Full text data of POLA2
POLA2
[Confidence: low (only semi-automatic identification from reviews)]
DNA polymerase alpha subunit B (DNA polymerase alpha 70 kDa subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA polymerase alpha subunit B (DNA polymerase alpha 70 kDa subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14181
ID DPOA2_HUMAN Reviewed; 598 AA.
AC Q14181; Q9BPV3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase alpha 70 kDa subunit;
GN Name=POLA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix epithelium;
RX PubMed=8223465;
RA Collins K.L., Russo A.A.R., Tseng B.Y., Kelly T.J.;
RT "The role of the 70 kDa subunit of human DNA polymerase alpha in DNA
RT replication.";
RL EMBO J. 12:4555-4566(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=1902230;
RA Nasheuer H.-P., Moore A., Wahl A.F., Wang T.S.-F.;
RT "Cell cycle-dependent phosphorylation of human DNA polymerase alpha.";
RL J. Biol. Chem. 266:7893-7903(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-127; THR-130;
RP SER-141 AND SER-147, AND MASS SPECTROMETRY.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127; THR-130; SER-141;
RP SER-147 AND SER-152, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play an essential role at the early stage of
CC chromosomal DNA replication by coupling the polymerase
CC alpha/primase complex to the cellular replication machinery (By
CC similarity).
CC -!- SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme
CC complex, which is assembled throughout the cell cycle, and
CC consists of the two DNA polymerase subunits A and B, and the DNA
CC primase large and small subunits. Subunit B binds to subunit A.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The N-terminal 240 amino acids are sufficient to mediate
CC complex formation.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M
CC phase.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L24559; AAA16459.1; -; mRNA.
DR EMBL; CR456737; CAG33018.1; -; mRNA.
DR EMBL; BC002990; AAH02990.1; -; mRNA.
DR EMBL; BC001347; AAH01347.1; -; mRNA.
DR PIR; S39621; S39621.
DR RefSeq; NP_002680.2; NM_002689.2.
DR UniGene; Hs.201897; -.
DR PDB; 2KEB; NMR; -; A=1-78.
DR PDB; 4E2I; X-ray; 5.00 A; 1/2/3/4/5/6/7/8/9/U/W=1-78.
DR PDBsum; 2KEB; -.
DR PDBsum; 4E2I; -.
DR ProteinModelPortal; Q14181; -.
DR SMR; Q14181; 1-78.
DR IntAct; Q14181; 31.
DR MINT; MINT-1382407; -.
DR STRING; 9606.ENSP00000265465; -.
DR DrugBank; DB00851; Dacarbazine.
DR PhosphoSite; Q14181; -.
DR DMDM; 90110415; -.
DR PaxDb; Q14181; -.
DR PeptideAtlas; Q14181; -.
DR PRIDE; Q14181; -.
DR DNASU; 23649; -.
DR Ensembl; ENST00000265465; ENSP00000265465; ENSG00000014138.
DR GeneID; 23649; -.
DR KEGG; hsa:23649; -.
DR UCSC; uc001odj.3; human.
DR CTD; 23649; -.
DR GeneCards; GC11P065029; -.
DR HGNC; HGNC:30073; POLA2.
DR HPA; HPA037570; -.
DR neXtProt; NX_Q14181; -.
DR PharmGKB; PA411; -.
DR eggNOG; COG5214; -.
DR HOGENOM; HOG000007382; -.
DR HOVERGEN; HBG055628; -.
DR InParanoid; Q14181; -.
DR KO; K02321; -.
DR OMA; DREHSSG; -.
DR OrthoDB; EOG7GXPB7; -.
DR PhylomeDB; Q14181; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR ChiTaRS; POLA2; human.
DR EvolutionaryTrace; Q14181; -.
DR GeneWiki; POLA2; -.
DR GenomeRNAi; 23649; -.
DR NextBio; 46481; -.
DR PRO; PR:Q14181; -.
DR ArrayExpress; Q14181; -.
DR Bgee; Q14181; -.
DR CleanEx; HS_POLA2; -.
DR Genevestigator; Q14181; -.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; TAS:Reactome.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000060; P:protein import into nucleus, translocation; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR InterPro; IPR007185; DNA_pol_alpha/epsilon_bsu.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR InterPro; IPR013627; Pol_alpha_B_N.
