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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)DescriptionActionsGraphical viewLength
Metal bindingi1283ZincBy similarity1
Metal bindingi1286ZincBy similarity1
Metal bindingi1310ZincBy similarity1
Metal bindingi1315ZincBy similarity1
Metal bindingi1348Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1353Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1371Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi1374Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1283 – 1315CysA-typeAdd BLAST33

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 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
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  • telomere maintenance via recombination 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

BioCyciZFISH:HS02310-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-174430. Telomere C-strand synthesis initiation.
R-HSA-68952. DNA replication initiation.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69091. Polymerase switching.
R-HSA-69166. Removal of the Flap Intermediate.
R-HSA-69183. Processive synthesis on the lagging strand.
R-HSA-69205. G1/S-Specific Transcription.

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
Proteomesi
  • UP000005640 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

DisGeNETi5422.
MalaCardsiPOLA1.
OpenTargetsiENSG00000101868.
PharmGKBiPA162399856.

Chemistry databases

ChEMBLiCHEMBL1828.
DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB01280. Nelarabine.

Polymorphism and mutation databases

BioMutaiPOLA1.
DMDMi60392197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464281 – 1462DNA polymerase alpha catalytic subunitAdd BLAST1462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei174PhosphothreonineCombined sources1
Modified residuei186PhosphoserineCombined sources1
Modified residuei190PhosphoserineCombined sources1
Modified residuei209PhosphoserineCombined sources1
Modified residuei224N6-acetyllysineBy similarity1
Modified residuei406PhosphothreonineCombined sources1
Modified residuei970N6-succinyllysineBy similarity1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei124 – 125Cleavage2

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09884.
MaxQBiP09884.
PaxDbiP09884.
PeptideAtlasiP09884.
PRIDEiP09884.

PTM databases

iPTMnetiP09884.
PhosphoSitePlusiP09884.

Expressioni

Gene expression databases

BgeeiENSG00000101868.
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.

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111418. 54 interactors.
IntActiP09884. 12 interactors.
MINTiMINT-1517478.
STRINGi9606.ENSP00000368349.

Chemistry databases

BindingDBiP09884.

Structurei

Secondary structure

11462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi340 – 350Combined sources11
Turni352 – 354Combined sources3
Beta strandi359 – 367Combined sources9
Helixi368 – 370Combined sources3
Beta strandi372 – 380Combined sources9
Beta strandi385 – 391Combined sources7
Beta strandi393 – 396Combined sources4
Turni398 – 400Combined sources3
Beta strandi403 – 407Combined sources5
Helixi410 – 419Combined sources10
Helixi421 – 425Combined sources5
Beta strandi431 – 438Combined sources8
Beta strandi441 – 445Combined sources5
Beta strandi448 – 457Combined sources10
Beta strandi471 – 477Combined sources7
Helixi483 – 491Combined sources9
Beta strandi495 – 503Combined sources9
Beta strandi512 – 522Combined sources11
Helixi523 – 525Combined sources3
Beta strandi526 – 529Combined sources4
Beta strandi537 – 548Combined sources12
Beta strandi550 – 552Combined sources3
Beta strandi555 – 568Combined sources14
Beta strandi570 – 572Combined sources3
Beta strandi576 – 578Combined sources3
Beta strandi580 – 586Combined sources7
Helixi598 – 605Combined sources8
Beta strandi609 – 611Combined sources3
Helixi615 – 629Combined sources15
Beta strandi632 – 638Combined sources7
Turni639 – 642Combined sources4
Helixi643 – 653Combined sources11
Helixi659 – 662Combined sources4
Beta strandi663 – 665Combined sources3
Helixi679 – 684Combined sources6
Turni685 – 687Combined sources3
Beta strandi688 – 692Combined sources5
Helixi693 – 700Combined sources8
Helixi708 – 716Combined sources9
Helixi725 – 732Combined sources8
Helixi735 – 758Combined sources24
Helixi761 – 772Combined sources12
Helixi776 – 779Combined sources4
Helixi785 – 798Combined sources14
Beta strandi850 – 852Combined sources3
Beta strandi856 – 861Combined sources6
Helixi864 – 871Combined sources8
Turni876 – 878Combined sources3
Helixi910 – 930Combined sources21
Beta strandi931 – 933Combined sources3
Helixi936 – 960Combined sources25
Helixi970 – 993Combined sources24
Beta strandi997 – 1000Combined sources4
Beta strandi1002 – 1009Combined sources8
Helixi1015 – 1030Combined sources16
Beta strandi1038 – 1051Combined sources14
Beta strandi1054 – 1062Combined sources9
Beta strandi1068 – 1076Combined sources9
Helixi1078 – 1080Combined sources3
Beta strandi1082 – 1084Combined sources3
Helixi1086 – 1099Combined sources14
Beta strandi1101 – 1103Combined sources3
Helixi1105 – 1125Combined sources21
Helixi1130 – 1133Combined sources4
Beta strandi1135 – 1138Combined sources4
Helixi1143 – 1145Combined sources3
Helixi1149 – 1151Combined sources3
Helixi1153 – 1164Combined sources12
Beta strandi1165 – 1167Combined sources3
Beta strandi1174 – 1181Combined sources8
Helixi1188 – 1190Combined sources3
Helixi1195 – 1200Combined sources6
Helixi1208 – 1214Combined sources7
Helixi1216 – 1224Combined sources9
Beta strandi1225 – 1227Combined sources3
Helixi1232 – 1238Combined sources7
Helixi1269 – 1272Combined sources4
Turni1273 – 1275Combined sources3
Beta strandi1279 – 1282Combined sources4
Turni1284 – 1286Combined sources3
Beta strandi1289 – 1298Combined sources10
Helixi1319 – 1322Combined sources4
Helixi1323 – 1342Combined sources20
Beta strandi1346 – 1349Combined sources4
Turni1351 – 1353Combined sources3
Beta strandi1356 – 1358Combined sources3
Beta strandi1359 – 1362Combined sources4
Beta strandi1364 – 1367Combined sources4
Beta strandi1368 – 1370Combined sources3
Beta strandi1372 – 1383Combined sources12
Helixi1385 – 1397Combined sources13
Helixi1401 – 1406Combined sources6
Helixi1411 – 1420Combined sources10
Helixi1424 – 1434Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5EXRX-ray3.60C/G335-1462[»]
5IUDX-ray3.30A/D/G/J338-1255[»]
ProteinModelPortaliP09884.
SMRiP09884.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09884.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni650 – 715DNA-binding regionSequence analysisAdd BLAST66
Regioni1245 – 1376DNA-binding regionSequence analysisAdd BLAST132

