CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022859
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase kappa 
Protein Synonyms/Alias
 DINB protein; DINP 
Gene Name
 POLK 
Gene Synonyms/Alias
 DINB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38LDKEKINKIIMEATKubiquitination[1]
45KIIMEATKGSRFYGNubiquitination[1]
55RFYGNELKKEKQVNQubiquitination[1]
56FYGNELKKEKQVNQRubiquitination[1]
71IENMMQQKAQITSQQubiquitination[1]
158AMPGFIAKRLCPQLIubiquitination[1]
173IVPPNFDKYRAVSKEubiquitination[1, 2]
224DKRRYFIKMGSSVENubiquitination[1]
236VENDNPGKEVNKLSEubiquitination[1]
240NPGKEVNKLSEHERSubiquitination[1]
326LAKVCSDKNKPNGQYubiquitination[1]
328KVCSDKNKPNGQYQIubiquitination[1]
347QAVMDFIKDLPIRKVubiquitination[1]
359RKVSGIGKVTEKMLKubiquitination[1]
427RTFSEINKAEEQYSLubiquitination[1]
448ELAQDLQKERLKGRTubiquitination[1]
461RTVTIKLKNVNFEVKubiquitination[1]
468KNVNFEVKTRASTVSubiquitination[1]
523FPNEEDRKHQQRSIIubiquitination[1]
576DKKRSERKWSHQDTFubiquitination[1]
584WSHQDTFKCEAVNKQubiquitination[1]
603SQPFQVLKKKMNENLubiquitination[1]
604QPFQVLKKKMNENLEubiquitination[1]
605PFQVLKKKMNENLEIubiquitination[1]
641ISLEALNKHVDECLDubiquitination[1]
683PASSLCEKQDYEAHPubiquitination[1]
693YEAHPKIKEISSVDCubiquitination[1]
722SIDALSNKHSKEECSubiquitination[1]
734ECSSLPSKSFNIEHCubiquitination[1]
772QPYLCEVKTGQALVCubiquitination[1]
814IQELRKDKFNPVNQPubiquitination[1]
822FNPVNQPKESSRSTGubiquitination[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] 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] 
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. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. 
Sequence Annotation
 DOMAIN 103 358 UmuC.
 ZN_FING 621 647 UBZ-type 1.
 ZN_FING 776 802 UBZ-type 2.
 METAL 107 107 Magnesium (By similarity).
 METAL 198 198 Magnesium (By similarity).
 METAL 199 199 Magnesium (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Repeat; Schiff base; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 870 AA 
Protein Sequence
MDSTKEKCDS YKDDLLLRMG LNDNKAGMEG LDKEKINKII MEATKGSRFY GNELKKEKQV 60
NQRIENMMQQ KAQITSQQLR KAQLQVDRFA MELEQSRNLS NTIVHIDMDA FYAAVEMRDN 120
PELKDKPIAV GSMSMLSTSN YHARRFGVRA AMPGFIAKRL CPQLIIVPPN FDKYRAVSKE 180
VKEILADYDP NFMAMSLDEA YLNITKHLEE RQNWPEDKRR YFIKMGSSVE NDNPGKEVNK 240
LSEHERSISP LLFEESPSDV QPPGDPFQVN FEEQNNPQIL QNSVVFGTSA QEVVKEIRFR 300
IEQKTTLTAS AGIAPNTMLA KVCSDKNKPN GQYQILPNRQ AVMDFIKDLP IRKVSGIGKV 360
TEKMLKALGI ITCTELYQQR ALLSLLFSET SWHYFLHISL GLGSTHLTRD GERKSMSVER 420
TFSEINKAEE QYSLCQELCS ELAQDLQKER LKGRTVTIKL KNVNFEVKTR ASTVSSVVST 480
AEEIFAIAKE LLKTEIDADF PHPLRLRLMG VRISSFPNEE DRKHQQRSII GFLQAGNQAL 540
SATECTLEKT DKDKFVKPLE MSHKKSFFDK KRSERKWSHQ DTFKCEAVNK QSFQTSQPFQ 600
VLKKKMNENL EISENSDDCQ ILTCPVCFRA QGCISLEALN KHVDECLDGP SISENFKMFS 660
CSHVSATKVN KKENVPASSL CEKQDYEAHP KIKEISSVDC IALVDTIDNS SKAESIDALS 720
NKHSKEECSS LPSKSFNIEH CHQNSSSTVS LENEDVGSFR QEYRQPYLCE VKTGQALVCP 780
VCNVEQKTSD LTLFNVHVDV CLNKSFIQEL RKDKFNPVNQ PKESSRSTGS SSGVQKAVTR 840
TKRPGLMTKY STSKKIKPNN PKHTLDIFFK 870 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:UniProtKB. 
Interpro
 IPR017961; DNA_pol_Y-fam_little_finger.
 IPR001126; DNA_repair_prot_UmuC-like.
 IPR017963; DNA_repair_prot_UmuC-like_N.
 IPR022880; DNApol_IV.
 IPR024728; PolY_HhH_motif.
 IPR006642; Znf_Rad18_put. 
Pfam
 PF00817; IMS
 PF11799; IMS_C
 PF11798; IMS_HHH 
SMART
 SM00734; ZnF_Rad18 
PROSITE
 PS50173; UMUC 
PRINTS