CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000977
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA polymerase zeta catalytic subunit 
Protein Synonyms/Alias
 Protein reversionless 3-like; REV3-like; hREV3 
Gene Name
 REV3L 
Gene Synonyms/Alias
 POLZ; REV3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
300PATESEKKFQKRLQEubiquitination[1]
924YTLRAKRKVNYETEDacetylation[2]
942SFVTHNSKISLPHPMacetylation[2]
960ESLDGTLKSRKRRKMacetylation[2]
1582RSVTSPRKPRTPRSTacetylation[3]
2508LSDWFDNKTDLYRWKubiquitination[4, 5]
2868DSCPAVSKILERSLKmethylation[6]
3087EQLVKICKNCTGCFDubiquitination[1]
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] Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics.
 Yang YY, Grammel M, Hang HC.
 Bioorg Med Chem Lett. 2011 Sep 1;21(17):4976-9. [PMID: 21669532]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] 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]
 [5] 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]
 [6] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510
Functional Description
 Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis. 
Sequence Annotation
 ZN_FING 3042 3057 CysA-type.
 REGION 1847 1898 Mediates interaction with MAD2L2.
 MOTIF 3086 3104 CysB motif.
 METAL 3042 3042 Zinc (By similarity).
 METAL 3045 3045 Zinc (By similarity).
 METAL 3054 3054 Zinc (By similarity).
 METAL 3057 3057 Zinc (By similarity).
 METAL 3086 3086 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 3089 3089 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 3099 3099 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 3104 3104 Iron-sulfur (4Fe-4S) (By similarity).
 MOD_RES 1030 1030 Phosphoserine.
 MOD_RES 1041 1041 Phosphothreonine.  
Keyword
 3D-structure; 4Fe-4S; Alternative splicing; Complete proteome; 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
 3130 AA 
Protein Sequence
MFSVRIVTAD YYMASPLQGL DTCQSPLTQA PVKKVPVVRV FGATPAGQKT CLHLHGIFPY 60
LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER 120
HFMKIYLYNP TMVKRICELL QSGAIMNKFY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV 180
KFRKARRKSN TLHATGSCKN HLSGNSLADT LFRWEQDEIP SSLILEGVEP QSTCELEVDA 240
VAADILNRLD IEAQIGGNPG LQAIWEDEKQ RRRNRNETSQ MSQPESQDHR FVPATESEKK 300
FQKRLQEILK QNDFSVTLSG SVDYSDGSQE FSAELTLHSE VLSPEMLQCT PANMVEVHKD 360
KESSKGHTRH KVEEALINEE AILNLMENSQ TFQPLTQRLS ESPVFMDSSP DEALVHLLAG 420
LESDGYRGER NRMPSPCRSF GNNKYPQNSD DEENEPQIEK EEMELSLVMS QRWDSNIEEH 480
CAKKRSLCRN THRSSTEDDD SSSGEEMEWS DNSLLLASLS IPQLDGTADE NSDNPLNNEN 540
SRTHSSVIAT SKLSVKPSIF HKDAATLEPS SSAKITFQCK HTSALSSHVL NKEDLIEDLS 600
QTNKNTEKGL DNSVTSFTNE STYSMKYPGS LSSTVHSENS HKENSKKEIL PVSSCESSIF 660
DYEEDIPSVT RQVPSRKYTN IRKIEKDSPF IHMHRHPNEN TLGKNSFNFS DLNHSKNKVS 720
SEGNEKGNST ALSSLFPSSF TENCELLSCS GENRTMVHSL NSTADESGLN KLKIRYEEFQ 780
EHKTEKPSLS QQAAHYMFFP SVVLSNCLTR PQKLSPVTYK LQPGNKPSRL KLNKRKLAGH 840
QETSTKSSET GSTKDNFIQN NPCNSNPEKD NALASDLTKT TRGAFENKTP TDGFIDCHFG 900
DGTLETEQSF GLYGNKYTLR AKRKVNYETE DSESSFVTHN SKISLPHPME IGESLDGTLK 960
SRKRRKMSKK LPPVIIKYII INRFRGRKNM LVKLGKIDSK EKQVILTEEK MELYKKLAPL 1020
KDFWPKVPDS PATKYPIYPL TPKKSHRRKS KHKSAKKKTG KQQRTNNENI KRTLSFRKKR 1080