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; Complete proteome; DNA replication; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 598 DNA polymerase alpha subunit B.
FT /FTId=PRO_0000194035.
FT COMPBIAS 101 107 Poly-Glu.
FT COMPBIAS 115 157 Pro/Ser/Thr-rich.
FT COMPBIAS 486 489 Poly-Ser.
FT MOD_RES 126 126 Phosphoserine.
FT MOD_RES 127 127 Phosphothreonine.
FT MOD_RES 130 130 Phosphothreonine.
FT MOD_RES 141 141 Phosphoserine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT VARIANT 583 583 G -> R (in dbSNP:rs487989).
FT /FTId=VAR_033896.
FT VARIANT 588 588 S -> N (in dbSNP:rs7123885).
FT /FTId=VAR_033897.
FT CONFLICT 383 384 DA -> ES (in Ref. 1; AAA16459).
FT HELIX 5 15
FT HELIX 21 34
FT HELIX 38 52
FT HELIX 59 68
FT HELIX 70 73
SQ SEQUENCE 598 AA; 65948 MW; F5CBD7E022ADDDBF CRC64;
MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT STHKVGLTSE
ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI EVEEEEEILL NSYTTPSKGS
QKRAISTPET PLTKRSVSTR SPHQLLSPSS FSPSATPSQK YNSRSNRGEV VTSFGLAQGV
SWSGRGGAGN ISLKVLGCPE ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF
TPLLAPAQEP VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ
VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT TSDSITYDPL
LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED IFKQCLRTII EGTRSSGSHL
VFVPSLRDVH HEPVYPQPPF SYSDLSREDK KQVQFVSEPC SLSINGVIFG LTSTDLLFHL
GAEEISSSSG TSDRFSRILK HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII
PSELRYFVKD VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI
//
ID DPOA2_HUMAN Reviewed; 598 AA.
AC Q14181; Q9BPV3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-FEB-2006, sequence version 2.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=DNA polymerase alpha subunit B;
DE AltName: Full=DNA polymerase alpha 70 kDa subunit;
GN Name=POLA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix epithelium;
RX PubMed=8223465;
RA Collins K.L., Russo A.A.R., Tseng B.Y., Kelly T.J.;
RT "The role of the 70 kDa subunit of human DNA polymerase alpha in DNA
RT replication.";
RL EMBO J. 12:4555-4566(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=1902230;
RA Nasheuer H.-P., Moore A., Wahl A.F., Wang T.S.-F.;
RT "Cell cycle-dependent phosphorylation of human DNA polymerase alpha.";
RL J. Biol. Chem. 266:7893-7903(1991).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; THR-127; THR-130;
RP SER-141 AND SER-147, AND MASS SPECTROMETRY.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127; THR-130; SER-141;
RP SER-147 AND SER-152, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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.,
RA Buerckstuemmer T., 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-152, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play an essential role at the early stage of
CC chromosomal DNA replication by coupling the polymerase
CC alpha/primase complex to the cellular replication machinery (By
CC similarity).
CC -!- SUBUNIT: DNA polymerase alpha:primase is a four subunit enzyme
CC complex, which is assembled throughout the cell cycle, and
CC consists of the two DNA polymerase subunits A and B, and the DNA
CC primase large and small subunits. Subunit B binds to subunit A.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The N-terminal 240 amino acids are sufficient to mediate
CC complex formation.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner, in G2/M
CC phase.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L24559; AAA16459.1; -; mRNA.
DR EMBL; CR456737; CAG33018.1; -; mRNA.
DR EMBL; BC002990; AAH02990.1; -; mRNA.
DR EMBL; BC001347; AAH01347.1; -; mRNA.
DR PIR; S39621; S39621.
DR RefSeq; NP_002680.2; NM_002689.2.
DR UniGene; Hs.201897; -.
DR PDB; 2KEB; NMR; -; A=1-78.
DR PDB; 4E2I; X-ray; 5.00 A; 1/2/3/4/5/6/7/8/9/U/W=1-78.
DR PDBsum; 2KEB; -.
DR PDBsum; 4E2I; -.
DR ProteinModelPortal; Q14181; -.
DR SMR; Q14181; 1-78.
DR IntAct; Q14181; 31.
DR MINT; MINT-1382407; -.
DR STRING; 9606.ENSP00000265465; -.
DR DrugBank; DB00851; Dacarbazine.
