DPOD4_HUMAN
ID DPOD4_HUMAN Reviewed; 107 AA.
AC Q9HCU8; F5H506;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA polymerase delta subunit 4;
DE AltName: Full=DNA polymerase delta subunit p12;
GN Name=POLD4; Synonyms=POLDS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ovarian carcinoma;
RX PubMed=10751307; DOI=10.1074/jbc.m001217200;
RA Liu L., Mo J.-Y., Rodriguez-Belmonte E.M., Lee M.Y.W.T.;
RT "Identification of a fourth subunit of mammalian DNA polymerase delta.";
RL J. Biol. Chem. 275:18739-18744(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-39.
RG NIEHS SNPs program;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN POL-DELTA COMPLEX, INTERACTION WITH POLD1, AND
RP CHARACTERIZATION OF POL-DELTA2 AND POL-DELTA4 COMPLEXES.
RX PubMed=12403614; DOI=10.1021/bi0262707;
RA Xie B., Mazloum N., Liu L., Rahmeh A., Li H., Lee M.Y.;
RT "Reconstitution and characterization of the human DNA polymerase delta
RT four-subunit holoenzyme.";
RL Biochemistry 41:13133-13142(2002).
RN [6]
RP INTERACTION WITH POLDIP2.
RX PubMed=12522211; DOI=10.1074/jbc.m208694200;
RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.;
RT "Identification of a novel protein, PDIP38, that interacts with the p50
RT subunit of DNA polymerase delta and proliferating cell nuclear antigen.";
RL J. Biol. Chem. 278:10041-10047(2003).
RN [7]
RP INTERACTION WITH WRNIP1.
RX PubMed=15670210; DOI=10.1111/j.1365-2443.2004.00812.x;
RA Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.;
RT "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel
RT modulator for DNA polymerase delta.";
RL Genes Cells 10:13-22(2005).
RN [8]
RP UBIQUITINATION, AND MUTAGENESIS OF LYS-4; LYS-15; LYS-25; LYS-74 AND
RP LYS-89.
RX PubMed=16934752; DOI=10.1016/j.bbrc.2006.08.049;
RA Liu G., Warbrick E.;
RT "The p66 and p12 subunits of DNA polymerase delta are modified by ubiquitin
RT and ubiquitin-like proteins.";
RL Biochem. Biophys. Res. Commun. 349:360-366(2006).
RN [9]
RP FUNCTION, INTERACTION WITH POLD1; POLD2 AND PCNA, AND MUTAGENESIS OF ILE-7
RP AND 10-SER-TYR-11.
RX PubMed=16510448; DOI=10.1074/jbc.m600322200;
RA Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y.,
RA Lee M.Y.;
RT "Functional roles of p12, the fourth subunit of human DNA polymerase
RT delta.";
RL J. Biol. Chem. 281:14748-14755(2006).
RN [10]
RP UBIQUITINATION, DEGRADATION IN RESPONSE TO DNA DAMAGE, AND IDENTIFICATION
RP IN POL-DELTA COMPLEX.
RX PubMed=17317665; DOI=10.1074/jbc.m610356200;
RA Zhang S., Zhou Y., Trusa S., Meng X., Lee E.Y., Lee M.Y.;
RT "A novel DNA damage response: rapid degradation of the p12 subunit of dna
RT polymerase delta.";
RL J. Biol. Chem. 282:15330-15340(2007).
RN [11]
RP FUNCTION.
RX PubMed=19074196; DOI=10.1093/nar/gkn1000;
RA Meng X., Zhou Y., Zhang S., Lee E.Y., Frick D.N., Lee M.Y.;
RT "DNA damage alters DNA polymerase delta to a form that exhibits increased
RT discrimination against modified template bases and mismatched primers.";
RL Nucleic Acids Res. 37:647-657(2009).
RN [12]
RP FUNCTION.
