DPOE3_MOUSE
ID DPOE3_MOUSE Reviewed; 145 AA.
AC Q9JKP7; Q8R198;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DNA polymerase epsilon subunit 3;
DE AltName: Full=DNA polymerase II subunit 3;
DE AltName: Full=DNA polymerase epsilon subunit p17;
DE AltName: Full=NF-YB-like protein;
DE AltName: Full=YB-like protein 1;
DE Short=YBL1;
GN Name=Pole3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell lymphoma;
RX PubMed=11000277; DOI=10.1093/nar/28.19.3830;
RA Bolognese F., Imbriano C., Caretti G., Mantovani R.;
RT "Cloning and characterization of the histone-fold proteins YBL1 and YCL1.";
RL Nucleic Acids Res. 28:3830-3838(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Accessory component of the DNA polymerase epsilon complex (By
CC similarity). 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 (By similarity).
CC Does not enhance nucleosome sliding activity of the ACF-5 ISWI
CC chromatin remodeling complex (By similarity).
CC {ECO:0000250|UniProtKB:Q04603, ECO:0000250|UniProtKB:Q9NRF9}.
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 (By similarity). 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 (By similarity). 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 (By similarity). Within the complex, the heterodimer with
CC CHRAC1 interacts with BAZ1A/ACF1; the interactions are direct (By
CC similarity). {ECO:0000250|UniProtKB:Q9NRF9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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DR EMBL; AF230806; AAF67146.1; -; mRNA.
DR EMBL; BC024996; AAH24996.1; -; mRNA.
DR CCDS; CCDS18244.1; -.
DR RefSeq; NP_067473.2; NM_021498.2.
DR AlphaFoldDB; Q9JKP7; -.
DR SMR; Q9JKP7; -.
DR BioGRID; 208472; 4.
DR ComplexPortal; CPX-2109; DNA polymerase epsilon complex.
DR ComplexPortal; CPX-858; CHRAC chromatin remodeling complex.
DR IntAct; Q9JKP7; 1.
DR MINT; Q9JKP7; -.
DR STRING; 10090.ENSMUSP00000030091; -.
DR iPTMnet; Q9JKP7; -.
DR PhosphoSitePlus; Q9JKP7; -.
DR EPD; Q9JKP7; -.
DR MaxQB; Q9JKP7; -.
DR PaxDb; Q9JKP7; -.
DR PeptideAtlas; Q9JKP7; -.
DR PRIDE; Q9JKP7; -.
DR ProteomicsDB; 279569; -.
DR DNASU; 59001; -.
DR GeneID; 59001; -.
DR KEGG; mmu:59001; -.
DR UCSC; uc008tfb.1; mouse.
DR CTD; 54107; -.
DR MGI; MGI:1933378; Pole3.
DR eggNOG; KOG0870; Eukaryota.
DR InParanoid; Q9JKP7; -.
DR OrthoDB; 1572458at2759; -.
DR PhylomeDB; Q9JKP7; -.
DR TreeFam; TF103008; -.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-68952; DNA replication initiation.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR BioGRID-ORCS; 59001; 9 hits in 111 CRISPR screens.
DR PRO; PR:Q9JKP7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JKP7; protein.
DR GO; GO:0140672; C:ATAC complex; ISO:MGI.
DR GO; GO:0008623; C:CHRAC; IBA:GO_Central.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ComplexPortal.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
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; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT CHAIN 2..145
FT /note="DNA polymerase epsilon subunit 3"
FT /id="PRO_0000208342"
FT REGION 92..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..144
FT /evidence="ECO:0000255"
FT COMPBIAS 92..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRF9"
FT CONFLICT 95..96
FT /note="DE -> EQ (in Ref. 2; AAH24996)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="V -> E (in Ref. 2; AAH24996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 16629 MW; 653B7D99E922E54F CRC64;
MAERPEDLNL PNAVITRIIK EALPDGVNIS KEARSAISRA ASVFVLYATS CANNFAMKGK
RKTLNASDVL SAMEEMEFQR FITPLKEALE AYRRDEKGKK EASEQKKKDK DKKDSEEQDK
SREVEEEDEE RLDEDDQNEE EEIDN
