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P09884

- DPOLA_HUMAN

UniProt

P09884 - DPOLA_HUMAN

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Protein

DNA polymerase alpha catalytic subunit

Gene
POLA1, POLA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes.1 Publication

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactori

Binds 1 4Fe-4S cluster By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei124 – 1252Cleavage
Metal bindingi1283 – 12831Zinc By similarity
Metal bindingi1286 – 12861Zinc By similarity
Metal bindingi1310 – 13101Zinc By similarity
Metal bindingi1315 – 13151Zinc By similarity
Metal bindingi1348 – 13481Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1353 – 13531Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1371 – 13711Iron-sulfur (4Fe-4S) By similarity
Metal bindingi1374 – 13741Iron-sulfur (4Fe-4S) By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1283 – 131533CysA-typeAdd
BLAST

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: RefGenome
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. chromatin binding Source: UniProtKB
  4. DNA binding Source: UniProtKB
  5. DNA-directed DNA polymerase activity Source: UniProtKB
  6. metal ion binding Source: UniProtKB-KW
  7. nucleoside binding Source: InterPro
  8. nucleotide binding Source: UniProtKB
  9. protein binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. DNA replication Source: UniProtKB
  3. DNA replication, synthesis of RNA primer Source: GOC
  4. DNA replication initiation Source: UniProtKB
  5. DNA strand elongation involved in DNA replication Source: UniProtKB
  6. double-strand break repair via nonhomologous end joining Source: UniProtKB
  7. G1/S transition of mitotic cell cycle Source: Reactome
  8. lagging strand elongation Source: UniProtKB
  9. leading strand elongation Source: UniProtKB
  10. mitotic cell cycle Source: Reactome
  11. mitotic S phase Source: UniProtKB
  12. nucleic acid phosphodiester bond hydrolysis Source: GOC
  13. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  14. telomere maintenance Source: Reactome
  15. telomere maintenance via recombination Source: Reactome
  16. telomere maintenance via semi-conservative replication Source: Reactome
  17. translesion synthesis Source: RefGenome
  18. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Host-virus interaction

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase alpha catalytic subunit (EC:2.7.7.7)
Alternative name(s):
DNA polymerase alpha catalytic subunit p180
Gene namesi
Name:POLA1
Synonyms:POLA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:9173. POLA1.

Subcellular locationi

GO - Cellular componenti

  1. alpha DNA polymerase:primase complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nuclear envelope Source: UniProtKB
  4. nuclear matrix Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. nucleoplasm Source: UniProtKB
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162399856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14621462DNA polymerase alpha catalytic subunitPRO_0000046428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741Phosphothreonine2 Publications
Modified residuei186 – 1861Phosphoserine4 Publications
Modified residuei190 – 1901Phosphoserine2 Publications
Modified residuei209 – 2091Phosphoserine3 Publications
Modified residuei224 – 2241N6-acetyllysine By similarity
Modified residuei970 – 9701N6-succinyllysine By similarity

Post-translational modificationi

A 165 kDa form is probably produced by proteolytic cleavage at Lys-124.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09884.
PaxDbiP09884.
PRIDEiP09884.

PTM databases

PhosphoSiteiP09884.

Expressioni

Gene expression databases

ArrayExpressiP09884.
BgeeiP09884.
CleanExiHS_POLA1.
GenevestigatoriP09884.

Organism-specific databases

HPAiCAB012274.
HPA002947.

Interactioni

Subunit structurei

The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Interacts with PARP1; this interaction functions as part of the control of replication fork progression. Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA. Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with SV40 Large T antigen; this interaction allows viral DNA replication. Interacts with herpes simplex virus 1 (HHV-1) replication origin-binding protein UL9.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030706EBI-850026,EBI-617698From a different organism.
E1P040142EBI-850026,EBI-7014446From a different organism.
RPA1P276942EBI-850026,EBI-621389
UL9P101934EBI-850026,EBI-8596799From a different organism.

Protein-protein interaction databases

BioGridi111418. 37 interactions.
IntActiP09884. 10 interactions.
MINTiMINT-1517478.
STRINGi9606.ENSP00000368349.

Structurei

Secondary structure

1
1462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1346 – 13494
Helixi1350 – 13589
Beta strandi1359 – 13624
Beta strandi1366 – 13694
Turni1370 – 13723
Helixi1375 – 13795

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0PNMR-A1347-1377[»]
1K18NMR-A1347-1377[»]
1N5GNMR-A1345-1382[»]
ProteinModelPortaliP09884.
SMRiP09884. Positions 341-1240, 1269-1429.

Miscellaneous databases

EvolutionaryTraceiP09884.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni650 – 71566DNA-binding region Reviewed predictionAdd
BLAST
Regioni1245 – 1376132DNA-binding region Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1348 – 137427CysB motifAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 11238Asp-richAdd
BLAST
Compositional biasi1047 – 10504Poly-Leu
Compositional biasi1051 – 10544Poly-Lys

Domaini

The CysB motif binds 1 4Fe-4S cluster and is required for the formation of polymerase complexes By similarity.