RX PubMed=20334433; DOI=10.1021/bi100042b;
RA Meng X., Zhou Y., Lee E.Y., Lee M.Y., Frick D.N.;
RT "The p12 subunit of human polymerase delta modulates the rate and fidelity
RT of DNA synthesis.";
RL Biochemistry 49:3545-3554(2010).
RN [13]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN POL-DELTA COMPLEX, INDUCTION BY UV,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=22801543; DOI=10.4161/cc.21280;
RA Chea J., Zhang S., Zhao H., Zhang Z., Lee E.Y., Darzynkiewicz Z., Lee M.Y.;
RT "Spatiotemporal recruitment of human DNA polymerase delta to sites of UV
RT damage.";
RL Cell Cycle 11:2885-2895(2012).
RN [14]
RP FUNCTION IN OKAZAKI FRAGMENT PROCESSING.
RX PubMed=24035200; DOI=10.1016/j.dnarep.2013.08.008;
RA Lin S.H., Wang X., Zhang S., Zhang Z., Lee E.Y., Lee M.Y.;
RT "Dynamics of enzymatic interactions during short flap human Okazaki
RT fragment processing by two forms of human DNA polymerase delta.";
RL DNA Repair 12:922-935(2013).
RN [15]
RP UBIQUITINATION BY RNF8, AND INDUCTION BY UV.
RX PubMed=23233665; DOI=10.1074/jbc.m112.423392;
RA Zhang S., Zhou Y., Sarkeshik A., Yates J.R. III, Thomson T.M., Zhang Z.,
RA Lee E.Y., Lee M.Y.;
RT "Identification of RNF8 as a ubiquitin ligase involved in targeting the p12
RT subunit of DNA polymerase delta for degradation in response to DNA
RT damage.";
RL J. Biol. Chem. 288:2941-2950(2013).
RN [16]
RP UBIQUITINATION BY DTL, DEVELOPMENTAL STAGE, DEGRADATION IN RESPONSE TO DNA
RP DAMAGE, AND MUTAGENESIS OF THR-8; ASP-9; LYS-15; ARG-16 AND ARG-17.
RX PubMed=23913683; DOI=10.1074/jbc.m113.490466;
RA Zhang S., Zhao H., Darzynkiewicz Z., Zhou P., Zhang Z., Lee E.Y., Lee M.Y.;
RT "A novel function of CRL4(Cdt2): regulation of the subunit structure of DNA
RT polymerase delta in response to DNA damage and during the S phase.";
RL J. Biol. Chem. 288:29550-29561(2013).
RN [17]
RP FUNCTION, INTERACTION WITH PCNA, INDUCTION BY UV, UBIQUITINATION BY DTL,
RP AND MUTAGENESIS OF 1-MET--ARG-16; LYS-4; SER-10 AND LYS-15.
RX PubMed=24022480; DOI=10.1074/jbc.c113.505586;
RA Terai K., Shibata E., Abbas T., Dutta A.;
RT "Degradation of p12 subunit by CRL4Cdt2 E3 ligase inhibits fork progression
RT after DNA damage.";
RL J. Biol. Chem. 288:30509-30514(2013).
RN [18]
RP INDUCTION BY IR AND UV, AND REVIEW.
RX PubMed=24300032; DOI=10.4161/cc.27407;
RA Lee M.Y., Zhang S., Lin S.H., Wang X., Darzynkiewicz Z., Zhang Z.,
RA Lee E.Y.;
RT "The tail that wags the dog: p12, the smallest subunit of DNA polymerase
RT delta, is degraded by ubiquitin ligases in response to DNA damage and
RT during cell cycle progression.";
RL Cell Cycle 13:23-31(2014).
RN [19]
RP FUNCTION.
RX PubMed=24310611; DOI=10.1126/science.1243211;
RA Costantino L., Sotiriou S.K., Rantala J.K., Magin S., Mladenov E.,
RA Helleday T., Haber J.E., Iliakis G., Kallioniemi O.P., Halazonetis T.D.;
RT "Break-induced replication repair of damaged forks induces genomic
RT duplications in human cells.";
RL Science 343:88-91(2014).
