DPOE3_HUMAN
ID DPOE3_HUMAN Reviewed; 147 AA.
AC Q9NRF9; Q5W0U1; Q8N758; Q8NCE5; Q9NR32;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA polymerase epsilon subunit 3;
DE AltName: Full=Arsenic-transactivated protein;
DE Short=AsTP;
DE AltName: Full=Chromatin accessibility complex 17 kDa protein;
DE Short=CHRAC-17;
DE Short=HuCHRAC17;
DE AltName: Full=DNA polymerase II subunit 3;
DE AltName: Full=DNA polymerase epsilon subunit p17;
GN Name=POLE3; Synonyms=CHRAC17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE CHRAC ISWI CHROMATIN
RP REMODELING COMPLEX, INTERACTION WITH SMARCA5; BAZ1A AND CHRAC1, AND TISSUE
RP SPECIFICITY.
RX PubMed=10880450; DOI=10.1093/emboj/19.13.3377;
RA Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V.,
RA Becker P.B., Bickmore W.A., Varga-Weisz P.D.;
RT "HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two
RT novel histone-fold proteins.";
RL EMBO J. 19:3377-3387(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 63-77 AND 81-86,
RP FUNCTION, AND IDENTIFICATION IN EPSILON DNA POLYMERASE COMPLEX.
RC TISSUE=Cervix carcinoma;
RX PubMed=10801849; DOI=10.1074/jbc.m002548200;
RA Li Y., Pursell Z.F., Linn S.;
RT "Identification and cloning of two histone fold motif-containing subunits
RT of HeLa DNA polymerase epsilon.";
RL J. Biol. Chem. 275:23247-23252(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu S.-H., Cheng J., Liu Y., Zheng Y.-J., Zhang Y.-X., Xie Q., Guo J.;
RT "Screening and cloning of target genes differential expressed in HepG2
RT cells treated with arsenic trioxide by suppression subtractive
RT hybridization technique.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-83 AND ASP-135.
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-17 AND 40-58, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP INTERACTION WITH BAZ1A.
RX PubMed=12434153; DOI=10.1038/ng1046;
RA Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G.,
RA Varga-Weisz P.D.;
RT "An ACF1-ISWI chromatin-remodeling complex is required for DNA replication
RT through heterochromatin.";
RL Nat. Genet. 32:627-632(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH SMARCA5 AND BAZ1A.
RX PubMed=14759371; DOI=10.1016/s1097-2765(03)00523-9;
RA Kukimoto I., Elderkin S., Grimaldi M., Oelgeschlager T., Varga-Weisz P.D.;
RT "The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding
RT and assembly mediated by ACF.";
RL Mol. Cell 13:265-277(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex
CC (PubMed:10801849). Participates in DNA repair and in chromosomal DNA
CC replication (By similarity). Forms a complex with CHRAC1 and binds
CC naked DNA, which is then incorporated into chromatin, aided by the
CC nucleosome-remodeling activity of ISWI/SNF2H and ACF1
CC (PubMed:10801849). Does not enhance nucleosome sliding activity of the
CC ACF-5 ISWI chromatin remodeling complex (PubMed:14759371).
CC {ECO:0000250|UniProtKB:Q04603, ECO:0000269|PubMed:10801849,
CC ECO:0000269|PubMed:14759371}.
CC -!- SUBUNIT: Component of the DNA polymerase epsilon complex consisting of
CC four subunits: the catalytic subunit POLE and the accessory subunits
CC POLE2, POLE3 and POLE4. Interaction with POLE4 is a prerequisite for
CC further binding with POLE and POLE2. Heterodimer with CHRAC1; binds to
CC DNA (PubMed:10880450). Component of the CHRAC ISWI chromatin remodeling
CC complex at least composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and
CC POLE3; the complex preferentially binds DNA through the CHRAC1-POLE3
CC heterodimer and possesses ATP-dependent nucleosome-remodeling activity
CC (PubMed:10880450). Within the complex, the heterodimer with CHRAC1
CC interacts with SMARCA5/SNF2H; the interaction is direct and enhances
CC nucleosome sliding activity by the SMARCA5/SNF2H and BAZ1A/ACF1
CC interaction (PubMed:10880450, PubMed:14759371). Within the complex, the
CC heterodimer with CHRAC1 interacts with BAZ1A/ACF1; the interactions are
CC direct (PubMed:10880450, PubMed:12434153, PubMed:14759371).
CC {ECO:0000269|PubMed:10801849, ECO:0000269|PubMed:10880450,
CC ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:14759371}.
CC -!- INTERACTION:
CC Q9NRF9; Q9NRG0: CHRAC1; NbExp=13; IntAct=EBI-744901, EBI-2795492;
CC Q9NRF9; Q658N3: DKFZp666G145; NbExp=3; IntAct=EBI-744901, EBI-10240005;
CC Q9NRF9; Q01658: DR1; NbExp=7; IntAct=EBI-744901, EBI-750300;
CC Q9NRF9; Q14919: DRAP1; NbExp=7; IntAct=EBI-744901, EBI-712941;
CC Q9NRF9; Q9NR33: POLE4; NbExp=6; IntAct=EBI-744901, EBI-867034;
CC Q9NRF9; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-744901, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10880450}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pole3/";
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DR EMBL; AF226077; AAF72417.1; -; mRNA.
DR EMBL; AF261689; AAF90133.1; -; Genomic_DNA.
