ID POLI_HUMAN Reviewed; 740 AA. AC Q9UNA4; Q8N590; Q9H0S1; Q9NYH6; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=DNA polymerase iota; DE EC=2.7.7.7 {ECO:0000269|PubMed:11013228, ECO:0000269|PubMed:11387224, ECO:0000269|PubMed:27555320}; DE AltName: Full=Eta2; DE AltName: Full=RAD30 homolog B; GN Name=POLI; Synonyms=RAD30B; 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 [GENOMIC DNA], AND VARIANTS GLY-96; MET-261; LYS-276; RP ARG-474; SER-532 AND ARG-560. RG NIEHS SNPs program; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-740, VARIANT THR-731, AND TISSUE RP SPECIFICITY. RC TISSUE=Umbilical vein endothelial cell; RX PubMed=10458907; DOI=10.1006/geno.1999.5906; RA McDonald J.P., Rapic-Otrin V., Epstein J.A., Broughton B.C., Wang X., RA Lehmann A.R., Wolgemuth D.J., Woodgate R.; RT "Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase RT eta."; RL Genomics 60:20-30(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-740, AND VARIANT SER-532. RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-740. RC TISSUE=Uterus; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-740, AND VARIANT THR-731. RA Poltoratsky V.P., Scharff M.D.; RT "Human eta2 gene homologous to bacterial UmuC and Rev1 genes."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11013228; DOI=10.1093/emboj/19.19.5259; RA Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R.; RT "Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase RT iota."; RL EMBO J. 19:5259-5266(2000). RN [8] RP FUNCTION, AND SCHIFF BASE FORMATION. RX PubMed=11251121; DOI=10.1126/science.1058386; RA Bebenek K., Tissier A., Frank E.G., McDonald J.P., Prasad R., Wilson S.H., RA Woodgate R., Kunkel T.A.; RT "5'-deoxyribose phosphate lyase activity of human DNA polymerase iota in RT vitro."; RL Science 291:2156-2159(2001). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=11387224; DOI=10.1093/emboj/20.11.2914; RA Frank E.G., Tissier A., McDonald J.P., Rapic-Otrin V., Zeng X., RA Gearhart P.J., Woodgate R.; RT "Altered nucleotide misinsertion fidelity associated with poliota-dependent RT replication at the end of a DNA template."; RL EMBO J. 20:2914-2922(2001). RN [10] RP FUNCTION. RX PubMed=12410315; DOI=10.1038/nature01117; RA Faili A., Aoufouchi S., Flatter E., Gueranger Q., Reynaud C.-A., RA Weill J.-C.; RT "Induction of somatic hypermutation in immunoglobulin genes is dependent on RT DNA polymerase iota."; RL Nature 419:944-947(2002). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH POLH. RX PubMed=12606586; RA Kannouche P.L., Fernandez de Henestrosa A.R., Coull B., Vidal A.E., RA Gray C., Zicha D., Woodgate R., Lehmann A.R.; RT "Localization of DNA polymerases eta and iota to the replication machinery RT is tightly co-ordinated in human cells."; RL EMBO J. 22:1223-1233(2003). RN [12] RP FUNCTION, AND SCHIFF BASE FORMATION. RX PubMed=14630940; DOI=10.1101/gad.1146103; RA Haracska L., Prakash L., Prakash S.; RT "A mechanism for the exclusion of low-fidelity human Y-family DNA RT polymerases from base excision repair."; RL Genes Dev. 17:2777-2785(2003). RN [13] RP FUNCTION. RX PubMed=15199127; DOI=10.1128/mcb.24.13.5687-5693.2004; RA Washington M.T., Minko I.G., Johnson R.E., Wolfle W.T., Harris T.M., RA Lloyd R.S., Prakash S., Prakash L.; RT "Efficient and error-free replication past a minor-groove DNA adduct by the RT sequential action of human DNA polymerases iota and kappa."; RL Mol. Cell. Biol. 24:5687-5693(2004). RN [14] {ECO:0007744|PDB:1T3N} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 52-439 IN COMPLEX WITH DNA; RP NUCLEOTIDE AND MAGNESIUM, FUNCTION, AND DOMAIN. RX PubMed=15254543; DOI=10.1038/nature02692; RA Nair D.T., Johnson