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1283 – 131533CysA-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0417.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
KOiK02320.
PhylomeDBiP09884.
TreeFamiTF103001.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PfamiPF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09884-1 [UniParc]FASTAAdd to Basket

« Hide

MAPVHGDDSL SDSGSFVSSR ARREKKSKKG RQEALERLKK AKAGEKYKYE     50
VEDFTGVYEE VDEEQYSKLV QARQDDDWIV DDDGIGYVED GREIFDDDLE 100
DDALDADEKG KDGKARNKDK RNVKKLAVTK PNNIKSMFIA CAGKKTADKA 150
VDLSKDGLLG DILQDLNTET PQITPPPVMI LKKKRSIGAS PNPFSVHTAT 200
AVPSGKIASP VSRKEPPLTP VPLKRAEFAG DDVQVESTEE EQESGAMEFE 250
DGDFDEPMEV EEVDLEPMAA KAWDKESEPA EEVKQEADSG KGTVSYLGSF 300
LPDVSCWDID QEGDSSFSVQ EVQVDSSHLP LVKGADEEQV FHFYWLDAYE 350
DQYNQPGVVF LFGKVWIESA ETHVSCCVMV KNIERTLYFL PREMKIDLNT 400
GKETGTPISM KDVYEEFDEK IATKYKIMKF KSKPVEKNYA FEIPDVPEKS 450
EYLEVKYSAE MPQLPQDLKG ETFSHVFGTN TSSLELFLMN RKIKGPCWLE 500
VKSPQLLNQP VSWCKVEAMA LKPDLVNVIK DVSPPPLVVM AFSMKTMQNA 550
KNHQNEIIAM AALVHHSFAL DKAAPKPPFQ SHFCVVSKPK DCIFPYAFKE 600
VIEKKNVKVE VAATERTLLG FFLAKVHKID PDIIVGHNIY GFELEVLLQR 650
INVCKAPHWS KIGRLKRSNM PKLGGRSGFG ERNATCGRMI CDVEISAKEL 700
IRCKSYHLSE LVQQILKTER VVIPMENIQN MYSESSQLLY LLEHTWKDAK 750
FILQIMCELN VLPLALQITN IAGNIMSRTL MGGRSERNEF LLLHAFYENN 800
YIVPDKQIFR KPQQKLGDED EEIDGDTNKY KKGRKKAAYA GGLVLDPKVG 850
FYDKFILLLD FNSLYPSIIQ EFNICFTTVQ RVASEAQKVT EDGEQEQIPE 900
LPDPSLEMGI LPREIRKLVE RRKQVKQLMK QQDLNPDLIL QYDIRQKALK 950
LTANSMYGCL GFSYSRFYAK PLAALVTYKG REILMHTKEM VQKMNLEVIY 1000
GDTDSIMINT NSTNLEEVFK LGNKVKSEVN KLYKLLEIDI DGVFKSLLLL 1050
KKKKYAALVV EPTSDGNYVT KQELKGLDIV RRDWCDLAKD TGNFVIGQIL 1100
SDQSRDTIVE NIQKRLIEIG ENVLNGSVPV SQFEINKALT KDPQDYPDKK 1150
SLPHVHVALW INSQGGRKVK AGDTVSYVIC QDGSNLTASQ RAYAPEQLQK 1200
QDNLTIDTQY YLAQQIHPVV ARICEPIDGI DAVLIATWLG LDPTQFRVHH 1250
YHKDEENDAL LGGPAQLTDE EKYRDCERFK CPCPTCGTEN IYDNVFDGSG 1300
TDMEPSLYRC SNIDCKASPL TFTVQLSNKL IMDIRRFIKK YYDGWLICEE 1350
PTCRNRTRHL PLQFSRTGPL CPACMKATLQ PEYSDKSLYT QLCFYRYIFD 1400
AECALEKLTT DHEKDKLKKQ FFTPKVLQDY RKLKNTAEQF LSRSGYSEVN 1450
LSKLFAGCAV KS 1462
Length:1,462
Mass (Da):165,913
Last modified:February 1, 2005 - v2
Checksum:iDC40C3EDD6F4B495
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti740 – 7401Y → H.
Corresponds to variant rs2230927 [ dbSNP | Ensembl ].
VAR_048877

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti503 – 5064SPQL → KSTA in CAA29920. 1 Publication
Sequence conflicti837 – 8371A → G in CAA29920. 1 Publication
Sequence conflicti1405 – 14051L → C AA sequence 1 Publication
Sequence conflicti1426 – 14261V → C AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06745 mRNA. Translation: CAA29920.1.
AY275833 Genomic DNA. Translation: AAP13534.1.
M64481 Genomic DNA. Translation: AAA52318.1.
CCDSiCCDS14214.1.
PIRiS00257. DJHUAC.
RefSeqiNP_058633.2. NM_016937.3.
UniGeneiHs.567319.