SHAILSPPSP SYNAETEDCD LNYSDVMSKL GFLSERSTSP INSSPPRCWS PTDPRAEEIM 1140
AAAEKEAMLF KGPNVYKKTV NSRIGKTSRA RAQIKKSKAK LANPSIVTKK RNKRNQTNKL 1200
VDDGKKKPRA KQKTNEKGTS RKHTTLKDEK IKSQSGAEVK FVLKHQNVSE FASSSGGSQL 1260
LFKQKDMPLM GSAVDHPLSA SLPTGINAQQ KLSGCFSSFL ESKKSVDLQT FPSSRDDLHP 1320
SVVCNSIGPG VSKINVQRPH NQSAMFTLKE STLIQKNIFD LSNHLSQVAQ NTQISSGMSS 1380
KIEDNANNIQ RNYLSSIGKL SEYRNSLESK LDQAYTPNFL HCKDSQQQIV CIAEQSKHSE 1440
TCSPGNTASE ESQMPNNCFV TSLRSPIKQI AWEQKQRGFI LDMSNFKPER VKPRSLSEAI 1500
SQTKALSQCK NRNVSTPSAF GEGQSGLAVL KELLQKRQQK AQNANTTQDP LSNKHQPNKN 1560
ISGSLEHNKA NKRTRSVTSP RKPRTPRSTK QKEKIPKLLK VDSLNLQNSS QLDNSVSDDS 1620
PIFFSDPGFE SCYSLEDSLS PEHNYNFDIN TIGQTGFCSF YSGSQFVPAD QNLPQKFLSD 1680
AVQDLFPGQA IEKNEFLSHD NQKCDEDKHH TTDSASWIRS GTLSPEIFEK STIDSNENRR 1740
HNQWKNSFHP LTTRSNSIMD SFCVQQAEDC LSEKSRLNRS SVSKEVFLSL PQPNNSDWIQ 1800
GHTRKEMGQS LDSANTSFTA ILSSPDGELV DVACEDLELY VSRNNDMLTP TPDSSPRSTS 1860
SPSQSKNGSF TPRTANILKP LMSPPSREEI MATLLDHDLS ETIYQEPFCS NPSDVPEKPR 1920
EIGGRLLMVE TRLANDLAEF EGDFSLEGLR LWKTAFSAMT QNPRPGSPLR SGQGVVNKGS 1980
SNSPKMVEDK KIVIMPCKCA PSRQLVQVWL QAKEEYERSK KLPKTKPTGV VKSAENFSSS 2040
VNPDDKPVVP PKMDVSPCIL PTTAHTKEDV DNSQIALQAP TTGCSQTASE SQMLPPVASA 2100
SDPEKDEDDD DNYYISYSSP DSPVIPPWQQ PISPDSKALN GDDRPSSPVE ELPSLAFENF 2160
LKPIKDGIQK SPCSEPQEPL VISPINTRAR TGKCESLCFH STPIIQRKLL ERLPEAPGLS 2220
PLSTEPKTQK LSNKKGSNTD TLRRVLLTQA KNQFAAVNTP QKETSQIDGP SLNNTYGFKV 2280
SIQNLQEAKA LHEIQNLTLI SVELHARTRR DLEPDPEFDP ICALFYCISS DTPLPDTEKT 2340
ELTGVIVIDK DKTVFSQDIR YQTPLLIRSG ITGLEVTYAA DEKALFHEIA NIIKRYDPDI 2400
LLGYEIQMHS WGYLLQRAAA LSIDLCRMIS RVPDDKIENR FAAERDEYGS YTMSEINIVG 2460
RITLNLWRIM RNEVALTNYT FENVSFHVLH QRFPLFTFRV LSDWFDNKTD LYRWKMVDHY 2520
VSRVRGNLQM LEQLDLIGKT SEMARLFGIQ FLHVLTRGSQ YRVESMMLRI AKPMNYIPVT 2580
PSVQQRSQMR APQCVPLIME PESRFYSNSV LVLDFQSLYP SIVIAYNYCF STCLGHVENL 2640
GKYDEFKFGC TSLRVPPDLL YQVRHDITVS PNGVAFVKPS VRKGVLPRML EEILKTRFMV 2700
KQSMKAYKQD RALSRMLDAR QLGLKLIANV TFGYTSANFS GRMPCIEVGD SIVHKARETL 2760
ERAIKLVNDT KKWGARVVYG DTDSMFVLLK GATKEQSFKI GQEIAEAVTA TNPKPVKLKF 2820
EKVYLPCVLQ TKKRYVGYMY ETLDQKDPVF DAKGIETVRR DSCPAVSKIL ERSLKLLFET 2880
RDISLIKQYV QRQCMKLLEG KASIQDFIFA KEYRGSFSYK PGACVPALEL TRKMLTYDRR 2940
SEPQVGERVP YVIIYGTPGV PLIQLVRRPV EVLQDPTLRL NATYYITKQI LPPLARIFSL 3000
IGIDVFSWYH ELPRIHKATS SSRSEPEGRK GTISQYFTTL HCPVCDDLTQ HGICSKCRSQ 3060
PQHVAVILNQ EIRELERQQE QLVKICKNCT GCFDRHIPCV SLNCPVLFKL SRVNRELSKA 3120
PYLRQLLDQF 3130 
Gene Ontology
 GO:0005694; C:chromosome; IBA:RefGenome.
 GO:0005634; C:nucleus; IBA:RefGenome.
 GO:0016035; C:zeta DNA polymerase complex; IDA:UniProtKB.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003887; F:DNA-directed DNA polymerase activity; IBA:RefGenome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0006261; P:DNA-dependent DNA replication; TAS:ProtInc.
 GO:0019985; P:translesion synthesis; IBA:RefGenome. 
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.
 IPR023211; DNA_pol_palm_dom.
 IPR012337; RNaseH-like_dom.
 IPR025687; Znf-C4pol. 
Pfam
 PF00136; DNA_pol_B
 PF03104; DNA_pol_B_exo1
 PF14260; zf-C4pol 
SMART
 SM00486; POLBc 
PROSITE
 PS00116; DNA_POLYMERASE_B 
PRINTS
 PR00106; DNAPOLB.