P33609

PR
Gene name
Pola1 (Pola)
Protein name
DNA polymerase alpha catalytic subunit
Names
DNA polymerase alpha catalytic subunit p180
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:18968
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

79-359 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P33609

Entry ID Method Resolution Chain Position Source
AF-P33609-F1 Predicted AlphaFoldDB

81 variants for P33609

Variant ID(s) Position Change Description Diseaes Association Provenance
rs239789249 13 A>T No EVA
rs3411504205 53 Y>A No EVA
rs3411280892 54 K>* No EVA
rs3411241560 54 K>I No EVA
rs3389569781 58 E>G No EVA
rs215933899 60 L>F No EVA
rs3411013174 64 Y>* No EVA
rs3389525468 71 Q>R No EVA
rs3409829542 91 I>L No EVA
rs233182249 113 C>Y No EVA
rs3389579052 135 T>K No EVA
rs3389582471 146 A>D No EVA
rs3389571809 168 I>F No EVA
rs3411391487 213 P>L No EVA
rs3411280908 213 P>T No EVA
rs3411170293 218 L>F No EVA
rs3411013246 218 L>P No EVA
rs3411280835 220 N>K No EVA
rs3409827336 223 L>P No EVA
rs3411013187 227 I>V No EVA
rs3389566874 230 K>I No EVA
rs3411125487 240 Q>E No EVA
rs233982093 283 T>I No EVA
rs252904871 283 T>S No EVA
rs220634646 288 R>K No EVA
rs29069945 305 N>S No EVA
rs3389579134 322 I>K No EVA
rs3389561859 365 L>R No EVA
rs3389560314 374 V>I No EVA
rs3389576611 385 K>E No EVA
rs3389475311 385 K>I No EVA
rs3389579074 395 P>S No EVA
rs1134094846 409 A>S No EVA
rs3389566871 444 A>D No EVA
rs3389560334 479 H>L No EVA
rs3409827341 587 F>I No EVA
rs3411331895 587 F>S No EVA
rs3411279148 628 A>E No EVA
rs3411012593 630 V>D No EVA
rs3411503008 630 V>I No EVA
rs3409716266 631 H>Q No EVA
rs3411503017 632 K>T No EVA
rs3411331903 633 I>L No EVA
rs3411122494 634 D>A No EVA
rs3411331886 634 D>Y No EVA
rs3389566830 684 G>C No EVA
rs3411122479 702 K>T No EVA
rs3389576637 725 I>N No EVA
rs3410319351 751 K>Q No EVA
rs3389547398 830 D>N No EVA
rs3389571856 831 T>I No EVA
rs217435687 842 T>A No EVA
rs258894373 844 A>T No EVA
rs3389582479 859 F>* No EVA
rs3389567705 897 E>D No EVA
rs239224712 902 I>V No EVA
rs3411169578 914 I>N No EVA
rs3411121141 915 L>M No EVA
rs3389534690 918 E>G No EVA
rs3411503026 920 R>W No EVA
rs3389582441 924 E>K No EVA
rs3389566854 930 K>* No EVA
rs3389582446 967 S>P No EVA
rs3389560351 980 V>M No EVA
rs3389560323 990 H>L No EVA
rs3409826532 1093 K>N No EVA
rs3411009338 1094 D>N No EVA
rs3411238370 1095 T>N No EVA
rs3411277967 1096 G>K* No EVA
rs3409712831 1096 G>R No EVA
rs3389571789 1155 S>G No EVA
rs3389569774 1160 H>L No EVA
rs3389579042 1176 G>S No EVA
1180 S>F temperature-sensitive FT20 cell line; defective activity [UniProt] No
rs3411119055 1192 A>T No EVA
rs3389564485 1224 V>M No EVA
rs3411167026 1229 E>G No EVA
rs3389515966 1231 I>V No EVA
rs3411329094 1307 M>I No EVA
rs3411009319 1309 P>A No EVA
rs3389561825 1403 F>L No EVA

No associated diseases with P33609

6 regional properties for P33609

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 375 - 714 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 779 - 1231 IPR006134
domain Zinc finger, DNA-directed DNA polymerase, family B, alpha 1270 - 1458 IPR015088
conserved_site DNA-directed DNA polymerase, family B, conserved site 1004 - 1012 IPR017964
domain DNA polymerase alpha catalytic subunit, N-terminal domain 41 - 102 IPR024647
domain DNA polymerase alpha catalytic subunit, catalytic domain 836 - 1246 IPR045846

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
  • Cytoplasm, cytosol
  • In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
alpha DNA polymerase:primase complex A complex of four polypeptides, comprising large and small DNA polymerase alpha subunits and two primase subunits, which are capable of catalyzing the synthesis of an RNA primer on the lagging strand of replicating DNA and the subsequent synthesis of a smal stretch of DNA. The smaller of the two primase subunits alone can catalyze oligoribonucleotide synthesis.
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
nuclear matrix The dense fibrillar network lying on the inner side of the nuclear membrane.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

11 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA replication origin binding Binding to a DNA replication origin, a unique DNA sequence of a replicon at which DNA replication is initiated and proceeds bidirectionally or unidirectionally.
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
double-stranded DNA binding Binding to double-stranded DNA.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
purine nucleotide binding Binding to a purine nucleotide, a compound consisting of a purine nucleoside esterified with (ortho)phosphate.
pyrimidine nucleotide binding Binding to a pyrimidine nucleotide, a pyrimidine nucleoside esterified with (ortho)phosphate.
single-stranded DNA binding Binding to single-stranded DNA.
zinc ion binding Binding to a zinc ion (Zn).