CC -!- FUNCTION: As a component of the tetrameric DNA polymerase delta complex
CC (Pol-delta4), plays a role in high fidelity genome replication and
CC repair. Within this complex, increases the rate of DNA synthesis and
CC decreases fidelity by regulating POLD1 polymerase and proofreading 3'
CC to 5' exonuclease activity (PubMed:16510448, PubMed:19074196,
CC PubMed:20334433). Pol-delta4 participates in Okazaki fragment
CC processing, through both the short flap pathway, as well as a nick
CC translation system (PubMed:24035200). Under conditions of DNA
CC replication stress, required for the repair of broken replication forks
CC through break-induced replication (BIR), a mechanism that may induce
CC segmental genomic duplications of up to 200 kb (PubMed:24310611).
CC Involved in Pol-delta4 translesion synthesis (TLS) of templates
CC carrying O6-methylguanine or abasic sites (PubMed:19074196). Its
CC degradation in response to DNA damage is required for the inhibition of
CC fork progression and cell survival (PubMed:24022480).
CC {ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:19074196,
CC ECO:0000269|PubMed:20334433, ECO:0000269|PubMed:24022480,
CC ECO:0000269|PubMed:24035200, ECO:0000269|PubMed:24310611}.
CC -!- SUBUNIT: Component of the tetrameric DNA polymerase delta complex (Pol-
CC delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and
CC POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading
CC exonuclease activities (PubMed:16510448, PubMed:17317665,
CC PubMed:22801543). Within this complex, directly interacts with POLD1
CC and POLD2 (PubMed:12403614, PubMed:16510448). Directly interacts with
CC PCNA, as do POLD1 and POLD3; this interaction stimulates Pol-delta4
CC polymerase activity (PubMed:24022480). As POLD1 and POLD2, directly
CC interacts with WRNIP1; this interaction stimulates DNA polymerase
CC delta-mediated DNA synthesis, independently of the presence of PCNA.
CC This stimulation may be due predominantly to an increase of initiation
CC frequency and also to increased processivity (PubMed:15670210). Upon
CC genotoxic stress induced by DNA damaging agents or by replication
CC stress, POLD4 is proteolytically degraded and Pol-delta4 is converted
CC into a trimeric form of the complex (Pol-delta3) which has an increased
CC proofreading activity (PubMed:22801543, PubMed:17317665). The DNA
CC polymerase delta complex interacts with POLDIP2; this interaction is
CC probably mediated through direct binding to POLD2 (PubMed:12522211).
CC {ECO:0000269|PubMed:12403614, ECO:0000269|PubMed:12522211,
CC ECO:0000269|PubMed:15670210, ECO:0000269|PubMed:16510448,
CC ECO:0000269|PubMed:17317665, ECO:0000269|PubMed:22801543,
CC ECO:0000269|PubMed:24022480}.
CC -!- INTERACTION:
CC Q9HCU8; P12004: PCNA; NbExp=4; IntAct=EBI-864968, EBI-358311;
CC Q9HCU8; P28340: POLD1; NbExp=12; IntAct=EBI-864968, EBI-716569;
CC Q9HCU8; P49005: POLD2; NbExp=5; IntAct=EBI-864968, EBI-372354;
CC Q9HCU8; Q96S55: WRNIP1; NbExp=2; IntAct=EBI-864968, EBI-2513471;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22801543}.
CC Note=Partially recruited to DNA damage sites within 2 hours following
CC UV irradiation, before degradation. {ECO:0000269|PubMed:22801543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCU8-2; Sequence=VSP_046864;
CC -!- DEVELOPMENTAL STAGE: Expression is cell cycle-dependent, with highest
CC levels in G2/M phase and a drastic drop in S phase (PubMed:22801543,
CC PubMed:23913683). This trough may be mediated by DCX(DTL) E3 ubiquitin
CC ligase complex (also called CRL4(CDT2))-mediated proteasomal
CC degradation (PubMed:23913683). {ECO:0000269|PubMed:22801543,
CC ECO:0000269|PubMed:23913683}.
