UniProtKB - P33609 (DPOLA_MOUSE)
DNA polymerase alpha catalytic subunit
Pola1
Functioni
Miscellaneous
Catalytic activityi
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 1287 | ZincBy similarity | 1 | |
Metal bindingi | 1290 | ZincBy similarity | 1 | |
Metal bindingi | 1314 | ZincBy similarity | 1 | |
Metal bindingi | 1319 | ZincBy similarity | 1 | |
Metal bindingi | 1352 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1357 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1375 | Iron-sulfur (4Fe-4S)By similarity | 1 | |
Metal bindingi | 1378 | Iron-sulfur (4Fe-4S)By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1287 – 1317 | CysA-typeAdd BLAST | 31 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
- chromatin binding Source: UniProtKB
- DNA binding Source: UniProtKB
- DNA-directed DNA polymerase activity Source: MGI
- DNA replication origin binding Source: GO_Central
- double-stranded DNA binding Source: MGI
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: UniProtKB
- protein kinase binding Source: MGI
- purine nucleotide binding Source: MGI
- pyrimidine nucleotide binding Source: MGI
- single-stranded DNA binding Source: GO_Central
GO - Biological processi
- DNA biosynthetic process Source: MGI
- DNA replication Source: MGI
- DNA replication, synthesis of RNA primer Source: UniProtKB
- DNA replication initiation Source: UniProtKB
- DNA strand elongation involved in DNA replication Source: UniProtKB
- DNA synthesis involved in DNA repair Source: MGI
- double-strand break repair via nonhomologous end joining Source: UniProtKB
- lagging strand elongation Source: UniProtKB
- leading strand elongation Source: UniProtKB
- mitotic DNA replication initiation Source: GO_Central
- regulation of type I interferon production Source: UniProtKB
Keywordsi
Molecular function | DNA-binding, DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase |
Biological process | DNA replication |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1 R-MMU-174411, Polymerase switching on the C-strand of the telomere R-MMU-174430, Telomere C-strand synthesis initiation R-MMU-68952, DNA replication initiation R-MMU-68962, Activation of the pre-replicative complex R-MMU-69091, Polymerase switching R-MMU-69166, Removal of the Flap Intermediate R-MMU-69183, Processive synthesis on the lagging strand |
Names & Taxonomyi
Protein namesi | Recommended name: DNA polymerase alpha catalytic subunit (EC:2.7.7.72 Publications)Alternative name(s): DNA polymerase alpha catalytic subunit p180 |
Gene namesi | Name:Pola1 Synonyms:Pola |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99660, Pola1 |
Subcellular locationi
Cytosol
- cytosol Source: UniProtKB
Nucleus
- alpha DNA polymerase:primase complex Source: UniProtKB
- nuclear envelope Source: UniProtKB
- nuclear matrix Source: UniProtKB
- nucleolus Source: UniProtKB
- nucleoplasm Source: UniProtKB
- nucleus Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1008 | D → N: Results in loss of primer extension catalytic activity but retains ability to bind to the primase complex. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2797 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000046429 | 1 – 1465 | DNA polymerase alpha catalytic subunitAdd BLAST | 1465 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 180 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 192 | PhosphoserineBy similarity | 1 | |
Modified residuei | 215 | PhosphoserineCombined sources | 1 | |
Modified residuei | 230 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 974 | N6-succinyllysineCombined sources | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
EPDi | P33609 |
jPOSTi | P33609 |
MaxQBi | P33609 |
PaxDbi | P33609 |
PeptideAtlasi | P33609 |
PRIDEi | P33609 |
ProteomicsDBi | 279570 |
PTM databases
iPTMneti | P33609 |
PhosphoSitePlusi | P33609 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSMUSG00000006678, Expressed in embryonic stem cell and 233 other tissues |
Genevisiblei | P33609, MM |
Interactioni
Subunit structurei
Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the primase complex subunits PRIM1 and PRIM2 respectively (PubMed:8253737, PubMed:8026492). Within the complex, POLA1 directly interacts with PRIM2 (PubMed:8253737).
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 (By similarity).