11 GO annotations of biological process

Name Definition
DNA biosynthetic process The biosynthetic process resulting in the formation of DNA.
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
DNA replication initiation The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.
DNA replication, synthesis of RNA primer The synthesis of a short RNA polymer, usually 4-15 nucleotides long, using one strand of unwound DNA as a template; the RNA then serves as a primer from which DNA polymerases extend synthesis.
DNA strand elongation involved in DNA replication The process in which an existing DNA strand is extended by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication.
DNA synthesis involved in DNA repair Synthesis of DNA that proceeds from the broken 3' single-strand DNA end and uses the homologous intact duplex as the template.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
lagging strand elongation The process in which an existing DNA strand is extended in a net 3' to 5' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Lagging strand DNA elongation proceeds by discontinuous synthesis of short stretches of DNA, known as Okazaki fragments, from RNA primers; these fragments are then joined by DNA ligase. Although each segment of nascent DNA is synthesized in the 5' to 3' direction, the overall direction of lagging strand synthesis is 3' to 5', mirroring the progress of the replication fork.
leading strand elongation The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork.
mitotic DNA replication initiation Any DNA replication initiation involved in mitotic cell cycle DNA replication.
regulation of type I interferon production Any process that modulates the frequency, rate, or extent of interferon type I production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P09884 POLA1 DNA polymerase alpha catalytic subunit Homo sapiens (Human) PR
O89042 Pola1 DNA polymerase alpha catalytic subunit Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MAPMHEEDCK LEASAVSDSG SFAASRARRE KKSKKGRQEA LERLKKAKAG EKYKYEVEDL
70 80 90 100 110 120
TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI FDDDLEDDAL DTCGKGSDGK
130 140 150 160 170 180
AHRKDRKDVK KPSVTKPNNI KAMFIASAGK KTTDKAVDLS KDDLLGDILQ DLNTETAQIT
190 200 210 220 230 240
PPPVLIPKKK RSTGALLNPF SVHTPKAIPS GKPASPVLRN EPLLTPIPLK RAELAGELAQ
250 260 270 280 290 300
PECPEDEQEL GVMEFEDGDF DESMDTEKVD EKPVTAKTWD QETEPVERVE HEADPERGTT
310 320 330 340 350 360
SYLENFLPDV SCWDIDQDDE SIPQEVQVDS SNLPLVKGAD DEQVFQFYWL DAYEDPYNQP
370 380 390 400 410 420
GVVFLFGKVW IESVKTHVSC CVMVKNIERT LYFLPREMKF DLNTGKETAI PVTMKDVYEE
430 440 450 460 470 480
FDSKISAKYK IMKFKSKIVE KNYAFEIPDV PEKSEYLEVR YSAEVPQLPQ NLKGETFSHV
490 500 510 520 530 540
FGTNTSSLEL FLMNRKIKGP CWLEVKNPQL LNQPISWCKF EVMALKPDLV NVIKDVSPPP
550 560 570 580 590 600
LVVMSFSMKT MQNVQNHQHE IIAMAALVHH SFALDKAPPE PPFQTHFCVV SKPKDCIFPC
610 620 630 640 650 660
DFKEVISKKN MKVEIAATER TLIGFFLAKV HKIDPDILVG HNICSFELEV LLQRINECKV
670 680 690 700 710 720
PYWSKIGRLR RSNMPKLGSR SGFGERNATC GRMICDVEIS AKELIHCKSY HLSELVQQIL
730 740 750 760 770 780
KTERIVIPTE NIRNMYSESS YLLYLLEHIW KDARFILQIM CELNVLPLAL QITNIAGNIM
790 800 810 820 830 840
SRTLMGGRSE RNEFLLLHAF YENNYIVPDK QIFRKPQQKL GDEDEEIDGD TNKYKKGRKK
850 860 870 880 890 900
ATYAGGLVLD PKVGFYDKFI LLLDFNSLYP SIIQEFNICF TTVQRVTSEV QKATEDEEQE
910 920 930 940 950 960
QIPELPDPNL EMGILPREIR KLVERRKQVK QLMKQQDLNP DLVLQYDIRQ KALKLTANSM
970 980 990 1000 1010 1020
YGCLGFSYSR FYAKPLAALV TYKGREILMH TKDMVQKMNL EVIYGDTDSI MINTNSTNLE
1030 1040 1050 1060 1070 1080
EVFKLGNKVK SEVNKLYKLL EIDIDAVFKS LLLLKKKKYA ALVVEPTSDG NYITKQELKG
1090 1100 1110 1120 1130 1140
LDIVRRDWCD LAKDTGNFVI GQILSDQSRD TIVENIQKRL IEIGENVLNG SVPVSQFEIN
1150 1160 1170 1180 1190 1200
KALTKDPQDY PDRKSLPHVH VALWINSQGG RKVKAGDTVS YVICQDGSNL TATQRAYAPE
1210 1220 1230 1240 1250 1260
QLQKLDNLAI DTQYYLAQQI HPVVARICEP IDGIDAVLIA LWLGLDSTQF RVHQYHKDEE
1270 1280 1290 1300 1310 1320
NDALLGGPAQ LTDEEKYKDC EKFKCLCPSC GTENIYDNVF EGSGLDMEPS LYRCSNVDCK
1330 1340 1350 1360 1370 1380
VSPLTFMVQL SNKLIMDIRR CIKKYYDGWL ICEEPTCCSR LRRLPLHFSR NGPLCPVCMK
1390 1400 1410 1420 1430 1440
AVLRPEYSDK SLYTQLCFYR YIFDADCALE KLTEHEKDKL KKQFFPLRVL QDYRKVKNIA
1450 1460
EQFLSWSGYS EVNLSKLFAN YAGKS