CC -!- INDUCTION: In response to DNA damage, genotoxic stress and replication
CC stress, following UV irradiation, ionizing radiation, treatment with
CC methyl methanesulfonate, hydroxyurea, or with aphidicolin, protein
CC expression drops to undetectable levels, due to proteasomal degradation
CC (PubMed:17317665, PubMed:22801543, PubMed:23233665, PubMed:23913683,
CC PubMed:24300032). This down-regulation is ATR-dependent
CC (PubMed:17317665). {ECO:0000269|PubMed:17317665,
CC ECO:0000269|PubMed:22801543, ECO:0000269|PubMed:23233665,
CC ECO:0000269|PubMed:23913683, ECO:0000269|PubMed:24300032}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked ubiquitination in
CC response to UV irradiation, leading to proteasomal degradation
CC (PubMed:17317665, PubMed:16934752, PubMed:23233665, PubMed:23913683).
CC This modification is partly mediated by RNF8 and by the DCX(DTL) E3
CC ubiquitin ligase complex (also called CRL4(CDT2)) (PubMed:23233665,
CC PubMed:24022480). Efficient degradation requires the presence of PCNA
CC and is required for the inhibition of fork progression after DNA damage
CC (PubMed:24022480). {ECO:0000269|PubMed:16934752,
CC ECO:0000269|PubMed:17317665, ECO:0000269|PubMed:23233665,
CC ECO:0000269|PubMed:23913683, ECO:0000269|PubMed:24022480}.
CC -!- SIMILARITY: Belongs to the DNA polymerase delta subunit 4 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pold4/";
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DR EMBL; AF179890; AAG08966.1; -; mRNA.
DR EMBL; AY928482; AAX09676.1; -; Genomic_DNA.
DR EMBL; AP003419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BG403692; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58149.1; -. [Q9HCU8-2]
DR CCDS; CCDS8158.1; -. [Q9HCU8-1]
DR RefSeq; NP_001243799.1; NM_001256870.1. [Q9HCU8-2]
DR RefSeq; NP_066996.3; NM_021173.4. [Q9HCU8-1]
DR PDB; 6HVO; X-ray; 2.10 A; D/E/F=1-19.
DR PDB; 6S1M; EM; 4.27 A; D=2-107.
DR PDB; 6S1N; EM; 4.86 A; D=2-107.
DR PDB; 6S1O; EM; 8.10 A; D=2-107.
DR PDB; 6TNY; EM; 3.08 A; D=2-107.
DR PDB; 6TNZ; EM; 4.05 A; D=2-107.
DR PDBsum; 6HVO; -.
DR PDBsum; 6S1M; -.
DR PDBsum; 6S1N; -.
DR PDBsum; 6S1O; -.
DR PDBsum; 6TNY; -.
DR PDBsum; 6TNZ; -.
DR AlphaFoldDB; Q9HCU8; -.
DR SMR; Q9HCU8; -.
DR BioGRID; 121774; 10.
DR ComplexPortal; CPX-2097; DNA polymerase delta complex.
DR CORUM; Q9HCU8; -.
DR IntAct; Q9HCU8; 8.
DR MINT; Q9HCU8; -.
DR STRING; 9606.ENSP00000311368; -.
DR ChEMBL; CHEMBL2363042; -.
DR iPTMnet; Q9HCU8; -.
DR PhosphoSitePlus; Q9HCU8; -.
DR BioMuta; POLD4; -.
DR EPD; Q9HCU8; -.
DR jPOST; Q9HCU8; -.
DR MassIVE; Q9HCU8; -.
DR MaxQB; Q9HCU8; -.
