CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase eta 
Protein Synonyms/Alias
 RAD30 homolog A; Xeroderma pigmentosum variant type protein 
Gene Name
 POLH 
Gene Synonyms/Alias
 RAD30; RAD30A; XPV 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32QNPHLRNKPCAVVQYubiquitination[1]
70MWADDAKKLCPDLLLubiquitination[1]
91RGKANLTKYREASVEubiquitination[1]
131AVQERLQKLQGQPISubiquitination[2]
224SHNKVLAKLACGLNKubiquitination[1]
231KLACGLNKPNRQTLVubiquitination[1]
311GIEHDPVKPRQLPKTubiquitination[1]
462PVTSSEAKTQGSGPAubiquitination[1, 2]
486SLESFFQKAAERQKVubiquitination[1]
682SAVSHQGKRNPKSPLubiquitination[1, 2, 3, 4, 5, 6]
686HQGKRNPKSPLACTNubiquitination[1, 6]
694SPLACTNKRPRPEGMubiquitination[6]
709QTLESFFKPLTH***ubiquitination[6]
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] 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] 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] 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] 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]
 [6] 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] 
Functional Description
 DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci. 
Sequence Annotation
 DOMAIN 9 259 UmuC.
 METAL 13 13 Magnesium (By similarity).
 METAL 115 115 Magnesium (By similarity).
 CROSSLNK 682 682 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 686 686 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 694 694 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 709 709 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Isopeptide bond; Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Schiff base; Transferase; Ubl conjugation; Xeroderma pigmentosum. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 713 AA 
Protein Sequence
MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV SYEARAFGVT 60
RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM EIMSRFAVIE RASIDEAYVD 120
LTSAVQERLQ KLQGQPISAD LLPSTYIEGL PQGPTTAEET VQKEGMRKQG LFQWLDSLQI 180
DNLTSPDLQL TVGAVIVEEM RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH 240
GSVPQLFSQM PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA 300
MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE RLTKDRNDND 360
RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF TVIKNCNTSG IQTEWSPPLT 420
MLFLCATKFS ASAPSSSTDI TSFLSSDPSS LPKVPVTSSE AKTQGSGPAV TATKKATTSL 480
ESFFQKAAER QKVKEASLSS LTAPTQAPMS NSPSKPSLPF QTSQSTGTEP FFKQKSLLLK 540
QKQLNNSSVS SPQQNPWSNC KALPNSLPTE YPGCVPVCEG VSKLEESSKA TPAEMDLAHN 600
SQSMHASSAS KSVLEVTQKA TPNPSLLAAE DQVPCEKCGS LVPVWDMPEH MDYHFALELQ 660
KSFLQPHSSN PQVVSAVSHQ GKRNPKSPLA CTNKRPRPEG MQTLESFFKP LTH 713 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003684; F:damaged DNA binding; TAS:ProtInc.
 GO:0003887; F:DNA-directed DNA polymerase activity; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0000731; P:DNA synthesis involved in DNA repair; IDA:UniProtKB.
 GO:0006301; P:postreplication repair; IEA:Compara.
 GO:0006290; P:pyrimidine dimer repair; IEA:Compara.
 GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
 GO:0010225; P:response to UV-C; IDA:UniProtKB. 
Interpro
 IPR017061; DNA_pol_eta.
 IPR017961; DNA_pol_Y-fam_little_finger.
 IPR001126; DNA_repair_prot_UmuC-like.
 IPR017963; DNA_repair_prot_UmuC-like_N. 
Pfam
 PF00817; IMS
 PF11799; IMS_C 
SMART
  
PROSITE
 PS50173; UMUC 
PRINTS