DR PhosphoSite; Q14181; -.
DR DMDM; 90110415; -.
DR PaxDb; Q14181; -.
DR PeptideAtlas; Q14181; -.
DR PRIDE; Q14181; -.
DR DNASU; 23649; -.
DR Ensembl; ENST00000265465; ENSP00000265465; ENSG00000014138.
DR GeneID; 23649; -.
DR KEGG; hsa:23649; -.
DR UCSC; uc001odj.3; human.
DR CTD; 23649; -.
DR GeneCards; GC11P065029; -.
DR HGNC; HGNC:30073; POLA2.
DR HPA; HPA037570; -.
DR neXtProt; NX_Q14181; -.
DR PharmGKB; PA411; -.
DR eggNOG; COG5214; -.
DR HOGENOM; HOG000007382; -.
DR HOVERGEN; HBG055628; -.
DR InParanoid; Q14181; -.
DR KO; K02321; -.
DR OMA; DREHSSG; -.
DR OrthoDB; EOG7GXPB7; -.
DR PhylomeDB; Q14181; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR ChiTaRS; POLA2; human.
DR EvolutionaryTrace; Q14181; -.
DR GeneWiki; POLA2; -.
DR GenomeRNAi; 23649; -.
DR NextBio; 46481; -.
DR PRO; PR:Q14181; -.
DR ArrayExpress; Q14181; -.
DR Bgee; Q14181; -.
DR CleanEx; HS_POLA2; -.
DR Genevestigator; Q14181; -.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; TAS:Reactome.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000060; P:protein import into nucleus, translocation; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR InterPro; IPR007185; DNA_pol_alpha/epsilon_bsu.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR InterPro; IPR013627; Pol_alpha_B_N.
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; Complete proteome; DNA replication; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 598 DNA polymerase alpha subunit B.
FT /FTId=PRO_0000194035.
FT COMPBIAS 101 107 Poly-Glu.
FT COMPBIAS 115 157 Pro/Ser/Thr-rich.
FT COMPBIAS 486 489 Poly-Ser.
FT MOD_RES 126 126 Phosphoserine.
FT MOD_RES 127 127 Phosphothreonine.
FT MOD_RES 130 130 Phosphothreonine.
FT MOD_RES 141 141 Phosphoserine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 152 152 Phosphoserine.
FT VARIANT 583 583 G -> R (in dbSNP:rs487989).
FT /FTId=VAR_033896.
FT VARIANT 588 588 S -> N (in dbSNP:rs7123885).
FT /FTId=VAR_033897.
FT CONFLICT 383 384 DA -> ES (in Ref. 1; AAA16459).
FT HELIX 5 15
FT HELIX 21 34
FT HELIX 38 52
FT HELIX 59 68
FT HELIX 70 73
SQ SEQUENCE 598 AA; 65948 MW; F5CBD7E022ADDDBF CRC64;
MSASAQQLAE ELQIFGLDCE EALIEKLVEL CVQYGQNEEG MVGELIAFCT STHKVGLTSE
ILNSFEHEFL SKRLSKARHS TCKDSGHAGA RDIVSIQELI EVEEEEEILL NSYTTPSKGS
QKRAISTPET PLTKRSVSTR SPHQLLSPSS FSPSATPSQK YNSRSNRGEV VTSFGLAQGV
SWSGRGGAGN ISLKVLGCPE ALTGSYKSMF QKLPDIREVL TCKIEELGSE LKEHYKIEAF
TPLLAPAQEP VTLLGQIGCD SNGKLNNKSV ILEGDREHSS GAQIPVDLSE LKEYSLFPGQ
VVIMEGINTT GRKLVATKLY EGVPLPFYQP TEEDADFEQS MVLVACGPYT TSDSITYDPL
LDLIAVINHD RPDVCILFGP FLDAKHEQVE NCLLTSPFED IFKQCLRTII EGTRSSGSHL
VFVPSLRDVH HEPVYPQPPF SYSDLSREDK KQVQFVSEPC SLSINGVIFG LTSTDLLFHL
GAEEISSSSG TSDRFSRILK HILTQRSYYP LYPPQEDMAI DYESFYVYAQ LPVTPDVLII
PSELRYFVKD VLGCVCVNPG RLTKGQVGGT FARLYLRRPA ADGAERQSPC IAVQVVRI
//