DR PaxDb; Q9HCU8; -.
DR PeptideAtlas; Q9HCU8; -.
DR PRIDE; Q9HCU8; -.
DR ProteomicsDB; 26732; -.
DR ProteomicsDB; 81802; -. [Q9HCU8-1]
DR Antibodypedia; 30343; 57 antibodies from 19 providers.
DR DNASU; 57804; -.
DR Ensembl; ENST00000312419.8; ENSP00000311368.3; ENSG00000175482.9. [Q9HCU8-1]
DR Ensembl; ENST00000539074.1; ENSP00000444780.1; ENSG00000175482.9. [Q9HCU8-2]
DR GeneID; 57804; -.
DR KEGG; hsa:57804; -.
DR MANE-Select; ENST00000312419.8; ENSP00000311368.3; NM_021173.5; NP_066996.3.
DR UCSC; uc001okm.5; human. [Q9HCU8-1]
DR CTD; 57804; -.
DR DisGeNET; 57804; -.
DR GeneCards; POLD4; -.
DR HGNC; HGNC:14106; POLD4.
DR HPA; ENSG00000175482; Tissue enhanced (liver).
DR MIM; 611525; gene.
DR neXtProt; NX_Q9HCU8; -.
DR OpenTargets; ENSG00000175482; -.
DR PharmGKB; PA33498; -.
DR VEuPathDB; HostDB:ENSG00000175482; -.
DR eggNOG; ENOG502SC9I; Eukaryota.
DR GeneTree; ENSGT00390000005096; -.
DR HOGENOM; CLU_132157_0_0_1; -.
DR InParanoid; Q9HCU8; -.
DR OMA; DPRFQYS; -.
DR PhylomeDB; Q9HCU8; -.
DR TreeFam; TF103004; -.
DR PathwayCommons; Q9HCU8; -.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-69091; Polymerase switching.
DR Reactome; R-HSA-69166; Removal of the Flap Intermediate.
DR Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR SignaLink; Q9HCU8; -.
DR SIGNOR; Q9HCU8; -.
DR BioGRID-ORCS; 57804; 19 hits in 1077 CRISPR screens.
DR ChiTaRS; POLD4; human.
DR GeneWiki; POLD4; -.
DR GenomeRNAi; 57804; -.
DR Pharos; Q9HCU8; Tdark.
DR PRO; PR:Q9HCU8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HCU8; protein.
DR Bgee; ENSG00000175482; Expressed in mucosa of transverse colon and 95 other tissues.
DR ExpressionAtlas; Q9HCU8; baseline and differential.
DR Genevisible; Q9HCU8; HS.
DR GO; GO:0043625; C:delta DNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR InterPro; IPR007218; DNA_pol_delta_4.
DR PANTHER; PTHR14303; PTHR14303; 1.
DR Pfam; PF04081; DNA_pol_delta_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA excision; DNA repair;
KW DNA replication; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..107
FT /note="DNA polymerase delta subunit 4"
FT /id="PRO_0000186051"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..16
FT /note="PCNA-interaction protein motif (PIP box)"
FT /evidence="ECO:0000269|PubMed:16510448,
FT ECO:0000269|PubMed:24022480"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 63..107
FT /note="GITRLQRWCRAKQMGLEPPPEVWQVLKTHPGDPRFQCSLWHLYPL -> VSG
FT ISIPYEAPRKTSCP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046864"
FT VARIANT 39
FT /note="R -> P (in dbSNP:rs28364240)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_022269"
FT VARIANT 59
FT /note="G -> R (in dbSNP:rs34136263)"
FT /id="VAR_057526"
FT MUTAGEN 1..16
FT /note="Missing: Complete loss of PCNA binding and of
FT degradation after UV irradiation."
FT /evidence="ECO:0000269|PubMed:24022480"
FT MUTAGEN 4
FT /note="K->A: No effect on PCNA binding."
