CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008829
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase subunit gamma-1 
Protein Synonyms/Alias
 Mitochondrial DNA polymerase catalytic subunit; PolG-alpha 
Gene Name
 POLG 
Gene Synonyms/Alias
 MDP1; POLG1; POLGA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
109RSVEHLQKHGLWGQPubiquitination[1]
316RSLWIAAKQGKHKVQubiquitination[1]
371VGGPPLEKEPRELFVubiquitination[1, 2, 3]
379EPRELFVKGTMKDIRubiquitination[1]
383LFVKGTMKDIRENFQubiquitination[1]
551MARACLQKLKGTTELubiquitination[1]
553RACLQKLKGTTELLPubiquitination[1]
633GRRDNLAKLPTGTTLubiquitination[1]
755WFFKLPHKDGNSCNVubiquitination[1]
768NVGSPFAKDFLPKMEubiquitination[1]
773FAKDFLPKMEDGTLQubiquitination[1, 2]
796PRALEINKMISFWRNubiquitination[1]
934RGTDLHSKTATTVGIubiquitination[1, 2, 3]
947GISREHAKIFNYGRIubiquitination[1]
981TQQEAAEKAQQMYAAubiquitination[1, 2, 4]
990QQMYAATKGLRWYRLubiquitination[1, 2, 4]
1040ARKSQWKKWEVVAERubiquitination[1]
1050VVAERAWKGGTESEMubiquitination[1]
1060TESEMFNKLESIATSubiquitination[1, 2, 4]
1191DIDRCLRKEVTMDCKubiquitination[1]
1198KEVTMDCKTPSNPTGubiquitination[1, 3, 5]
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] 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]
 [3] 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]
 [4] 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]
 [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] 
Functional Description
 Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Disease mutation; DNA replication; DNA-binding; DNA-directed DNA polymerase; Leigh syndrome; Magnesium; Mitochondrion; Mitochondrion nucleoid; Neurodegeneration; Neuropathy; Nucleotidyltransferase; Polymorphism; Progressive external ophthalmoplegia; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1239 AA 
Protein Sequence
MSRLLWRKVA GATVGPGPVP APGRWVSSSV PASDPSDGQR RRQQQQQQQQ QQQQQPQQPQ 60
VLSSEGGQLR HNPLDIQMLS RGLHEQIFGQ GGEMPGEAAV RRSVEHLQKH GLWGQPAVPL 120
PDVELRLPPL YGDNLDQHFR LLAQKQSLPY LEAANLLLQA QLPPKPPAWA WAEGWTRYGP 180
EGEAVPVAIP EERALVFDVE VCLAEGTCPT LAVAISPSAW YSWCSQRLVE ERYSWTSQLS 240
PADLIPLEVP TGASSPTQRD WQEQLVVGHN VSFDRAHIRE QYLIQGSRMR FLDTMSMHMA 300
ISGLSSFQRS LWIAAKQGKH KVQPPTKQGQ KSQRKARRGP AISSWDWLDI SSVNSLAEVH 360
RLYVGGPPLE KEPRELFVKG TMKDIRENFQ DLMQYCAQDV WATHEVFQQQ LPLFLERCPH 420
PVTLAGMLEM GVSYLPVNQN WERYLAEAQG TYEELQREMK KSLMDLANDA CQLLSGERYK 480
EDPWLWDLEW DLQEFKQKKA KKVKKEPATA SKLPIEGAGA PGDPMDQEDL GPCSEEEEFQ 540
QDVMARACLQ KLKGTTELLP KRPQHLPGHP GWYRKLCPRL DDPAWTPGPS LLSLQMRVTP 600
KLMALTWDGF PLHYSERHGW GYLVPGRRDN LAKLPTGTTL ESAGVVCPYR AIESLYRKHC 660
LEQGKQQLMP QEAGLAEEFL LTDNSAIWQT VEELDYLEVE AEAKMENLRA AVPGQPLALT 720
ARGGPKDTQP SYHHGNGPYN DVDIPGCWFF KLPHKDGNSC NVGSPFAKDF LPKMEDGTLQ 780
AGPGGASGPR ALEINKMISF WRNAHKRISS QMVVWLPRSA LPRAVIRHPD YDEEGLYGAI 840
LPQVVTAGTI TRRAVEPTWL TASNARPDRV GSELKAMVQA PPGYTLVGAD VDSQELWIAA 900
VLGDAHFAGM HGCTAFGWMT LQGRKSRGTD LHSKTATTVG ISREHAKIFN YGRIYGAGQP 960
FAERLLMQFN HRLTQQEAAE KAQQMYAATK GLRWYRLSDE GEWLVRELNL PVDRTEGGWI 1020
SLQDLRKVQR ETARKSQWKK WEVVAERAWK GGTESEMFNK LESIATSDIP RTPVLGCCIS 1080
RALEPSAVQE EFMTSRVNWV VQSSAVDYLH LMLVAMKWLF EEFAIDGRFC ISIHDEVRYL 1140
VREEDRYRAA LALQITNLLT RCMFAYKLGL NDLPQSVAFF SAVDIDRCLR KEVTMDCKTP 1200
SNPTGMERRY GIPQGEALDI YQIIELTKGS LEKRSQPGP 1239 
Gene Ontology
 GO:0005760; C:gamma DNA polymerase complex; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; IDA:MGI.
 GO:0004527; F:exonuclease activity; IEA:Compara.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006287; P:base-excision repair, gap-filling; IDA:MGI.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0006261; P:DNA-dependent DNA replication; TAS:ProtInc.
 GO:0006264; P:mitochondrial DNA replication; IEA:Compara. 
Interpro
 IPR019760; DNA-dir_DNA_pol_A_CS.
 IPR002297; DNA-dir_DNA_pol_A_mt.
 IPR016265; DNA-dir_DNA_pol_A_mt_sub.
 IPR001098; DNA-dir_DNA_pol_A_palm_dom.
 IPR012337; RNaseH-like_dom. 
Pfam
 PF00476; DNA_pol_A 
SMART
 SM00482; POLAc 
PROSITE
 PS00447; DNA_POLYMERASE_A 
PRINTS
 PR00867; DNAPOLG.