By similarity2 PublicationsBinary interactionsi
Hide detailsGO - Molecular functioni
- protein kinase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 202287, 2 interactors |
ComplexPortali | CPX-2088, DNA polymerase alpha:primase complex |
CORUMi | P33609 |
IntActi | P33609, 4 interactors |
STRINGi | 10090.ENSMUSP00000006856 |
Miscellaneous databases
RNActi | P33609, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 654 – 719 | DNA-bindingSequence analysisAdd BLAST | 66 | |
Regioni | 1249 – 1380 | DNA-bindingSequence analysisAdd BLAST | 132 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 1352 – 1378 | CysB motifAdd BLAST | 27 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1287 – 1317 | CysA-typeAdd BLAST | 31 |
Keywords - Domaini
Zinc-fingerPhylogenomic databases
eggNOGi | KOG0970, Eukaryota |
GeneTreei | ENSGT00550000074891 |
HOGENOMi | CLU_001718_0_0_1 |
InParanoidi | P33609 |
OMAi | NIMPLAL |
OrthoDBi | 293315at2759 |
PhylomeDBi | P33609 |
TreeFami | TF103001 |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 1.10.3200.20, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro 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 IPR043502, DNA/RNA_pol_sf IPR024647, DNA_pol_a_cat_su_N IPR042087, DNA_pol_B_C IPR023211, DNA_pol_palm_dom_sf IPR038256, Pol_alpha_znc_sf IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR015088, Znf_DNA-dir_DNA_pol_B_alpha |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MAPMHEEDCK LEASAVSDSG SFAASRARRE KKSKKGRQEA LERLKKAKAG
60 70 80 90 100
EKYKYEVEDL TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI
110 120 130 140 150
FDDDLEDDAL DTCGKGSDGK AHRKDRKDVK KPSVTKPNNI KAMFIASAGK
160 170 180 190 200
KTTDKAVDLS KDDLLGDILQ DLNTETAQIT PPPVLIPKKK RSTGALLNPF
210 220 230 240 250
SVHTPKAIPS GKPASPVLRN EPLLTPIPLK RAELAGELAQ PECPEDEQEL
260 270 280 290 300
GVMEFEDGDF DESMDTEKVD EKPVTAKTWD QETEPVERVE HEADPERGTT
310 320 330 340 350
SYLENFLPDV SCWDIDQDDE SIPQEVQVDS SNLPLVKGAD DEQVFQFYWL
360 370 380 390 400
DAYEDPYNQP GVVFLFGKVW IESVKTHVSC CVMVKNIERT LYFLPREMKF
410 420 430 440 450
DLNTGKETAI PVTMKDVYEE FDSKISAKYK IMKFKSKIVE KNYAFEIPDV
460 470 480 490 500
PEKSEYLEVR YSAEVPQLPQ NLKGETFSHV FGTNTSSLEL FLMNRKIKGP
510 520 530 540 550
CWLEVKNPQL LNQPISWCKF EVMALKPDLV NVIKDVSPPP LVVMSFSMKT
560 570 580 590 600
MQNVQNHQHE IIAMAALVHH SFALDKAPPE PPFQTHFCVV SKPKDCIFPC
610 620 630 640 650
DFKEVISKKN MKVEIAATER TLIGFFLAKV HKIDPDILVG HNICSFELEV
660 670 680 690 700
LLQRINECKV PYWSKIGRLR RSNMPKLGSR SGFGERNATC GRMICDVEIS
710 720 730 740 750
AKELIHCKSY HLSELVQQIL KTERIVIPTE NIRNMYSESS YLLYLLEHIW
760 770 780 790 800
KDARFILQIM CELNVLPLAL QITNIAGNIM SRTLMGGRSE RNEFLLLHAF
810 820 830 840 850
YENNYIVPDK QIFRKPQQKL GDEDEEIDGD TNKYKKGRKK ATYAGGLVLD
860 870 880 890 900
PKVGFYDKFI LLLDFNSLYP SIIQEFNICF TTVQRVTSEV QKATEDEEQE
910 920 930 940 950
QIPELPDPNL EMGILPREIR KLVERRKQVK QLMKQQDLNP DLVLQYDIRQ
960 970 980 990 1000
KALKLTANSM YGCLGFSYSR FYAKPLAALV TYKGREILMH TKDMVQKMNL
1010 1020 1030 1040 1050
EVIYGDTDSI MINTNSTNLE EVFKLGNKVK SEVNKLYKLL EIDIDAVFKS
1060 1070 1080 1090 1100
LLLLKKKKYA ALVVEPTSDG NYITKQELKG LDIVRRDWCD LAKDTGNFVI
1110 1120 1130 1140 1150
GQILSDQSRD TIVENIQKRL IEIGENVLNG SVPVSQFEIN KALTKDPQDY
1160 1170 1180 1190 1200
PDRKSLPHVH VALWINSQGG RKVKAGDTVS YVICQDGSNL TATQRAYAPE
1210 1220 1230 1240 1250
QLQKLDNLAI DTQYYLAQQI HPVVARICEP IDGIDAVLIA LWLGLDSTQF
1260 1270 1280 1290 1300
RVHQYHKDEE NDALLGGPAQ LTDEEKYKDC EKFKCLCPSC GTENIYDNVF
1310 1320 1330 1340 1350
EGSGLDMEPS LYRCSNVDCK VSPLTFMVQL SNKLIMDIRR CIKKYYDGWL
1360 1370 1380 1390 1400
ICEEPTCCSR LRRLPLHFSR NGPLCPVCMK AVLRPEYSDK SLYTQLCFYR
