRQ IFDEAMPPPL 420
LKKELLIHKN VLESYYNHLW TNHPLGGSWH LLYPPNKELP QSKQFDLCLL LALIKHLNVF 480
PAPKKGWNME PPSSDISKSA DILRLCKYRD ILLSEILMNG LTESQFNSIW KKVSDILLRL 540
GMMQEDIDKV KENPIENISL DYHQLSVYLG IPVPEIIQRM LSCYQQGIAL QSITGSQRIE 600
IEELQNEEEE LSPPLMEYNI NVKSHPEIQF AEINKDGTSI PSESSTESLK DLQEVKSKQR 660
KKKKTKNKKN KDSKEDQVPY VVEKEEQLRK EQANPHSVSR LIKDDASDVQ EDSAMEDKFY 720
SLDELHILDM IEQGSAGKVT TDYGETEKER LARQRQLYKL HYQCEDFKRQ LRTVTFRWQE 780
NQMQIKKKDK IIASLNQQVA FGINKVSKLQ RQIHAKDNEI KNLKEQLSMK RSQWEMEKHN 840
LESTMKTYVS KLNAETSRAL TAEVYFLQCR RDFGLLHLEQ TEKECLNQLA RVTHMAASNL 900
ESLQLKAAVD SWNAIVADVR NKIAFLRTQY NEQINKVKQG FALSTLPPVQ LPPPPPSPEI 960
LMQQFLGRPL VKESFFRPIL TVPQMPAVCP GVVSATGQPR APLMTGIAWA LPAPVGDAVP 1020
PSAGLRSDPS IMNWERITDR LKTAFPQQTR KELTDFLRKL KDAYGKSLSE LTFDEIVCKI 1080
SQFIDPKKSQ SQGKSVSNVN CVSPSHSPSQ PDAAQPPKPA WRPLTSQGPA TWEGASNPDE 1140
EEEEEEPCVI CHENLSPENL SVLPCAHKFH AQCIRPWLMQ QGTCPTCRLH VLLPEEFPGH 1200
PSRQLPKI 1208 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0019902; F:phosphatase binding; IDA:UniProtKB.
 GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS