CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022117
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RAD18 
Protein Synonyms/Alias
 Postreplication repair protein RAD18; hHR18; hRAD18; RING finger protein 73 
Gene Name
 RAD18 
Gene Synonyms/Alias
 RNF73 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17PPGLAVMKTIDDLLRubiquitination[1, 2]
52YCSLCIRKFLSYKTQubiquitination[1]
57IRKFLSYKTQCPTCCubiquitination[1]
73TVTEPDLKNNRILDEubiquitination[1, 3, 4]
83RILDELVKSLNFARNubiquitination[1, 3, 5, 6]
102FALESPAKSPASSSSubiquitination[1, 2, 3, 5, 6]
110SPASSSSKNLAVKVYubiquitination[1, 2, 3, 4, 6]
115SSKNLAVKVYTPVASubiquitination[1, 2, 3, 4, 5, 6]
151STSELLIKENKSKFSubiquitination[1, 2, 3, 4, 5, 6]
161KSKFSPQKEASPAAKubiquitination[1, 5, 6]
168KEASPAAKTKETRSVubiquitination[6]
186APDPSEAKRPEPPSTubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
197PPSTSTLKQVTKVDCubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
201STLKQVTKVDCPVCGubiquitination[1]
218IPESHINKHLDSCLSubiquitination[1, 4, 5, 8]
229SCLSREEKKESLRSSubiquitination[1]
245HKRKPLPKTVYNLLSubiquitination[5]
257LLSDRDLKKKLKEHGubiquitination[1, 6]
258LSDRDLKKKLKEHGLubiquitination[1]
259SDRDLKKKLKEHGLSubiquitination[1]
261RDLKKKLKEHGLSIQubiquitination[1, 3, 4, 5, 6]
271GLSIQGNKQQLIKRHubiquitination[1, 5, 6]
309REIENIEKTRMRLEAubiquitination[2, 4, 5, 6, 7, 8, 9]
318RMRLEASKLNESVMVubiquitination[1, 5, 6, 9, 10, 11]
328ESVMVFTKDQTEKEIubiquitination[1, 2, 5, 6, 10, 11]
333FTKDQTEKEIDEIHSubiquitination[1, 6, 10, 11]
341EIDEIHSKYRKKHKSubiquitination[1, 10, 11]
347SKYRKKHKSEFQLLVubiquitination[1, 6, 10]
362DQARKGYKKIAGMSQubiquitination[6]
370KIAGMSQKTVTITKEubiquitination[1, 2, 5, 11]
376QKTVTITKEDESTEKubiquitination[1, 6]
383KEDESTEKLSSVCMGubiquitination[1]
462EAWEASHKNDLQDTEubiquitination[6, 8, 10]
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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [8] 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]
 [9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [10] 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]
 [11] 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] 
Functional Description
 E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap- filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono- ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity. 
Sequence Annotation
 DOMAIN 248 282 SAP.
 ZN_FING 25 64 RING-type.
 ZN_FING 201 224 UBZ-type.
 MOTIF 232 240 LR motif.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 103 103 Phosphoserine.
 MOD_RES 118 118 Phosphothreonine.
 MOD_RES 164 164 Phosphoserine.
 MOD_RES 471 471 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; DNA damage; DNA repair; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 495 AA 
Protein Sequence
MDSLAESRWP PGLAVMKTID DLLRCGICFE YFNIAMIIPQ CSHNYCSLCI RKFLSYKTQC 60
PTCCVTVTEP DLKNNRILDE LVKSLNFARN HLLQFALESP AKSPASSSSK NLAVKVYTPV 120
ASRQSLKQGS RLMDNFLIRE MSGSTSELLI KENKSKFSPQ KEASPAAKTK ETRSVEEIAP 180
DPSEAKRPEP PSTSTLKQVT KVDCPVCGVN IPESHINKHL DSCLSREEKK ESLRSSVHKR 240
KPLPKTVYNL LSDRDLKKKL KEHGLSIQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI 300
VREIENIEKT RMRLEASKLN ESVMVFTKDQ TEKEIDEIHS KYRKKHKSEF QLLVDQARKG 360
YKKIAGMSQK TVTITKEDES TEKLSSVCMG QEDNMTSVTN HFSQSKLDSP EELEPDREED 420
SSSCIDIQEV LSSSESDSCN SSSSDIIRDL LEEEEAWEAS HKNDLQDTEI SPRQNRRTRA 480
AESAEIEPRN KRNRN 495 
Gene Ontology
 GO:0000785; C:chromatin; IEA:Compara.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0005657; C:replication fork; IDA:UniProtKB.
 GO:0001741; C:XY body; IEA:Compara.
 GO:0003684; F:damaged DNA binding; NAS:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
 GO:0000403; F:Y-form DNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; NAS:UniProtKB.
 GO:0045910; P:negative regulation of DNA recombination; IEA:Compara.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0009411; P:response to UV; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR003034; SAP_dom.
 IPR006642; Znf_Rad18_put.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF02037; SAP 
SMART
 SM00184; RING
 SM00513; SAP
 SM00734; ZnF_Rad18 
PROSITE
 PS50800; SAP
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS