DPOA2_YEAST
ID DPOA2_YEAST Reviewed; 705 AA.
AC P38121; D6VPW4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase I subunit B;
DE AltName: Full=DNA polymerase alpha:primase complex p86 subunit;
DE Short=Pol alpha-primase complex p86 subunit;
DE AltName: Full=DNA polymerase-primase complex p74 subunit;
GN Name=POL12; OrderedLocusNames=YBL035C; ORFNames=YBL0414;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091857; DOI=10.1002/yea.320100003;
RA Skala J., van Dyck L., Purnelle B., Goffeau A.;
RT "The sequence of an 8.8 kb segment on the left arm of chromosome II from
RT Saccharomyces cerevisiae reveals four new open reading frames including
RT homologs of animal DNA polymerase alpha-primases and bacterial GTP
RT cyclohydrolase II.";
RL Yeast 10:S13-S24(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
RX PubMed=3061469; DOI=10.1016/0167-4781(88)90096-6;
RA Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C.,
RA Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G.;
RT "The yeast DNA polymerase-primase complex: genes and proteins.";
RL Biochim. Biophys. Acta 951:268-273(1988).
RN [5]
RP PHOSPHORYLATION, AND IDENTIFICATION IN THE DNA POLYMERASE ALPHA:PRIMASE
RP COMPLEX.
RX PubMed=8621497; DOI=10.1074/jbc.271.15.8661;
RA Ferrari M., Lucchini G., Plevani P., Foiani M.;
RT "Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent
RT on its association with the p180 polypeptide.";
RL J. Biol. Chem. 271:8661-8666(1996).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INTERACTION WITH MCM10.
RX PubMed=16675460; DOI=10.1074/jbc.m513551200;
RA Ricke R.M., Bielinsky A.-K.;
RT "A conserved Hsp10-like domain in Mcm10 is required to stabilize the
RT catalytic subunit of DNA polymerase-alpha in budding yeast.";
RL J. Biol. Chem. 281:18414-18425(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10] {ECO:0007744|PDB:3FLO}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 246-705 IN COMPLEX WITH POL1.
RX PubMed=19494830; DOI=10.1038/emboj.2009.150;
RA Klinge S., Nunez-Ramirez R., Llorca O., Pellegrini L.;
RT "3D architecture of DNA Pol alpha reveals the functional core of multi-
RT subunit replicative polymerases.";
RL EMBO J. 28:1978-1987(2009).
CC -!- FUNCTION: Non-catalytic component of DNA polymerase alpha, which in a
CC complex with DNA primase (DNA polymerase alpha:primase) constitutes a
CC replicative polymerase. POL12 may play an essential role at the early
CC stage of chromosomal DNA replication by coupling DNA polymerase alpha
CC to the cellular replication machinery (By similarity). Interacts with
CC MCM10. {ECO:0000250}.
CC -!- SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme complex,
CC which is assembled throughout the cell cycle, and consists of the two
CC DNA polymerase subunits A POL1 and B POL12, and the DNA primase large
CC PRI2 and small PRI1 subunits (PubMed:3061469). Subunit B POL12 binds to
CC subunit A POL1 (PubMed:19494830). {ECO:0000269|PubMed:19494830,
CC ECO:0000269|PubMed:3061469}.
CC -!- INTERACTION:
CC P38121; P13382: POL1; NbExp=4; IntAct=EBI-6111, EBI-6128;
CC P38121; P38960: STN1; NbExp=2; IntAct=EBI-6111, EBI-18427;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner.
CC {ECO:0000269|PubMed:8621497}.
CC -!- MISCELLANEOUS: Present with 11200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000305}.
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DR EMBL; Z35796; CAA84855.1; -; Genomic_DNA.
DR EMBL; X74738; CAA52761.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07084.1; -; Genomic_DNA.
DR PIR; S45769; S45769.
DR RefSeq; NP_009518.1; NM_001178275.1.
DR PDB; 3FLO; X-ray; 2.50 A; A/C/E/G=246-705.
DR PDBsum; 3FLO; -.
DR AlphaFoldDB; P38121; -.
DR SMR; P38121; -.
DR BioGRID; 32662; 417.
DR ComplexPortal; CPX-2091; DNA polymerase alpha:primase complex.
DR DIP; DIP-2536N; -.
DR IntAct; P38121; 30.
DR MINT; P38121; -.
DR STRING; 4932.YBL035C; -.
DR iPTMnet; P38121; -.
DR MaxQB; P38121; -.
DR PaxDb; P38121; -.
DR PRIDE; P38121; -.
DR EnsemblFungi; YBL035C_mRNA; YBL035C; YBL035C.
DR GeneID; 852245; -.
DR KEGG; sce:YBL035C; -.
DR SGD; S000000131; POL12.
DR VEuPathDB; FungiDB:YBL035C; -.
DR eggNOG; KOG1625; Eukaryota.
DR GeneTree; ENSGT00390000016784; -.
DR HOGENOM; CLU_014923_1_0_1; -.
DR InParanoid; P38121; -.
DR OMA; NETHTEY; -.
DR BioCyc; YEAST:G3O-28937-MON; -.
DR Reactome; R-SCE-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-SCE-68952; DNA replication initiation.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR Reactome; R-SCE-69091; Polymerase switching.
DR Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR EvolutionaryTrace; P38121; -.
DR PRO; PR:P38121; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38121; protein.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:GOC.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006273; P:lagging strand elongation; IC:SGD.
DR GO; GO:0016233; P:telomere capping; IMP:SGD.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
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 3D-structure; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..705
FT /note="DNA polymerase alpha subunit B"
FT /id="PRO_0000194041"
FT REGION 115..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 254..276
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 294..306
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:3FLO"
FT TURN 505..509
FT /evidence="ECO:0007829|PDB:3FLO"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 520..526
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 556..567
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 614..620
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 680..683
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:3FLO"
FT HELIX 694..697
FT /evidence="ECO:0007829|PDB:3FLO"
FT STRAND 698..704
FT /evidence="ECO:0007829|PDB:3FLO"
SQ SEQUENCE 705 AA; 78774 MW; F9F06D12F6979637 CRC64;
MSGSIDVITH FGPDADKPEI ITALENLTKL HALSVEDLYI KWEQFSNQRR QTHTDLTSKN
IDEFKQFLQL QMEKRANQIS SSSKVNTSTK KPVIKKSLNS SPLFGLSIPK TPTLKKRKLH
GPFSLSDSKQ TYNVGSEAET NEKGNSSLKL EFTPGMAEDA VGDSAPLSHA KSSDAKTPGS
STFQTPTTNT PTTSRQNVPA GEILDSLNPE NIEISSGNPN VGLLSTEEPS YNQVKVEPFY
DAKKYKFRTM RQNLQEASDV LDDQIESFTK IIQNHYKLSP NDFADPTIQS QSEIYAVGRI
VPDSPTYDKF LNPESLSLET SRMGGVGRRV RLDLSQVNEL SFFLGQIVAF KGKNANGDYF
TVNSILPLPY PNSPVSTSQE LQEFQANLEG SSLKVIVTCG PYFANDNFSL ELLQEFIDSI
NNEVKPHVLI MFGPFIDITH PLIASGKLPN FPQFKTQPKT LDELFLKLFT PILKTISPHI
QTVLIPSTKD AISNHAAYPQ ASLIRKALQL PKRNFKCMAN PSSFQINEIY FGCSNVDTFK
DLKEVIKGGT TSSRYRLDRV SEHILQQRRY YPIFPGSIRT RIKPKDVSTK KETNDMESKE
EKVYEHISGA DLDVSYLGLT EFVGGFSPDI MIIPSELQHF ARVVQNVVVI NPGRFIRATG
NRGSYAQITV QCPDLEDGKL TLVEGEEPVY LHNVWKRARV DLIAS
