CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029153
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 DNA polymerase 
Protein Synonyms/Alias
  
Gene Name
 POLA1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
136VKKLAVTKPNNIKSMacetylation[1]
936KQVKQLMKQQDLNPDubiquitination[2]
976SYSRFYAKPLAALVTubiquitination[3, 4]
1081YVTKQELKGLDIVRRacetylation[1]
1206YAPEQLQKQDNLTIDubiquitination[2, 5, 6]
1382PLCPACMKATLQPEYubiquitination[2, 7]
1425HEKDKLKKQFFTPKVubiquitination[2]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] 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
  
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
 1468 AA 
Protein Sequence
MAPVHGDDCE IGASALSDSG SFVSSRARRE KKSKKGRQEA LERLKKAKAG EKYKYEVEDF 60
TGVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI FDDDLEDDAL DADEKGKDGK 120
ARNKDKRNVK KLAVTKPNNI KSMFIACAGK KTADKAVDLS KDGLLGDILQ DLNTETPQIT 180
PPPVMILKKK RSIGASPNPF SVHTATAVPS GKIASPVSRK EPPLTPVPLK RAEFAGDDVQ 240
VESTEEEQES GAMEFEDGDF DEPMEVEEVD LEPMAAKAWD KESEPAEEVK QEADSGKGTV 300
SYLGSFLPDV SCWDIDQEGD SSFSVQEVQV DSSHLPLVKG ADEEQVFHFY WLDAYEDQYN 360
QPGVVFLFGK VWIESAETHV SCCVMVKNIE RTLYFLPREM KIDLNTGKET GTPISMKDVY 420
EEFDEKIATK YKIMKFKSKP VEKNYAFEIP DVPEKSEYLE VKYSAEMPQL PQDLKGETFS 480
HVFGTNTSSL ELFLMNRKIK GPCWLEVKSP QLLNQPVSWC KVEAMALKPD LVNVIKDVSP 540
PPLVVMAFSM KTMQNAKNHQ NEIIAMAALV HHSFALDKAA PKPPFQSHFC VVSKPKDCIF 600
PYAFKEVIEK KNVKVEVAAT ERTLLGFFLA KVHKIDPDII VGHNIYGFEL EVLLQRINVC 660
KAPHWSKIGR LKRSNMPKLG GRSGFGERNA TCGRMICDVE ISAKELIRCK SYHLSELVQQ 720
ILKTERVVIP MENIQNMYSE SSQLLYLLEH TWKDAKFILQ IMCELNVLPL ALQITNIAGN 780
IMSRTLMGGR SERNEFLLLH AFYENNYIVP DKQIFRKPQQ KLGDEDEEID GDTNKYKKGR 840
KKAAYAGGLV LDPKVGFYDK FILLLDFNSL YPSIIQEFNI CFTTVQRVAS EAQKVTEDGE 900
QEQIPELPDP SLEMGILPRE IRKLVERRKQ VKQLMKQQDL NPDLILQYDI RQKALKLTAN 960
SMYGCLGFSY SRFYAKPLAA LVTYKGREIL MHTKEMVQKM NLEVIYGDTD SIMINTNSTN 1020
LEEVFKLGNK VKSEVNKLYK LLEIDIDGVF KSLLLLKKKK YAALVVEPTS DGNYVTKQEL 1080
KGLDIVRRDW CDLAKDTGNF VIGQILSDQS RDTIVENIQK RLIEIGENVL NGSVPVSQFE 1140
INKALTKDPQ DYPDKKSLPH VHVALWINSQ GGRKVKAGDT VSYVICQDGS NLTASQRAYA 1200
PEQLQKQDNL TIDTQYYLAQ QIHPVVARIC EPIDGIDAVL IATWLGLDPT QFRVHHYHKD 1260
EENDALLGGP AQLTDEEKYR DCERFKCPCP TCGTENIYDN VFDGSGTDME PSLYRCSNID 1320
CKASPLTFTV QLSNKLIMDI RRFIKKYYDG WLICEEPTCR NRTRHLPLQF SRTGPLCPAC 1380
MKATLQPEYS DKSLYTQLCF YRYIFDAECA LEKLTTDHEK DKLKKQFFTP KVLQDYRKLK 1440
NTAEQFLSRS GYSEVNLSKL FAGCAVKS 1468 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
 GO:0001882; F:nucleoside binding; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 
Interpro
 IPR006172; DNA-dir_DNA_pol_B.
 IPR017964; DNA-dir_DNA_pol_B_CS.
 IPR006133; DNA-dir_DNA_pol_B_exonuc.
 IPR006134; DNA-dir_DNA_pol_B_multi_dom.
 IPR004578; DNA-dir_DNA_pol_B_pol2.
 IPR024647; DNA_pol_a_cat_su_N.
 IPR023211; DNA_pol_palm_dom.
 IPR012337; RNaseH-like_dom.
 IPR015088; Znf_DNA-dir_DNA_pol_B_alpha. 
Pfam
 PF12254; DNA_pol_alpha_N
 PF00136; DNA_pol_B
 PF03104; DNA_pol_B_exo1
 PF08996; zf-DNA_Pol 
SMART
 SM00486; POLBc 
PROSITE
 PS00116; DNA_POLYMERASE_B 
PRINTS
 PR00106; DNAPOLB.