CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034577
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 DNA polymerase 
Protein Synonyms/Alias
  
Gene Name
 Pole 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
130KFQGKIAKLENVPKEacetylation[1]
1179LEKNDIYKQKKISELacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; DNA replication; DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2283 AA 
Protein Sequence
MVLRNSGRRH PEPGADSEGS RDDGPSSSVS ALKRLERSQW TDKMDLRFGF ERLKEPGERT 60
GWLINMHPTE ILDEDKRLVS AVDYYFIQDD GSRFKVALPY KPYFYIAARK GCDREVSSFL 120
SKKFQGKIAK LENVPKEDLD LPNHLVGLKR SYIKLSFHTV EDLVKVRKEI SPAVKKNREQ 180
DHASDEYTTM LSSILQGGSL ITDEEETSKK IADQLDNIVD MREYDVPYHI RLSIDLRIHV 240
AHWYNVRFRG NAFPVEIARR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI 300
DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE VHLIQRWFEH IQETKPTIMV 360
TYNGDFFDWP FVEARAAIHG LSMYQEIGFQ KDSQGEYKAP QCIHMDCLRW VKRDSYLPVG 420
SHNLKAAAKA KLGYDPVELD PEDMCRMATE QPQTLATYSV SDAVATYYLY MKYVHPFIFA 480
LCTIIPMEPD EVLRKGSGTL CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDAETYV 540
GGHVEALESG VFRSDIPCRF RMNPAAFDFL LQRVEKTMRH AIEEEEKVPV EQATNFQEVC 600
EQIKTKLTSL KDVPNRIECP LIYHLDVGAM YPNIILTNRL QPSAIVDEAT CAACDFNKPG 660
ATCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLFP EGPARAFHEL SREEQAKYEK 720
RRLADYCRKA YKKIHMTKVE ERLTTICQRE NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS 780
AAVEVGDASE VKRCKNMEIL YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA 840
NIITQARELI EQIGRPLELD TDGIWCVLPN SFPENFVIKT TNVKKPKLTI SYPGAMLNIM 900
VKEGFTNHQY QELTEPSSLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK KLKKRYAVFN 960
EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE EVYASVAKVA DYWLDVLYSK 1020
AANMPDSELF ELISENRSMS RKLEDYGEQK STSISTAKRL AEFLGDQMVK DAGLSCRYII 1080
SRKPEGSPVT ERAIPLAIFQ AEPTVRKHFL RKWLKSSSLQ DFDIRTILDW DYYIERLGSA 1140
IQKIITIPAA LQQVKNPVPR VKHPDWLHKK LLEKNDIYKQ KKISELFVLE GKRQIVMAQA 1200
SENSLSLCTP DMEDFGLTKP YHSTVPVATK RKRVWESQKE SQDITLTVPW QEVLGQPPSL 1260
GTTQEEWLVW LQFHKKKWQL QAQQRLARRK KQRLESAEDM PRLGAIREGP ATGLGSFLRR 1320
TARSIMDLPW QIIQISETRQ AGLFRLWAII GSDLHCIKLS IPRVFYVNQR VAKAEDGPSY 1380
RKVNRALPRS NIVYNLYEYS VPEDMYQEHI NEINTELSAP DIEGVYETQV PLLFRALVQL 1440
GCVCVVNKQL ARQLSGWEAE TFALEHLEMR SLAQFSYLEP GSIRHIYLYH HTQGHKALFG 1500
VFIPSQRRAS VFVLDTVRSN QMPGLSALYS AEHSLLLDKV GPNLLPPPKH TFEVRAETNL 1560
KTICRAIQRF LLAYKEERRG PTLIAIQSSW ELCRLTSEIP VLEEFPLVPV RVADKISYAV 1620
LDWQRHGARR MIRHYLNLDI CLSQAFEMSR YFHIPVGNLP EDISTFGSDL FFARHLQRHN 1680
HLLWLSPTSR PDLGGKEADD NRLVMEFDDR ATVEINNSGC YSTVCVELDI QNLAVNTILQ 1740
SHHVNDMEGA GSMGISFDVI QQASLEDMVT GNQAASALAS YDETALCSST FRILKSMVVG 1800
WVKEITQYHN IYADNQVMHF YRWLQSPCSL LHDPALHRTL HNMMKKLFLQ LIAEFKRLGS 1860
SVIYANFNRI ILCTKKRRIE DALAYVEYIT NSIHSKEIFH SLTISFSRCW EFLLWMDPSN 1920
YGGIKGKVPS SIHCGQVREQ DSQTREETED EEDNEKDEEE EEDMGQSEVE DLLENNWNIL 1980
QFLPQAASCQ SYFLMIVSAY IVAVYQSMKD ELRHSAPGST PVKRKGASQF SQEAEGAAGA 2040
LPGMITFSQD YVANELTQTF FTITQKIQKK VTGSRNTAEP SEMFPVLPGS HLLLNNPALE 2100
FIKYVCKVLS LDTNITNQVN KLNRDLLRLV DVGEFSEEAQ FRDPCHSYVL PEVICHSCNF 2160
CRDLDLCKDS SFSQDGAILP QWLCSNCQAP YDSSAIESAL VEALQRKLMA FTLQDLVCLK 2220
CRGMKETHMP VYCGCAGDFV LTIHTEVFME QIRIFQNIAK YYNMSYLQEA IEWLLQTSPV 2280
SNF 2283 
Gene Ontology
 GO:0008622; C:epsilon DNA polymerase complex; IEA:Compara.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006287; P:base-excision repair, gap-filling; IEA:Compara.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
 GO:0000731; P:DNA synthesis involved in DNA repair; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEP:RGD.
 GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:Compara. 
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