P52431

PR
Gene name
Pold1
Protein name
DNA polymerase delta catalytic subunit
Names
3'-5' exodeoxyribonuclease
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:18971
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)

1-143 (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 P52431

Entry ID Method Resolution Chain Position Source
AF-P52431-F1 Predicted AlphaFoldDB

55 variants for P52431

Variant ID(s) Position Change Description Diseaes Association Provenance
rs51625983 11 P>S No EVA
rs3397912161 13 V>G No EVA
rs3397823889 14 P>T No EVA
rs3388893787 17 R>W No EVA
rs3388879993 71 A>V No EVA
rs3388880006 75 P>S No EVA
rs50640891 83 R>H No EVA
rs3388887944 94 F>I No EVA
rs3397079063 96 Q>L No EVA
rs6201929 114 L>P No EVA
rs3388904553 149 P>L No EVA
rs6200825 175 R>H No EVA
rs3388885434 179 E>K No EVA
rs3388903461 217 L>P No EVA
rs3388906819 230 R>L No EVA
rs3388906506 293 V>A No EVA
rs3388910452 350 R>C No EVA
rs3388904484 371 R>L No EVA
rs3388907014 375 L>Q No EVA
rs3388866990 413 V>M No EVA
rs3388866935 418 F>Y No EVA
rs3388879964 428 N>S No EVA
rs3388879948 474 A>V No EVA
rs3388887979 518 L>F No EVA
rs3388903497 522 E>K No EVA
rs3388879955 554 V>M No EVA
rs3719256 576 S>G No EVA
rs3388899240 585 I>F No EVA
rs3388866998 589 K>R No EVA
rs3388908644 600 D>E No EVA
rs3388902274 607 S>P No EVA
rs3388909836 619 L>P No EVA
rs3388864301 622 P>L No EVA
rs3388899235 623 G>W No EVA
rs3388904520 625 A>V No EVA
rs3388879998 642 D>N No EVA
rs3397441569 690 A>V No EVA
rs3388908646 736 K>M No EVA
rs223460663 739 V>M No EVA
rs31839949 744 D>N No EVA
rs259030498 746 N>D No EVA
rs3388902193 811 L>H No EVA
rs3388906600 818 A>T No EVA
rs3388904565 842 V>I No EVA
rs3388885499 920 V>F No EVA
rs3388902234 943 V>M No EVA
rs3388909840 968 F>L No EVA
rs264695398 1023 V>M No EVA
rs3397849364 1058 R>S No EVA
rs3397838048 1060 Q>H No EVA
rs3397784860 1060 Q>P No EVA
rs3397784924 1073 D>V No EVA
rs3397605747 1076 I>T No EVA
rs3397823910 1081 K>M* No EVA
rs224648821 1102 P>S No EVA

No associated diseases with P52431

4 regional properties for P52431

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 129 - 475 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 540 - 971 IPR006134
conserved_site DNA-directed DNA polymerase, family B, conserved site 751 - 759 IPR017964
domain C4-type zinc-finger of DNA polymerase delta 1010 - 1080 IPR025687

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
  • Colocalizes with PCNA and POLD3 at S phase replication sites
  • After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination
  • This recruitment requires POLD3, PCNA and RFC1-replication factor C complex
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
aggresome An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules.
chromosome, telomeric region The end of a linear chromosome, required for the integrity and maintenance of the end. A chromosome telomere usually includes a region of telomerase-encoded repeats the length of which rarely exceeds 20 bp each and that permits the formation of a telomeric loop (T-loop). The telomeric repeat region is usually preceded by a sub-telomeric region that is gene-poor but rich in repetitive elements. Some telomeres only consist of the latter part (for eg. D. melanogaster telomeres).
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
delta DNA polymerase complex A multimeric DNA polymerase enzyme complex which differs in composition amongst species; in humans it is a heterotetramer of four subunits of approximately 125, 50, 68 and 12kDa, while in S. cerevisiae, it has three different subunits which form a heterotrimer, and the active enzyme is a dimer of this heterotrimer. Functions in DNA replication, mismatch repair and excision repair.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleotide-excision repair complex Any complex formed of proteins that act in nucleotide-excision repair.
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.

10 GO annotations of molecular function

Name Definition
3'-5' exonuclease activity Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
3'-5'-exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule.
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
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.
damaged DNA binding Binding to damaged DNA.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
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.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
metal ion binding Binding to a metal ion.
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.