FT /evidence="ECO:0000269|PubMed:24022480"
FT MUTAGEN 4
FT /note="K->Q: No effect on PCNA binding, nor on degradation
FT after UV irradiation; when associated with Y-10. No effect
FT on PCNA binding, but normal degradation after UV
FT irradiation; when associated with Y-10 and A-15."
FT /evidence="ECO:0000269|PubMed:24022480"
FT MUTAGEN 4
FT /note="K->R: No effect on ubiquitination. Loss of
FT ubiquitination, when associated with R-15, R-25, R-74 and
FT R-89."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 7
FT /note="I->A: Complete loss of PCNA binding; when associated
FT with 10-AA-11."
FT /evidence="ECO:0000269|PubMed:16510448"
FT MUTAGEN 8
FT /note="T->A: Strongly increased stability following UV
FT irradiation; when associated with A-9."
FT /evidence="ECO:0000269|PubMed:23913683"
FT MUTAGEN 8
FT /note="T->D: Complete loss of PCNA binding."
FT /evidence="ECO:0000269|PubMed:24022480"
FT MUTAGEN 9
FT /note="D->A: Strongly increased stability following UV
FT irradiation; when associated with A-8."
FT /evidence="ECO:0000269|PubMed:23913683"
FT MUTAGEN 10..11
FT /note="SY->AA: Complete loss of PCNA binding; when
FT associated with A-7."
FT /evidence="ECO:0000269|PubMed:16510448"
FT MUTAGEN 10
FT /note="S->Y: No effect on PCNA binding, nor on degradation
FT after UV irradiation; when associated with Q-4. No effect
FT on PCNA binding, but normal degradation after UV
FT irradiation with Q-4 and A-15."
FT /evidence="ECO:0000269|PubMed:24022480"
FT MUTAGEN 15
FT /note="K->A: Decreased PCNA binding. No effect on PCNA
FT binding, but normal degradation after UV irradiation; when
FT associated with Q-4 and Y-10. Increased stability following
FT UV irradiation and no trough during S phase; when
FT associated with A-16 and A-17."
FT /evidence="ECO:0000269|PubMed:23913683,
FT ECO:0000269|PubMed:24022480"
FT MUTAGEN 15
FT /note="K->R: No effect on ubiquitination. Loss of
FT ubiquitination; when associated with R-4, R-25, R-74 and R-
FT 89."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 16
FT /note="R->A: Increased stability following UV irradiation
FT and no trough during S phase; when associated with A-15 and
FT A-17."
FT /evidence="ECO:0000269|PubMed:23913683"
FT MUTAGEN 17
FT /note="R->A: Increased stability following UV irradiation
FT and no trough during S phase; when associated with A-15 and
FT A-16."
FT /evidence="ECO:0000269|PubMed:23913683"
FT MUTAGEN 25
FT /note="K->R: No effect on ubiquitination. Loss of
FT ubiquitination; when associated with R-4, R-15, R-74 and R-
FT 89."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 74
FT /note="K->R: No effect on ubiquitination. Loss of
FT ubiquitination; when associated with R-4, R-15, R-25 and R-
FT 89."
FT /evidence="ECO:0000269|PubMed:16934752"
FT MUTAGEN 89
FT /note="K->R: No effect on ubiquitination. Loss of
FT ubiquitination; when associated with R-4, R-15, R-25 and R-
FT 74."
FT /evidence="ECO:0000269|PubMed:16934752"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6HVO"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6HVO"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:6TNY"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6TNY"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6TNY"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6TNY"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6TNY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6TNY"
SQ SEQUENCE 107 AA; 12433 MW; 6F412738E4D9A19C CRC64;
MGRKRLITDS YPVVKRREGP AGHSKGELAP ELGEEPQPRD EEEAELELLR QFDLAWQYGP
CTGITRLQRW CRAKQMGLEP PPEVWQVLKT HPGDPRFQCS LWHLYPL