R.E., Prakash S., Prakash L., Aggarwal A.K.; RT "Replication by human DNA polymerase-iota occurs by Hoogsteen base- RT pairing."; RL Nature 430:377-380(2004). RN [15] {ECO:0007744|PDB:5KT2, ECO:0007744|PDB:5KT3, ECO:0007744|PDB:5KT4, ECO:0007744|PDB:5KT5, ECO:0007744|PDB:5KT6, ECO:0007744|PDB:5KT7} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 26-445 IN COMPLEXES WITH DNA; RP MAGNESIUM AND MANGANESE, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS RP OF 1-MET--ALA-25, AND VARIANT GLY-96. RX PubMed=27555320; DOI=10.1074/jbc.m116.748285; RA Choi J.Y., Patra A., Yeom M., Lee Y.S., Zhang Q., Egli M., Guengerich F.P.; RT "Kinetic and Structural Impact of Metal Ions and Genetic Variations on RT Human DNA Polymerase iota."; RL J. Biol. Chem. 291:21063-21073(2016). CC -!- FUNCTION: Error-prone DNA polymerase specifically involved in DNA CC repair (PubMed:11013228, PubMed:11387224). Plays an important role in CC translesion synthesis, where the normal high-fidelity DNA polymerases CC cannot proceed and DNA synthesis stalls (PubMed:11013228, CC PubMed:11387224, PubMed:14630940, PubMed:15199127). Favors Hoogsteen CC base-pairing in the active site (PubMed:15254543). Inserts the correct CC base with high-fidelity opposite an adenosine template CC (PubMed:15254543). Exhibits low fidelity and efficiency opposite a CC thymidine template, where it will preferentially insert guanosine CC (PubMed:11013228). May play a role in hypermutation of immunoglobulin CC genes (PubMed:12410315). Forms a Schiff base with 5'-deoxyribose CC phosphate at abasic sites, but may not have lyase activity CC (PubMed:11251121, PubMed:14630940). {ECO:0000269|PubMed:11013228, CC ECO:0000269|PubMed:11251121, ECO:0000269|PubMed:11387224, CC ECO:0000269|PubMed:12410315, ECO:0000269|PubMed:14630940, CC ECO:0000269|PubMed:15199127, ECO:0000269|PubMed:15254543}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.7; CC Evidence={ECO:0000269|PubMed:11013228, ECO:0000269|PubMed:11387224, CC ECO:0000269|PubMed:27555320}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:27555320}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:27555320}; CC Note=Binds nucleotide much more tightly and catalyzes nucleotide CC insertion much more efficiently in the presence of Mg(2+) than in the CC presence of Mn(2+). {ECO:0000269|PubMed:27555320}; CC -!- SUBUNIT: Interacts with POLH (PubMed:12606586). Interacts with REV1 (By CC similarity). Interacts with ubiquitin (By similarity). CC {ECO:0000250|UniProtKB:Q6R3M4, ECO:0000269|PubMed:12606586}. CC -!- INTERACTION: CC Q9UNA4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-741774, EBI-724310; CC Q9UNA4; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-741774, EBI-748420; CC Q9UNA4; Q92993: KAT5; NbExp=3; IntAct=EBI-741774, EBI-399080; CC Q9UNA4; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-741774, EBI-11742507; CC Q9UNA4; Q15843: NEDD8; NbExp=2; IntAct=EBI-741774, EBI-716247; CC Q9UNA4; Q6FI35: PCNA; NbExp=2; IntAct=EBI-741774, EBI-8469539; CC Q9UNA4; P17252: PRKCA; NbExp=3; IntAct=EBI-741774, EBI-1383528; CC Q9UNA4; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-741774, EBI-9090795; CC Q9UNA4; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-741774, EBI-9675724; CC Q9UNA4; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-741774, EBI-359276; CC Q9UNA4; Q9HCM9: TRIM39; NbExp=4; IntAct=EBI-741774, EBI-739510; CC Q9UNA4; P0CG48: UBC; NbExp=4; IntAct=EBI-741774, EBI-3390054; CC Q9UNA4; P18887: XRCC1; NbExp=2; IntAct=EBI-741774, EBI-947466; CC Q9UNA4; P61981: YWHAG; NbExp=3; IntAct=EBI-741774, EBI-359832; CC Q9UNA4; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-741774, EBI-5658292; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12606586}. CC