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1348 – 1374CysB motifAdd BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi75 – 112Asp-richAdd BLAST38
Compositional biasi1047 – 1050Poly-Leu4
Compositional biasi1051 – 1054Poly-Lys4

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)DescriptionActionsGraphical viewLength
Zinc fingeri1283 – 1315CysA-typeAdd BLAST33

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
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:SF21. PTHR10322:SF21. 4 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti503 – 506SPQL → KSTA in CAA29920 (PubMed:3359994).Curated4
Sequence conflicti837A → G in CAA29920 (PubMed:3359994).Curated1
Sequence conflicti1405L → C AA sequence (PubMed:2243771).Curated1
Sequence conflicti1426V → C AA sequence (PubMed:2243771).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048877740Y → H.Corresponds to variant rs2230927dbSNPEnsembl.1

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.4. 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
PDB 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[»]
5EXRX-ray3.60C/G335-1462[»]
5IUDX-ray3.30A/D/G/J338-1255[»]
ProteinModelPortaliP09884.
SMRiP09884.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111418. 54 interactors.
IntActiP09884. 12 interactors.
MINTiMINT-1517478.
STRINGi9606.ENSP00000368349.

Chemistry databases

BindingDBiP09884.
ChEMBLiCHEMBL1828.
DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB01280. Nelarabine.

PTM databases

iPTMnetiP09884.
PhosphoSitePlusiP09884.

Polymorphism and mutation databases

BioMutaiPOLA1.
DMDMi60392197.

Proteomic databases

EPDiP09884.
MaxQBiP09884.
PaxDbiP09884.
PeptideAtlasiP09884.
PRIDEiP09884.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379059; ENSP00000368349; ENSG00000101868.
GeneIDi5422.
KEGGihsa:5422.
UCSCiuc004dbl.4. human.

Organism-specific databases

CTDi5422.
DisGeNETi5422.
GeneCardsiPOLA1.
H-InvDBHIX0028476.
HGNCiHGNC:9173. POLA1.
HPAiCAB012274.
HPA002947.
MalaCardsiPOLA1.
MIMi312040. gene.
neXtProtiNX_P09884.
OpenTargetsiENSG00000101868.
PharmGKBiPA162399856.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0970. Eukaryota.
COG0417. LUCA.
GeneTreeiENSGT00550000074891.
HOGENOMiHOG000163524.
HOVERGENiHBG080008.
InParanoidiP09884.
KOiK02320.
PhylomeDBiP09884.
TreeFamiTF103001.

Enzyme and pathway databases

BioCyciZFISH:HS02310-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-174411. Polymerase switching on the C-strand of the telomere.
R-HSA-174430. Telomere C-strand synthesis initiation.
R-HSA-68952. DNA replication initiation.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69091. Polymerase switching.
R-HSA-69166. Removal of the Flap Intermediate.
R-HSA-69183. Processive synthesis on the lagging strand.
R-HSA-69205. G1/S-Specific Transcription.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000101868.
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:SF21. PTHR10322:SF21. 4 hits.
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...

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: November 2, 2016
This is version 172 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

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 one 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.