DPOA2_MOUSE
ID DPOA2_MOUSE Reviewed; 600 AA.
AC P33611; Q8VDR3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase alpha 70 kDa subunit;
GN Name=Pola2;
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], AND PROTEIN SEQUENCE OF 84-102; 269-285 AND
RP 394-403.
RX PubMed=8463324; DOI=10.1016/s0021-9258(18)53069-6;
RA Miyazawa H., Izumi M., Tada S., Takada R., Masutani M., Ui M., Hanaoka F.;
RT "Molecular cloning of the cDNAs for the four subunits of mouse DNA
RT polymerase alpha-primase complex and their gene expression during cell
RT proliferation and the cell cycle.";
RL J. Biol. Chem. 268:8111-8122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127 AND THR-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis (By similarity).
CC During the S phase of the cell cycle, the DNA polymerase alpha complex
CC (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and
CC two primase subunits, the catalytic subunit PRIM1 and the regulatory
CC subunit PRIM2) is recruited to DNA at the replicative forks via direct
CC interactions with MCM10 and WDHD1 (By similarity). The primase subunit
CC of the polymerase alpha complex initiates DNA synthesis by
CC oligomerising short RNA primers on both leading and lagging strands.
CC These primers are initially extended by the polymerase alpha catalytic
CC subunit and subsequently transferred to polymerase delta and polymerase
CC epsilon for processive synthesis on the lagging and leading strand,
CC respectively (By similarity). {ECO:0000250|UniProtKB:P09884,
CC ECO:0000250|UniProtKB:P20664, ECO:0000250|UniProtKB:Q14181}.
CC -!- SUBUNIT: Component of the alpha DNA polymerase complex (also known as
CC the alpha DNA polymerase-primase complex) consisting of four subunits:
CC the catalytic subunit POLA1, the regulatory subunit POLA2, and the
CC primase complex subunits PRIM1 and PRIM2 respectively (By similarity).
CC Within the complex, POLA1 directly interacts with PRIM2 (By
CC similarity). {ECO:0000250|UniProtKB:P20664,
CC ECO:0000250|UniProtKB:Q14181}.
CC -!- INTERACTION:
CC P33611; P33609: Pola1; NbExp=5; IntAct=EBI-848759, EBI-688051;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M phase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000305}.
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DR EMBL; D13546; BAA02746.1; -; mRNA.
DR EMBL; AK150099; BAE29306.1; -; mRNA.
DR EMBL; CH466612; EDL33190.1; -; Genomic_DNA.
DR EMBL; BC021424; AAH21424.1; -; mRNA.
DR EMBL; BC064795; AAH64795.1; -; mRNA.
DR CCDS; CCDS29485.1; -.
DR PIR; B46642; B46642.
DR RefSeq; NP_032919.2; NM_008893.3.
DR AlphaFoldDB; P33611; -.
DR SMR; P33611; -.
DR BioGRID; 202288; 3.
DR ComplexPortal; CPX-2088; DNA polymerase alpha:primase complex.
DR CORUM; P33611; -.
DR IntAct; P33611; 3.
DR STRING; 10090.ENSMUSP00000025752; -.
DR iPTMnet; P33611; -.
DR PhosphoSitePlus; P33611; -.
DR EPD; P33611; -.
DR jPOST; P33611; -.
DR MaxQB; P33611; -.
DR PaxDb; P33611; -.
DR PeptideAtlas; P33611; -.
DR PRIDE; P33611; -.
DR ProteomicsDB; 277386; -.
DR DNASU; 18969; -.
DR Ensembl; ENSMUST00000025752; ENSMUSP00000025752; ENSMUSG00000024833.
DR GeneID; 18969; -.
DR KEGG; mmu:18969; -.
DR UCSC; uc008ggb.2; mouse.
DR CTD; 23649; -.
DR MGI; MGI:99690; Pola2.
DR VEuPathDB; HostDB:ENSMUSG00000024833; -.
DR eggNOG; KOG1625; Eukaryota.
DR GeneTree; ENSGT00390000016784; -.
DR HOGENOM; CLU_014923_3_1_1; -.
DR InParanoid; P33611; -.
DR OMA; PFLDIEH; -.
DR OrthoDB; 513979at2759; -.
DR PhylomeDB; P33611; -.
DR TreeFam; TF314249; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-MMU-68952; DNA replication initiation.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69091; Polymerase switching.
DR Reactome; R-MMU-69166; Removal of the Flap Intermediate.
DR Reactome; R-MMU-69183; Processive synthesis on the lagging strand.
DR BioGRID-ORCS; 18969; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Pola2; mouse.
DR PRO; PR:P33611; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P33611; protein.
DR Bgee; ENSMUSG00000024833; Expressed in cerebellum ventricular layer and 247 other tissues.
DR ExpressionAtlas; P33611; baseline and differential.
DR Genevisible; P33611; MM.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IDA:MGI.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR Gene3D; 1.10.8.530; -; 1.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR043034; DNA_pol_alpha_B_N_sf.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR InterPro; IPR013627; Pol_alpha_B_N.
DR PANTHER; PTHR23061; PTHR23061; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR Pfam; PF08418; Pol_alpha_B_N; 1.
DR PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..600
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194036"
FT REGION 107..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 127
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14181"
FT CONFLICT 346
FT /note="C -> R (in Ref. 1; BAA02746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66214 MW; 79F94443EF33FAA9 CRC64;
MAVSTQQLAE ELQIFGLDYE DSLLEKLAEL CVLYRQTEDG MVSELIAFCT SAGKTCLTVD
ILNSFEYEVL NKKLSKAWHS ASKDSGHAGT RDIVSIQELI EAEEEEETLL SSYTTPSKGP
LKRVSSTPET PLTKRSVAAR SPRQLLSPSS FSPSATPSQK YTSRTNRGEV VTTFGSAQGL
SWSGRGGSGS VSLKVVGDPE PLTGSYKAMF QQLMGVREVL TSKIEELGSE LKEHHKIEAF
TPLLVPAQEP VILLGQIGCD SNGKLNSKSV ILEGDQEHSY GAQIPVDLSE LKEYSLFPGQ
VVIMEGFNTT GRRLTATKLY EGVPLPFYQP TEEEGASEQT MVVVACGPYT TSDSITYDPL
LDLIAIINRD QPDVCILFGP FLDAKHEQVE NCKLTSPFED VFKQCLRTVI EGTRSSGSHL
VFVPSLRDVH HEPVYPQPPF TFSELSREDK KRVQFVSEPC SLSINGVMFG LTSTDLLFHI
GAEEIFSSSG TSDRFSRVLK HILTQRSYYP LYPPHEDMAI DYENFYTYAQ LPVTPDVFIV
PSELRYFVKD IFGCVCVNPG RLTKGQVGGT FGRLYLRRQP KAMDGGGRQG LSVAAQVVRI