1410 1420 1430 1440 1450
YIFDADCALE KLTEHEKDKL KKQFFPLRVL QDYRKVKNIA EQFLSWSGYS
1460
EVNLSKLFAN YAGKS
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 1180 | S → F in temperature-sensitive FT20 cell line; defective activity. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D13543 mRNA Translation: BAA40003.1 D17384 mRNA Translation: BAA04202.1 |
CCDSi | CCDS30272.1 |
PIRi | S45628 |
RefSeqi | NP_032918.1, NM_008892.2 |
Genome annotation databases
Ensembli | ENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678 |
GeneIDi | 18968 |
KEGGi | mmu:18968 |
UCSCi | uc009tss.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D13543 mRNA Translation: BAA40003.1 D17384 mRNA Translation: BAA04202.1 |
CCDSi | CCDS30272.1 |
PIRi | S45628 |
RefSeqi | NP_032918.1, NM_008892.2 |
3D structure databases
SMRi | P33609 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 202287, 2 interactors |
ComplexPortali | CPX-2088, DNA polymerase alpha:primase complex |
CORUMi | P33609 |
IntActi | P33609, 4 interactors |
STRINGi | 10090.ENSMUSP00000006856 |
Chemistry databases
ChEMBLi | CHEMBL2797 |
PTM databases
iPTMneti | P33609 |
PhosphoSitePlusi | P33609 |
Proteomic databases
EPDi | P33609 |
jPOSTi | P33609 |
MaxQBi | P33609 |
PaxDbi | P33609 |
PeptideAtlasi | P33609 |
PRIDEi | P33609 |
ProteomicsDBi | 279570 |
Protocols and materials databases
Antibodypediai | 498, 184 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000006856; ENSMUSP00000006856; ENSMUSG00000006678 |
GeneIDi | 18968 |
KEGGi | mmu:18968 |
UCSCi | uc009tss.2, mouse |
Organism-specific databases
CTDi | 5422 |
MGIi | MGI:99660, Pola1 |
Phylogenomic databases
eggNOGi | KOG0970, Eukaryota |
GeneTreei | ENSGT00550000074891 |
HOGENOMi | CLU_001718_0_0_1 |
InParanoidi | P33609 |
OMAi | NIMPLAL |
OrthoDBi | 293315at2759 |
PhylomeDBi | P33609 |
TreeFami | TF103001 |
Enzyme and pathway databases
Reactomei | R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1 R-MMU-174411, Polymerase switching on the C-strand of the telomere R-MMU-174430, Telomere C-strand synthesis initiation R-MMU-68952, DNA replication initiation R-MMU-68962, Activation of the pre-replicative complex R-MMU-69091, Polymerase switching R-MMU-69166, Removal of the Flap Intermediate R-MMU-69183, Processive synthesis on the lagging strand |
Miscellaneous databases
BioGRID-ORCSi | 18968, 17 hits in 53 CRISPR screens |
ChiTaRSi | Pola1, mouse |
PROi | PR:P33609 |
RNActi | P33609, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000006678, Expressed in embryonic stem cell and 233 other tissues |
Genevisiblei | P33609, MM |
Family and domain databases
Gene3Di | 1.10.132.60, 1 hit 1.10.3200.20, 1 hit 3.30.420.10, 1 hit 3.90.1600.10, 1 hit |
InterProi | View protein in InterPro 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 IPR043502, DNA/RNA_pol_sf IPR024647, DNA_pol_a_cat_su_N IPR042087, DNA_pol_B_C IPR023211, DNA_pol_palm_dom_sf IPR038256, Pol_alpha_znc_sf IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf IPR015088, Znf_DNA-dir_DNA_pol_B_alpha |
Pfami | View protein in Pfam 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 |
PRINTSi | PR00106, DNAPOLB |
SMARTi | View protein in SMART SM00486, POLBc, 1 hit |
SUPFAMi | SSF53098, SSF53098, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS00116, DNA_POLYMERASE_B, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DPOLA_MOUSE | |
Accessioni | P33609Primary (citable) accession number: P33609 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | April 7, 2021 | |
This is version 174 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families