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Protein

DNA polymerase alpha catalytic subunit

Gene

POLA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei124 – 1252Cleavage
Metal bindingi1283 – 12831ZincBy similarity
Metal bindingi1286 – 12861ZincBy similarity
Metal bindingi1310 – 13101ZincBy similarity
Metal bindingi1315 – 13151ZincBy 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

  • 3'-5' exonuclease activity Source: InterPro
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-directed DNA polymerase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • nucleoside binding Source: InterPro
  • nucleotide binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • DNA biosynthetic process Source: GOC
  • DNA-dependent DNA replication Source: GO_Central
  • DNA replication Source: UniProtKB
  • DNA replication, synthesis of RNA primer Source: GOC
  • DNA replication initiation Source: UniProtKB
  • DNA strand elongation involved in DNA replication Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: UniProtKB
  • G1/S transition of mitotic cell cycle Source: Reactome
  • lagging strand elongation Source: UniProtKB
  • leading strand elongation Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  • telomere maintenance Source: Reactome
  • telomere maintenance via recombination Source: Reactome
  • telomere maintenance via semi-conservative replication Source: Reactome
  • 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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9173. POLA1.

Subcellular locationi

GO - Cellular componenti

  • alpha DNA polymerase:primase complex Source: UniProtKB
  • cytoplasm Source: HPA
  • nuclear envelope Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162399856.

Chemistry

DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB01280. Nelarabine.

Polymorphism and mutation databases

BioMutaiPOLA1.
DMDMi60392197.

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-acetyllysineBy similarity
Modified residuei970 – 9701N6-succinyllysineBy similarity

Post-translational modificationi

A 165 kDa form is probably produced by proteolytic cleavage at Lys-124.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP09884.
PaxDbiP09884.
PRIDEiP09884.

PTM databases

PhosphoSiteiP09884.

Expressioni

Gene expression databases

BgeeiP09884.
CleanExiHS_POLA1.
ExpressionAtlasiP09884. baseline and differential.
GenevisibleiP09884. HS.

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. 47 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
Beta strandi340 – 35011Combined sources
Turni352 – 3543Combined sources
Beta strandi359 – 3679Combined sources
Helixi368 – 3703Combined sources
Beta strandi372 – 3809Combined sources
Beta strandi385 – 3917Combined sources
Beta strandi393 – 3964Combined sources
Turni398 – 4003Combined sources
Beta strandi403 – 4075Combined sources
Helixi410 – 41910Combined sources
Helixi421 – 4255Combined sources
Beta strandi431 – 4388Combined sources
Beta strandi448 – 45710Combined sources
Beta strandi471 – 4777Combined sources
Helixi483 – 4919Combined sources
Beta strandi495 – 5039Combined sources
Beta strandi512 – 52211Combined sources
Helixi523 – 5253Combined sources
Beta strandi526 – 5294Combined sources
Beta strandi537 – 54812Combined sources
Beta strandi550 – 5523Combined sources
Beta strandi555 – 56814Combined sources
Beta strandi570 – 5723Combined sources
Beta strandi576 – 5783Combined sources
Beta strandi580 – 5867Combined sources
Helixi598 – 6058Combined sources
Beta strandi609 – 6113Combined sources
Helixi615 – 62915Combined sources
Beta strandi632 – 6387Combined sources
Turni639 – 6424Combined sources
Helixi643 – 65311Combined sources
Helixi659 – 6624Combined sources
Beta strandi663 – 6653Combined sources
Helixi679 – 6846Combined sources
Turni685 – 6873Combined sources
Beta strandi688 – 6925Combined sources
Helixi693 – 7008Combined sources
Helixi708 – 7169Combined sources
Helixi725 – 7328Combined sources
Helixi735 – 75824Combined sources
Helixi761 – 77212Combined sources
Helixi776 – 7794Combined sources
Helixi785 – 79814Combined sources
Beta strandi850 – 8523Combined sources
Beta strandi856 – 8616Combined sources
Helixi864 – 8718Combined sources
Turni876 – 8783Combined sources
Helixi910 – 93021Combined sources
Beta strandi931 – 9333Combined sources
Helixi936 – 96025Combined sources
Helixi970 – 99324Combined sources
Beta strandi997 – 10004Combined sources
Beta strandi1002 – 10098Combined sources
Helixi1015 – 103016Combined sources
Beta strandi1038 – 105114Combined sources
Beta strandi1054 – 10629Combined sources
Beta strandi1068 – 10769Combined sources
Helixi1078 – 10803Combined sources
Beta strandi1082 – 10843Combined sources
Helixi1086 – 109914Combined sources
Beta strandi1101 – 11033Combined sources
Helixi1105 – 112521Combined sources
Helixi1130 – 11334Combined sources
Beta strandi1135 – 11384Combined sources
Helixi1143 – 11453Combined sources
Helixi1149 – 11513Combined sources
Helixi1153 – 116412Combined sources
Beta strandi1165 – 11673Combined sources
Beta strandi1174 – 11818Combined sources
Helixi1188 – 11903Combined sources
Helixi1195 – 12006Combined sources
Helixi1208 – 12147Combined sources
Helixi1216 – 12249Combined sources
Helixi1232 – 12387Combined sources
Helixi1269 – 12724Combined sources
Turni1273 – 12753Combined sources
Beta strandi1279 – 12824Combined sources
Turni1284 – 12863Combined sources
Beta strandi1289 – 129810Combined sources
Helixi1319 – 13224Combined sources
Helixi1323 – 134220Combined sources
Beta strandi1346 – 13494Combined sources
Turni1351 – 13533Combined sources
Beta strandi1356 – 13583Combined sources
Beta strandi1359 – 13624Combined sources
Beta strandi1364 – 13674Combined sources
Beta strandi1368 – 13703Combined sources
Beta strandi1372 – 138312Combined sources
Helixi1385 – 139713Combined sources
Helixi1401 – 14066Combined sources
Helixi1411 – 142010Combined sources
Helixi1424 – 143411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0PNMR-A1347-1377[»]
1K18NMR-A1347-1377[»]
1N5GNMR-A1345-1382[»]
4Q5VX-ray2.52A/E336-1257[»]
4QCLX-ray2.20A336-1257[»]
4Y97X-ray2.51B/D/F/H1265-1444[»]
ProteinModelPortaliP09884.
SMRiP09884. Positions 338-1244, 1345-1382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09884.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni650 – 71566DNA-binding regionSequence AnalysisAdd
BLAST
Regioni1245 – 1376132DNA-binding regionSequence AnalysisAdd
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