10 GO annotations of biological process

Name Definition
base-excision repair, gap-filling Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template.
cellular response to UV Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ultraviolet radiation (UV light) stimulus. Ultraviolet radiation is electromagnetic radiation with a wavelength in the range of 10 to 380 nanometers.
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 proofreading Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
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.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
error-free translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
fatty acid homeostasis Any process involved in the maintenance of an internal steady state of fatty acid within an organism or cell.
nucleotide-excision repair, DNA gap filling Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P28339 POLD1 DNA polymerase delta catalytic subunit Bos taurus (Bovine) PR
P54358 PolD1 DNA polymerase delta catalytic subunit Drosophila melanogaster (Fruit fly) PR
P28340 POLD1 DNA polymerase delta catalytic subunit Homo sapiens (Human) PR
O54747 Pold1 DNA polymerase delta catalytic subunit Rattus norvegicus (Rat) PR
Q9LRE6 POLD1 DNA polymerase delta catalytic subunit Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MDCKRRQGPG PGVPPKRARG HLWDEDEPSP SQFEANLALL EEIEAENRLQ EAEEELQLPP
70 80 90 100 110 120
EGTVGGQFST ADIDPRWRRP TLRALDPSTE PLIFQQLEID HYVGSAPPLP EGPLPSRNSV
130 140 150 160 170 180
PILRAFGVTD EGFSVCCHIQ GFAPYFYTPA PPGFGAEHLS ELQQELNAAI SRDQRGGKEL
190 200 210 220 230 240
SGPAVLAIEL CSRESMFGYH GHGPSPFLRI TLALPRLMAP ARRLLEQGVR VPGLGTPSFA
250 260 270 280 290 300
PYEANVDFEI RFMVDADIVG CNWLELPAGK YVRRAEKKAT LCQLEVDVLW SDVISHPPEG
310 320 330 340 350 360
QWQRIAPLRV LSFDIECAGR KGIFPEPERD PVIQICSLGL RWGEPEPFLR LALTLRPCAP
370 380 390 400 410 420
ILGAKVQSYE REEDLLQAWA DFILAMDPDV ITGYNIQNFD LPYLISRAQA LKVDRFPFLG
430 440 450 460 470 480
RVTGLRSNIR DSSFQSRQVG RRDSKVISMV GRVQMDMLQV LLREHKLRSY TLNAVSFHFL
490 500 510 520 530 540
GEQKEDVQHS IITDLQNGNE QTRRRLAVYC LKDAFLPLRL LERLMVLVNN VEMARVTGVP
550 560 570 580 590 600
LGYLLTRGQQ VKVVSQLLRQ AMRQGLLMPV VKTEGSEDYT GATVIEPLKG YYDVPIATLD
610 620 630 640 650 660
FSSLYPSIMM AHNLCYTTLL RPGAAQKLGL KPDEFIKTPT GDEFVKSSVR KGLLPQILEN
670 680 690 700 710 720
LLSARKRAKA ELAQETDPLR RQVLDGRQLA LKVSANSVYG FTGAQVGKLP CLEISQSVTG
730 740 750 760 770 780
FGRQMIEKTK QLVESKYTVE NGYDANAKVV YGDTDSVMCR FGVSSVAEAM SLGREAANWV
790 800 810 820 830 840
SSHFPSPIRL EFEKVYFPYL LISKKRYAGL LFSSRSDAHD KMDCKGLEAV RRDNCPLVAN
850 860 870 880 890 900
LVTSSLRRIL VDRDPDGAVA HAKDVISDLL CNRIDISQLV ITKELTRAAA DYAGKQAHVE
910 920 930 940 950 960
LAERMRKRDP GSAPSLGDRV PYVIIGAAKG VAAYMKSEDP LFVLEHSLPI DTQYYLEQQL
970 980 990 1000 1010 1020
AKPLLRIFEP ILGEGRAESV LLRGDHTRCK TVLTSKVGGL LAFTKRRNCC IGCRSVIDHQ
1030 1040 1050 1060 1070 1080
GAVCKFCQPR ESELYQKEVS HLNALEERFS RLWTQCQRCQ GSLHEDVICT SRDCPIFYMR
1090 1100
KKVRKDLEDQ ERLLQRFGPP GPEAW