Genome annotation databases

EnsembliENST00000379059; ENSP00000368349; ENSG00000101868.
GeneIDi5422.
KEGGihsa:5422.
UCSCiuc004dbl.3. human.

Polymorphism databases

DMDMi60392197.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06745 mRNA. Translation: CAA29920.1 .
AY275833 Genomic DNA. Translation: AAP13534.1 .
M64481 Genomic DNA. Translation: AAA52318.1 .
CCDSi CCDS14214.1.
PIRi S00257. DJHUAC.
RefSeqi NP_058633.2. NM_016937.3.
UniGenei Hs.567319.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K0P NMR - A 1347-1377 [» ]
1K18 NMR - A 1347-1377 [» ]
1N5G NMR - A 1345-1382 [» ]
ProteinModelPortali P09884.
SMRi P09884. Positions 341-1240, 1269-1429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111418. 37 interactions.
IntActi P09884. 10 interactions.
MINTi MINT-1517478.
STRINGi 9606.ENSP00000368349.

Chemistry

BindingDBi P09884.
ChEMBLi CHEMBL2363042.
DrugBanki DB00631. Clofarabine.
DB01073. Fludarabine.

PTM databases

PhosphoSitei P09884.

Polymorphism databases

DMDMi 60392197.

Proteomic databases

MaxQBi P09884.
PaxDbi P09884.
PRIDEi P09884.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379059 ; ENSP00000368349 ; ENSG00000101868 .
GeneIDi 5422.
KEGGi hsa:5422.
UCSCi uc004dbl.3. human.

Organism-specific databases

CTDi 5422.
GeneCardsi GC0XP024712.
H-InvDB HIX0028476.
HGNCi HGNC:9173. POLA1.
HPAi CAB012274.
HPA002947.
MIMi 312040. gene.
neXtProti NX_P09884.
PharmGKBi PA162399856.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0417.
HOGENOMi HOG000163524.
HOVERGENi HBG080008.
KOi K02320.
PhylomeDBi P09884.
TreeFami TF103001.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1385. Processive synthesis on the lagging strand.
REACT_1792. Polymerase switching.
REACT_1838. Leading Strand Synthesis.
REACT_2244. DNA replication initiation.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_70. Removal of the Flap Intermediate.
REACT_7987. Polymerase switching on the C-strand of the telomere.
REACT_7993. Telomere C-strand synthesis initiation.

Miscellaneous databases

ChiTaRSi POLA1. human.
EvolutionaryTracei P09884.
GeneWikii Polymerase_(DNA_directed),_alpha_1.
GenomeRNAii 5422.
NextBioi 20977.
PROi P09884.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09884.
Bgeei P09884.
CleanExi HS_POLA1.
Genevestigatori P09884.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProi IPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view ]
Pfami PF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view ]
PRINTSi PR00106. DNAPOLB.
SMARTi SM00486. POLBc. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 1 hit.
PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases."
    Wong S.W., Wahl A.F., Yuan P.-M., Arai N., Pearson B.E., Arai K., Korn D., Hunkapiller M.W., Wang T.S.-F.
    EMBO J. 7:37-47(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells."
    Pearson B.E., Nasheuer H.-P., Wang T.S.-F.
    Mol. Cell. Biol. 11:2081-2095(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
  4. "Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus."
    Hsi K.-L., Copeland W.C., Wang T.S.-F.
    Nucleic Acids Res. 18:6231-6237(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-37 AND 1405-1426, PROTEOLYTIC PROCESSING AT LYS-124.
  5. "T-antigen-DNA polymerase alpha complex implicated in simian virus 40 DNA replication."
    Smale S.T., Tjian R.
    Mol. Cell. Biol. 6:4077-4087(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
  6. "Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha."
    Lee S.S., Dong Q., Wang T.S., Lehman I.R.
    Proc. Natl. Acad. Sci. U.S.A. 92:7882-7886(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 UL9 PROTEIN.
  7. "Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms."
    Braun K.A., Lao Y., He Z., Ingles C.J., Wold M.S.
    Biochemistry 36:8443-8454(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPA1.
  8. "Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
    Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Menissier-de Murcia J.
    Nucleic Acids Res. 26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PARP1.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-190 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Physical interactions between Mcm10, DNA, and DNA polymerase alpha."
    Warren E.M., Huang H., Fanning E., Chazin W.J., Eichman B.F.
    J. Biol. Chem. 284:24662-24672(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCM10.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; SER-186; SER-190 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha."
    Evanics F., Maurmann L., Yang W.W., Bose R.N.
    Biochim. Biophys. Acta 1651:163-171(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1345-1382.

Entry informationi

Entry nameiDPOLA_HUMAN
AccessioniPrimary (citable) accession number: P09884
Secondary accession number(s): Q86UQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 2005
Last modified: September 3, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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