Belongs to the DNA polymerase type-B family.Curated
Contains 1 CysA-type zinc finger.Curated

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0417.
GeneTreeiENSGT00550000074891.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
InParanoidiP09884.
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.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PANTHERiPTHR10322:SF18. PTHR10322:SF18. 1 hit.
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

        10         20         30         40         50
MAPVHGDDSL SDSGSFVSSR ARREKKSKKG RQEALERLKK AKAGEKYKYE
60 70 80 90 100
VEDFTGVYEE VDEEQYSKLV QARQDDDWIV DDDGIGYVED GREIFDDDLE
110 120 130 140 150
DDALDADEKG KDGKARNKDK RNVKKLAVTK PNNIKSMFIA CAGKKTADKA
160 170 180 190 200
VDLSKDGLLG DILQDLNTET PQITPPPVMI LKKKRSIGAS PNPFSVHTAT
210 220 230 240 250
AVPSGKIASP VSRKEPPLTP VPLKRAEFAG DDVQVESTEE EQESGAMEFE
260 270 280 290 300
DGDFDEPMEV EEVDLEPMAA KAWDKESEPA EEVKQEADSG KGTVSYLGSF
310 320 330 340 350
LPDVSCWDID QEGDSSFSVQ EVQVDSSHLP LVKGADEEQV FHFYWLDAYE
360 370 380 390 400
DQYNQPGVVF LFGKVWIESA ETHVSCCVMV KNIERTLYFL PREMKIDLNT
410 420 430 440 450
GKETGTPISM KDVYEEFDEK IATKYKIMKF KSKPVEKNYA FEIPDVPEKS
460 470 480 490 500
EYLEVKYSAE MPQLPQDLKG ETFSHVFGTN TSSLELFLMN RKIKGPCWLE
510 520 530 540 550
VKSPQLLNQP VSWCKVEAMA LKPDLVNVIK DVSPPPLVVM AFSMKTMQNA
560 570 580 590 600
KNHQNEIIAM AALVHHSFAL DKAAPKPPFQ SHFCVVSKPK DCIFPYAFKE
610 620 630 640 650
VIEKKNVKVE VAATERTLLG FFLAKVHKID PDIIVGHNIY GFELEVLLQR
660 670 680 690 700
INVCKAPHWS KIGRLKRSNM PKLGGRSGFG ERNATCGRMI CDVEISAKEL
710 720 730 740 750
IRCKSYHLSE LVQQILKTER VVIPMENIQN MYSESSQLLY LLEHTWKDAK
760 770 780 790 800
FILQIMCELN VLPLALQITN IAGNIMSRTL MGGRSERNEF LLLHAFYENN
810 820 830 840 850
YIVPDKQIFR KPQQKLGDED EEIDGDTNKY KKGRKKAAYA GGLVLDPKVG
860 870 880 890 900
FYDKFILLLD FNSLYPSIIQ EFNICFTTVQ RVASEAQKVT EDGEQEQIPE
910 920 930 940 950
LPDPSLEMGI LPREIRKLVE RRKQVKQLMK QQDLNPDLIL QYDIRQKALK
960 970 980 990 1000
LTANSMYGCL GFSYSRFYAK PLAALVTYKG REILMHTKEM VQKMNLEVIY
1010 1020 1030 1040 1050
GDTDSIMINT NSTNLEEVFK LGNKVKSEVN KLYKLLEIDI DGVFKSLLLL
1060 1070 1080 1090 1100
KKKKYAALVV EPTSDGNYVT KQELKGLDIV RRDWCDLAKD TGNFVIGQIL
1110 1120 1130 1140 1150
SDQSRDTIVE NIQKRLIEIG ENVLNGSVPV SQFEINKALT KDPQDYPDKK
1160 1170 1180 1190 1200
SLPHVHVALW INSQGGRKVK AGDTVSYVIC QDGSNLTASQ RAYAPEQLQK
1210 1220 1230 1240 1250
QDNLTIDTQY YLAQQIHPVV ARICEPIDGI DAVLIATWLG LDPTQFRVHH
1260 1270 1280 1290 1300
YHKDEENDAL LGGPAQLTDE EKYRDCERFK CPCPTCGTEN IYDNVFDGSG
1310 1320 1330 1340 1350
