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DPOE4_MOUSE
ID   DPOE4_MOUSE             Reviewed;         118 AA.
AC   Q9CQ36; Q3TJ13;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=DNA polymerase epsilon subunit 4;
DE   AltName: Full=DNA polymerase II subunit 4;
DE   AltName: Full=DNA polymerase epsilon subunit p12;
GN   Name=Pole4;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=Liver, Spleen, and 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). {ECO:0000250|UniProtKB:P27344,
CC       ECO:0000250|UniProtKB:Q9NR33}.
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 POLE3 is a prerequisite for
CC       further binding with POLE and POLE2. {ECO:0000250|UniProtKB:Q9NR33}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AK010135; BAB26722.1; -; mRNA.
DR   EMBL; AK010300; BAB26833.1; -; mRNA.
DR   EMBL; AK011595; BAB27723.1; -; mRNA.
DR   EMBL; AK160582; BAE35889.1; -; mRNA.
DR   EMBL; AK167631; BAE39682.1; -; mRNA.
DR   EMBL; BC023189; AAH23189.1; -; mRNA.
DR   CCDS; CCDS39524.1; -.
DR   RefSeq; NP_080158.1; NM_025882.3.
DR   AlphaFoldDB; Q9CQ36; -.
DR   SMR; Q9CQ36; -.
DR   ComplexPortal; CPX-2109; DNA polymerase epsilon complex.
DR   STRING; 10090.ENSMUSP00000093462; -.
DR   iPTMnet; Q9CQ36; -.
DR   PhosphoSitePlus; Q9CQ36; -.
DR   REPRODUCTION-2DPAGE; Q9CQ36; -.
DR   EPD; Q9CQ36; -.
DR   MaxQB; Q9CQ36; -.
DR   PaxDb; Q9CQ36; -.
DR   PRIDE; Q9CQ36; -.
DR   ProteomicsDB; 277489; -.
DR   Antibodypedia; 31631; 83 antibodies from 17 providers.
DR   DNASU; 66979; -.
DR   Ensembl; ENSMUST00000095786; ENSMUSP00000093462; ENSMUSG00000030042.
DR   GeneID; 66979; -.
DR   KEGG; mmu:66979; -.
DR   UCSC; uc009clk.1; mouse.
DR   CTD; 56655; -.
DR   MGI; MGI:1914229; Pole4.
DR   VEuPathDB; HostDB:ENSMUSG00000030042; -.
DR   eggNOG; KOG1658; Eukaryota.
DR   GeneTree; ENSGT00940000160888; -.
DR   HOGENOM; CLU_045277_8_0_1; -.
DR   InParanoid; Q9CQ36; -.
DR   OMA; HDPDRCG; -.
DR   OrthoDB; 1622159at2759; -.
DR   PhylomeDB; Q9CQ36; -.
DR   TreeFam; TF103009; -.
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; 66979; 4 hits in 108 CRISPR screens.
DR   ChiTaRS; Pole4; mouse.
DR   PRO; PR:Q9CQ36; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9CQ36; protein.
DR   Bgee; ENSMUSG00000030042; Expressed in animal zygote and 274 other tissues.
DR   ExpressionAtlas; Q9CQ36; baseline and differential.
DR   Genevisible; Q9CQ36; MM.
DR   GO; GO:0140672; C:ATAC complex; ISO:MGI.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated 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; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR33"
FT   CHAIN           2..118
FT                   /note="DNA polymerase epsilon subunit 4"
FT                   /id="PRO_0000191747"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR33"
FT   MOD_RES         11
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR33"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NR33"
SQ   SEQUENCE   118 AA;  12240 MW;  CE6B47CD7BC93A09 CRC64;
     MAAAAAAGSG TPREEEAPGG EAAASQAQAP TSAPGGVRLS RLPLARVKAL VKADPDVTLA
     GQEAIFILAR AAELFVETIA KDAYCCAQQG KRKTLQRRDL DNAIEAVDEF AFLEGTLD
 
 
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