CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037083
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54ERSQWTDKMDLRFGFubiquitination[1]
87TEILDEDKRLGSAVDubiquitination[1]
133EVSSFLSKKFQGKIAubiquitination[1]
134VSSFLSKKFQGKIAKubiquitination[1]
160PNHLVGLKRNYIRLSubiquitination[1]
220TDEEETSKKIADQLDubiquitination[2, 3]
221DEEETSKKIADQLDNubiquitination[1]
402QQEIGFQKDSQGEYKubiquitination[1]
436PVGSHNLKAAAKAKLubiquitination[1]
442LKAAAKAKLGYDPVEubiquitination[1]
669CAACDFNKPGANCQRubiquitination[1]
677PGANCQRKMAWQWRGubiquitination[1]
803VGDAAEVKRCKNMEVubiquitination[1]
980DGSLAELKGFEVKRRubiquitination[1]
1061LEDYGEQKSTSISTAubiquitination[2, 4]
1081FLGDQMVKDAGLSCRubiquitination[1]
1166PAALQQVKNPVPRVKubiquitination[1]
1185LHKKLLEKNDVYKQKubiquitination[1]
1385YVNQRVAKAEEGASYubiquitination[1]
1573VRAETDLKTICRAIQubiquitination[1]
2121EFIKYVCKVLSLDTNubiquitination[5]
2135NITNQVNKLNRDLLRubiquitination[1, 2, 3, 5, 6, 7]
2234LQDLVCLKCRGVKETubiquitination[3]
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] 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]
 [4] 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]
 [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] 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]
 [7] 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
  
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
 2297 AA 
Protein Sequence
MSRPLGLKSF PRHKQAPLPL SLTFHGCLLL RRDDGATSSV SALKRLERSQ WTDKMDLRFG 60
FERLKEPGEK TGWLINMHPT EILDEDKRLG SAVDYYFIQD DGSRFKVALP YKPYFYIATR 120
KGCEREVSSF LSKKFQGKIA KVETVPKEDL DLPNHLVGLK RNYIRLSFHT VEDLVKVRKE 180
ISPAVKKNRE QDHASDAYTA LLSSVLQRGG VITDEEETSK KIADQLDNIV DMREYDVPYH 240
IRLSIDLKIH VAHWYNVRYR GNAFPVEITR RDDLVERPDP VVLAFDIETT KLPLKFPDAE 300
TDQIMMISYM IDGQGYLITN REIVSEDIED FEFTPKPEYE GPFCVFNEPD EAHLIQRWFE 360
HVQETKPTIM VTYNGDFFDW PFVEARAAVH GLSMQQEIGF QKDSQGEYKA PQCIHMDCLR 420
WVKRDSYLPV GSHNLKAAAK AKLGYDPVEL DPEDMCRMAT EQPQTLATYS VSDAVATYYL 480
YMKYVHPFIF ALCTIIPMEP DEVLRKGSGT LCEALLMVQA FHANIIFPNK QEQEFNKLTD 540
DGHVLDSETY VGGHVEALES GVFRSDIPCR FRMNPAAFDF LLQRVEKTLR HALEEEEKVP 600
VEQVTNFEEV CDEIKSKLAS LKDVPSRIEC PLIYHLDVGA MYPNIILTNR LQPSAMVDEA 660
TCAACDFNKP GANCQRKMAW QWRGEFMPAS RSEYHRIQHQ LESEKFPPLF PEGPARAFHE 720
LSREEQAKYE KRRLADYCRK AYKKIHITKV EERLTTICQR ENSFYVDTVR AFRDRRYEFK 780
GLHKVWKKKL SAAVEVGDAA EVKRCKNMEV LYDSLQLAHK CILNSFYGYV MRKGARWYSM 840
EMAGIVCFTG ANIITQAREL IEQIGRPLEL DTDGIWCVLP NSFPENFVFK TTNVKKPKVT 900
ISYPGAMLNI MVKEGFTNDQ YQELAEPSSL TYVTRSENSI FFEVDGPYLA MILPASKEEG 960
KKLKKRYAVF NEDGSLAELK GFEVKRRGEL QLIKIFQSSV FEAFLKGSTL EEVYGSVAKV 1020
ADYWLDVLYS KAANMPDSEL FELISENRSM SRKLEDYGEQ KSTSISTAKR LAEFLGDQMV 1080
KDAGLSCRYI ISRKPEGSPV TERAIPLAIF QAEPTVRKHF LRKWLKSSSL QDFDIRAILD 1140
WDYYIERLGS AIQKIITIPA ALQQVKNPVP RVKHPDWLHK KLLEKNDVYK QKKISELFTL 1200
EGRRQVTMAE ASEDSPRPSA PDMEDFGLVK LPHPAAPVTV KRKRVLWESQ EESQDLTPTV 1260
PWQEILGQPP ALGTSQEEWL VWLRFHKKKW QLQARQRLAR RKRQRLESAE GVLRPGAIRD 1320
GPATGLGSFL RRTARSILDL PWQIVQISET SQAGLFRLWA LVGSDLHCIR LSIPRVFYVN 1380
QRVAKAEEGA SYRKVNRVLP RSNMVYNLYE YSVPEDMYQE HINEINAELS APDIEGVYET 1440
QVPLLFRALV HLGCVCVVNK QLVRHLSGWE AETFALEHLE MRSLAQFSYL EPGSIRHIYL 1500
YHHAQAHKAL FGIFIPSQRR ASVFVLDTVR SNQMPSLGAL YSAEHGLLLE KVGPELLPPP 1560
KHTFEVRAET DLKTICRAIQ RFLLAYKEER RGPTLIAVQS SWELKRLASE IPVLEEFPLV 1620
PICVADKINY GVLDWQRHGA RRMIRHYLNL DTCLSQAFEM SRYFHIPIGN LPEDISTFGS 1680
DLFFARHLQR HNHLLWLSPT ARPDLGGKEA DDNCLVMEFD DQATVEINSS GCYSTVCVEL 1740
DLQNLAVNTI LQSHHVNDME GADSMGISFD VIQQASLEDM ITGGQAASAP ASYDETALCS 1800
NTFRILKSMV VGWVKEITQY HNIYADNQVM HFYRWLRSPS SLLHDPALHR TLHNMMKKLF 1860
LQLIAEFKRL GSSVIYANFN RIILCTKKRR VEDAIAYVEY ITSSIHSKET FHSLTISFSR 1920
CWEFLLWMDP SNYGGIKGKV SSRIHCGLQD SQKAGGAEDE QENEDDEEER DGEEEEEAEE 1980
SNVEDLLENN WNILQFLPQA ASCQNYFLMI VSAYIVAVYH CMKDGLRRSA PGSTPVRRRG 2040
ASQLSQEAEG AVGALPGMIT FSQDYVANEL TQSFFTITQK IQKKVTGSRN STELSEMFPV 2100
LPGSHLLLNN PALEFIKYVC KVLSLDTNIT NQVNKLNRDL LRLVDVGEFS EEAQFRDPCR 2160
SYVLPEVICR SCNFCRDLDL CKDSSFSEDG AVLPQWLCSN CQAPYDSSAI EMTLVEVLQK 2220
KLMAFTLQDL VCLKCRGVKE TSMPVYCSCA GDFALTIHTQ VFMEQIGIFR NIAQHYGMSY 2280
LLETLEWLLQ KNPQLGH 2297 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 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:0006260; P:DNA replication; IEA:UniProtKB-KW. 
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