CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011533
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase epsilon catalytic subunit A 
Protein Synonyms/Alias
 DNA polymerase II subunit A 
Gene Name
 POLE 
Gene Synonyms/Alias
 POLE1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
209TDEEETSKKIADQLDubiquitination[1]
2110EFIKYVCKVLSLDTNubiquitination[2]
2124NITNQVNKLNRDLLRubiquitination[1, 2]
2223LQDLVCLKCRGVKETubiquitination[1]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Participates in DNA repair and in chromosomal DNA replication. 
Sequence Annotation
 ZN_FING 2158 2190 CysA-type.
 MOTIF 2221 2238 CysB motif.
 METAL 2158 2158 Zinc (By similarity).
 METAL 2161 2161 Zinc (By similarity).
 METAL 2187 2187 Zinc (By similarity).
 METAL 2190 2190 Zinc (By similarity).
 METAL 2221 2221 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 2224 2224 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 2236 2236 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 2238 2238 Iron-sulfur (4Fe-4S) (By similarity).
 MOD_RES 1184 1184 Phosphoserine.
 MOD_RES 1940 1940 Phosphoserine.  
Keyword
 4Fe-4S; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2286 AA 
Protein Sequence
MSLRSGGRRR ADPGADGEAS RDDGATSSVS ALKRLERSQW TDKMDLRFGF ERLKEPGEKT 60
GWLINMHPTE ILDEDKRLGS AVDYYFIQDD GSRFKVALPY KPYFYIATRK GCEREVSSFL 120
SKKFQGKIAK VETVPKEDLD LPNHLVGLKR NYIRLSFHTV EDLVKVRKEI SPAVKKNREQ 180
DHASDAYTAL LSSVLQRGGV ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLKIHV 240
AHWYNVRYRG NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI 300
DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE AHLIQRWFEH VQETKPTIMV 360
TYNGDFFDWP FVEARAAVHG LSMQQEIGFQ KDSQGEYKAP QCIHMDCLRW VKRDSYLPVG 420
SHNLKAAAKA KLGYDPVELD PEDMCRMATE QPQTLATYSV SDAVATYYLY MKYVHPFIFA 480
LCTIIPMEPD EVLRKGSGTL CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDSETYV 540
GGHVEALESG VFRSDIPCRF RMNPAAFDFL LQRVEKTLRH ALEEEEKVPV EQVTNFEEVC 600
DEIKSKLASL KDVPSRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT CAACDFNKPG 660
ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP EGPARAFHEL SREEQAKYEK 720
RRLADYCRKA YKKIHITKVE ERLTTICQRE NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS 780
AAVEVGDAAE VKRCKNMEVL YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA 840
NIITQARELI EQIGRPLELD TDGIWCVLPN SFPENFVFKT TNVKKPKVTI SYPGAMLNIM 900
VKEGFTNDQY QELAEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK KLKKRYAVFN 960
EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE EVYGSVAKVA DYWLDVLYSK 1020
AANMPDSELF ELISENRSMS RKLEDYGEQK STSISTAKRL AEFLGDQMVK DAGLSCRYII 1080
SRKPEGSPVT ERAIPLAIFQ AEPTVRKHFL RKWLKSSSLQ DFDIRAILDW DYYIERLGSA 1140
IQKIITIPAA LQQVKNPVPR VKHPDWLHKK LLEKNDVYKQ KKISELFTLE GRRQVTMAEA 1200
SEDSPRPSAP DMEDFGLVKL PHPAAPVTVK RKRVLWESQE ESQDLTPTVP WQEILGQPPA 1260
LGTSQEEWLV WLRFHKKKWQ LQARQRLARR KRQRLESAEG VLRPGAIRDG PATGLGSFLR 1320
RTARSILDLP WQIVQISETS QAGLFRLWAL VGSDLHCIRL SIPRVFYVNQ RVAKAEEGAS 1380
YRKVNRVLPR SNMVYNLYEY SVPEDMYQEH INEINAELSA PDIEGVYETQ VPLLFRALVH 1440
LGCVCVVNKQ LVRHLSGWEA ETFALEHLEM RSLAQFSYLE PGSIRHIYLY HHAQAHKALF 1500
GIFIPSQRRA SVFVLDTVRS NQMPSLGALY SAEHGLLLEK VGPELLPPPK HTFEVRAETD 1560
LKTICRAIQR FLLAYKEERR GPTLIAVQSS WELKRLASEI PVLEEFPLVP ICVADKINYG 1620
VLDWQRHGAR RMIRHYLNLD TCLSQAFEMS RYFHIPIGNL PEDISTFGSD LFFARHLQRH 1680
NHLLWLSPTA RPDLGGKEAD DNCLVMEFDD QATVEINSSG CYSTVCVELD LQNLAVNTIL 1740
QSHHVNDMEG ADSMGISFDV IQQASLEDMI TGGQAASAPA SYDETALCSN TFRILKSMVV 1800
GWVKEITQYH NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL QLIAEFKRLG 1860
SSVIYANFNR IILCTKKRRV EDAIAYVEYI TSSIHSKETF HSLTISFSRC WEFLLWMDPS 1920
NYGGIKGKVS SRIHCGLQDS QKAGGAEDEQ ENEDDEEERD GEEEEEAEES NVEDLLENNW 1980
NILQFLPQAA SCQNYFLMIV SAYIVAVYHC MKDGLRRSAP GSTPVRRRGA SQLSQEAEGA 2040
VGALPGMITF SQDYVANELT QSFFTITQKI QKKVTGSRNS TELSEMFPVL PGSHLLLNNP 2100
ALEFIKYVCK VLSLDTNITN QVNKLNRDLL RLVDVGEFSE EAQFRDPCRS YVLPEVICRS 2160
CNFCRDLDLC KDSSFSEDGA VLPQWLCSNC QAPYDSSAIE MTLVEVLQKK LMAFTLQDLV 2220
CLKCRGVKET SMPVYCSCAG DFALTIHTQV FMEQIGIFRN IAQHYGMSYL LETLEWLLQK 2280
NPQLGH 2286 
Gene Ontology
 GO:0008622; C:epsilon DNA polymerase complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IDA:UniProtKB.
 GO:0003887; F:DNA-directed DNA polymerase activity; IMP:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006287; P:base-excision repair, gap-filling; IDA:UniProtKB.
 GO:0006270; P:DNA replication initiation; TAS:Reactome.
 GO:0000731; P:DNA synthesis involved in DNA repair; IMP:UniProtKB.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:UniProtKB.
 GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
 GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome. 
Interpro
 IPR006172; DNA-dir_DNA_pol_B.
 IPR006133; DNA-dir_DNA_pol_B_exonuc.
 IPR006134; DNA-dir_DNA_pol_B_multi_dom.
 IPR013697; DNA_pol_e_suA_C.
 IPR012337; RNaseH-like_dom. 
Pfam
 PF00136; DNA_pol_B
 PF03104; DNA_pol_B_exo1
 PF08490; DUF1744 
SMART
 SM00486; POLBc 
PROSITE
  
PRINTS