TDMEPSLYRC SNIDCKASPL TFTVQLSNKL IMDIRRFIKK YYDGWLICEE
1360 1370 1380 1390 1400
PTCRNRTRHL PLQFSRTGPL CPACMKATLQ PEYSDKSLYT QLCFYRYIFD
1410 1420 1430 1440 1450
AECALEKLTT DHEKDKLKKQ FFTPKVLQDY RKLKNTAEQF LSRSGYSEVN
1460
LSKLFAGCAV KS
Length:1,462
Mass (Da):165,913
Last modified:February 1, 2005 - v2
Checksum:iDC40C3EDD6F4B495
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti503 – 5064SPQL → KSTA in CAA29920 (PubMed:3359994).Curated
Sequence conflicti837 – 8371A → G in CAA29920 (PubMed:3359994).Curated
Sequence conflicti1405 – 14051L → C AA sequence (PubMed:2243771).Curated
Sequence conflicti1426 – 14261V → C AA sequence (PubMed:2243771).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0PNMR-A1347-1377[»]
1K18NMR-A1347-1377[»]
1N5GNMR-A1345-1382[»]
4Q5VX-ray2.52A/E336-1257[»]
4QCLX-ray2.20A336-1257[»]
4Y97X-ray2.51B/D/F/H1265-1444[»]
ProteinModelPortaliP09884.
SMRiP09884. Positions 338-1244, 1345-1382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111418. 47 interactions.
IntActiP09884. 10 interactions.
MINTiMINT-1517478.
STRINGi9606.ENSP00000368349.

Chemistry

BindingDBiP09884.
ChEMBLiCHEMBL2363042.
DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB01280. Nelarabine.

PTM databases

PhosphoSiteiP09884.

Polymorphism and mutation databases

BioMutaiPOLA1.
DMDMi60392197.

Proteomic databases

MaxQBiP09884.
PaxDbiP09884.
PRIDEiP09884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5422.
GeneCardsiGC0XP024712.
H-InvDBHIX0028476.
HGNCiHGNC:9173. POLA1.
HPAiCAB012274.
HPA002947.
MIMi312040. gene.
neXtProtiNX_P09884.
PharmGKBiPA162399856.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0417.
GeneTreeiENSGT00550000074891.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
InParanoidiP09884.
KOiK02320.
PhylomeDBiP09884.
TreeFamiTF103001.

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.

Miscellaneous databases

ChiTaRSiPOLA1. human.
EvolutionaryTraceiP09884.
GeneWikiiPolymerase_(DNA_directed),_alpha_1.
GenomeRNAii5422.
NextBioi20977.
PROiP09884.
SOURCEiSearch...

Gene expression databases

BgeeiP09884.
CleanExiHS_POLA1.
ExpressionAtlasiP09884. baseline and differential.
GenevisibleiP09884. HS.

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.
IPR029702. POLA/Pol1.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]
PANTHERiPTHR10322:SF18. PTHR10322:SF18. 1 hit.
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]
ProtoNetiSearch...

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: July 22, 2015
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.