DR EMBL; AY720898; AAU15052.1; -; mRNA.
DR EMBL; AK074629; BAC11099.1; -; mRNA.
DR EMBL; AK074762; BAC11190.1; -; mRNA.
DR EMBL; AK074782; BAC11206.1; -; mRNA.
DR EMBL; DQ072116; AAY57326.1; -; Genomic_DNA.
DR EMBL; AL137066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003166; AAH03166.1; -; mRNA.
DR EMBL; BC004170; AAH04170.1; -; mRNA.
DR CCDS; CCDS6795.1; -.
DR RefSeq; NP_001265184.1; NM_001278255.1.
DR RefSeq; NP_059139.3; NM_017443.4.
DR AlphaFoldDB; Q9NRF9; -.
DR SMR; Q9NRF9; -.
DR BioGRID; 119903; 73.
DR ComplexPortal; CPX-2108; DNA polymerase epsilon complex.
DR ComplexPortal; CPX-785; CHRAC chromatin remodeling complex.
DR CORUM; Q9NRF9; -.
DR IntAct; Q9NRF9; 11.
DR MINT; Q9NRF9; -.
DR STRING; 9606.ENSP00000363286; -.
DR ChEMBL; CHEMBL2363042; -.
DR DrugBank; DB00242; Cladribine.
DR GlyGen; Q9NRF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRF9; -.
DR PhosphoSitePlus; Q9NRF9; -.
DR SwissPalm; Q9NRF9; -.
DR BioMuta; POLE3; -.
DR DMDM; 22653710; -.
DR EPD; Q9NRF9; -.
DR jPOST; Q9NRF9; -.
DR MassIVE; Q9NRF9; -.
DR MaxQB; Q9NRF9; -.
DR PaxDb; Q9NRF9; -.
DR PeptideAtlas; Q9NRF9; -.
DR PRIDE; Q9NRF9; -.
DR ProteomicsDB; 82350; -.
DR TopDownProteomics; Q9NRF9; -.
DR Antibodypedia; 15326; 219 antibodies from 29 providers.
DR DNASU; 54107; -.
DR Ensembl; ENST00000374169.7; ENSP00000363284.3; ENSG00000148229.13.
DR Ensembl; ENST00000374171.5; ENSP00000363286.4; ENSG00000148229.13.
DR GeneID; 54107; -.
DR KEGG; hsa:54107; -.
DR MANE-Select; ENST00000374171.5; ENSP00000363286.4; NM_017443.5; NP_059139.3.
DR UCSC; uc004bhn.4; human.
DR CTD; 54107; -.
DR DisGeNET; 54107; -.
DR GeneCards; POLE3; -.
DR HGNC; HGNC:13546; POLE3.
DR HPA; ENSG00000148229; Low tissue specificity.
DR MIM; 607267; gene.
DR neXtProt; NX_Q9NRF9; -.
DR OpenTargets; ENSG00000148229; -.
DR PharmGKB; PA33499; -.
DR VEuPathDB; HostDB:ENSG00000148229; -.
DR eggNOG; KOG0870; Eukaryota.
DR GeneTree; ENSGT00940000161417; -.
DR HOGENOM; CLU_066247_7_2_1; -.
DR InParanoid; Q9NRF9; -.
DR OMA; KQNHRTI; -.
DR OrthoDB; 1572458at2759; -.
DR PhylomeDB; Q9NRF9; -.
DR TreeFam; TF103008; -.
DR BRENDA; 2.7.7.7; 2681.
DR PathwayCommons; Q9NRF9; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-68952; DNA replication initiation.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; Q9NRF9; -.
DR SIGNOR; Q9NRF9; -.
DR BioGRID-ORCS; 54107; 195 hits in 1096 CRISPR screens.
DR ChiTaRS; POLE3; human.
DR GeneWiki; POLE3; -.
DR GenomeRNAi; 54107; -.
DR Pharos; Q9NRF9; Tbio.
DR PRO; PR:Q9NRF9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NRF9; protein.
DR Bgee; ENSG00000148229; Expressed in gastrocnemius and 200 other tissues.
DR ExpressionAtlas; Q9NRF9; baseline and differential.
DR Genevisible; Q9NRF9; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; TAS:ProtInc.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:BHF-UCL.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT CHAIN 2..147
FT /note="DNA polymerase epsilon subunit 3"
FT /id="PRO_0000208341"
FT REGION 93..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..146
FT /evidence="ECO:0000255"
FT COMPBIAS 93..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VARIANT 83
FT /note="T -> A (in dbSNP:rs36023979)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023464"
FT VARIANT 126
FT /note="D -> A (in dbSNP:rs34852828)"
FT /id="VAR_057527"
FT VARIANT 135
FT /note="E -> D (in dbSNP:rs35933626)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023465"
FT CONFLICT 58
FT /note="K -> N (in Ref. 3; AAU15052 and 4; BAC11206)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="T -> I (in Ref. 4; BAC11190)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="D -> Y (in Ref. 2; AAF90133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16860 MW; DC0A4D2097046569 CRC64;
MAERPEDLNL PNAVITRIIK EALPDGVNIS KEARSAISRA ASVFVLYATS CANNFAMKGK
RKTLNASDVL SAMEEMEFQR FVTPLKEALE AYRREQKGKK EASEQKKKDK DKKTDSEEQD
KSRDEDNDED EERLEEEEQN EEEEVDN