Note=Binding to ubiquitin mediates localization to replication forks CC after UV-induced DNA damage. {ECO:0000250|UniProtKB:Q6R3M4}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis. CC {ECO:0000269|PubMed:10458907, ECO:0000269|PubMed:11387224}. CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb CC subdomains, but the fingers and thumb subdomains are much smaller than CC in high-fidelity polymerases; residues from five sequence motifs of the CC Y-family cluster around an active site cleft that can accommodate DNA CC and nucleotide substrates with relaxed geometric constraints, with CC consequently higher rates of misincorporation and low processivity. CC {ECO:0000269|PubMed:15254543, ECO:0000269|PubMed:27555320}. CC -!- DOMAIN: Ubiquitin-binding motif 1 and ubiquitin-binding motif 2 CC regulate POLI protein monoubiquitination and localization to nuclear CC foci after UV-induced DNA damage. {ECO:0000250|UniProtKB:Q6R3M4}. CC -!- PTM: Monoubiquitinated. Protein monoubiquitination prevents POLI CC binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin- CC binding motif 2. {ECO:0000250|UniProtKB:Q6R3M4}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD50381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63383.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH32662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAM11872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB66605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/poli/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY094607; AAM11872.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC093462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF140501; AAD50381.1; ALT_INIT; mRNA. DR EMBL; AL136670; CAB66605.1; ALT_INIT; mRNA. DR EMBL; BC032662; AAH32662.1; ALT_INIT; mRNA. DR EMBL; AF245438; AAF63383.1; ALT_INIT; mRNA. DR CCDS; CCDS11954.2; -. DR RefSeq; NP_009126.2; NM_007195.2. DR PDB; 1T3N; X-ray; 2.30 A; A/B=52-439. DR PDB; 1ZET; X-ray; 2.30 A; A=52-439. DR PDB; 2ALZ; X-ray; 2.50 A; A=50-439. DR PDB; 2DPI; X-ray; 2.30 A; A=26-445. DR PDB; 2DPJ; X-ray; 2.30 A; A=26-445. DR PDB; 2FLL; X-ray; 2.60 A; A=26-445. DR PDB; 2FLN; X-ray; 2.50 A; A=26-445. DR PDB; 2FLP; X-ray; 2.40 A; A=26-445. DR PDB; 2KHU; NMR; -; A=697-740. DR PDB; 2KHW; NMR; -; A=697-740. DR PDB; 2KTF; NMR; -; B=704-730. DR PDB; 2L0F; NMR; -; B=699-740. DR PDB; 2L0G; NMR; -; A=704-730. DR PDB; 2MBB; NMR; -; A=516-555. DR PDB; 3EPG; X-ray; 2.50 A; A=26-445. DR PDB; 3EPI; X-ray; 2.90 A; A=26-445. DR PDB; 3G6V; X-ray; 2.20 A; A=26-445. DR PDB; 3G6X; X-ray; 2.08 A; A=26-445. DR PDB; 3G6Y; X-ray; 2.10 A; A=26-445. DR PDB; 3GV5; X-ray; 2.00 A; B/D=26-445. DR PDB; 3GV7; X-ray; 2.20 A; B=26-445. DR PDB; 3GV8; X-ray; 2.00 A; B=26-445. DR PDB; 3H40; X-ray; 2.30 A; A=51-439. DR PDB; 3H4B; X-ray; 2.85 A; A=50-439. DR PDB; 3H4D; X-ray; 2.20 A; A=50-439. DR PDB; 3NGD; X-ray; 2.80 A; A=26-445. DR PDB; 3OSN; X-ray; 1.90 A; A=26-445. DR PDB; 3Q8P; X-ray; 1.95 A; B=26-445. DR PDB; 3Q8Q; X-ray; 2.03 A; B=26-445. DR PDB; 3Q8R; X-ray; 2.45 A; B=26-445. DR PDB; 3Q8S; X-ray; 2.09 A; B=26-445. DR PDB; 4EBC; X-ray; 2.90 A; A=26-445. DR PDB; 4EBD; X-ray; 2.57 A; A=26-445. DR PDB; 4EBE; X-ray; 2.10 A; A=26-445. DR PDB; 4EYH; X-ray; 2.90 A; B=26-445. DR PDB; 4EYI; X-ray; 2.90 A; B=26-445. DR PDB; 4FS1; X-ray; 2.50 A; A=26-445. DR PDB; 4FS2; X-ray; 2.05 A; A=26-445. DR PDB; 5KT2; X-ray; 2.49 A; A=26-445. DR PDB; 5KT3; X-ray; 2.64 A; A=26-445. DR PDB; 5KT4; X-ray; 2.78 A; A=1-445. DR PDB; 5KT5; X-ray; 2.80 A; A=1-445. DR PDB; 5KT6; X-ray; 3.54 A; A=1-445. DR PDB; 5KT7; X-ray; 3.15 A; A=1-445. DR PDB; 5ULW; X-ray; 2.62 A; A=26-445. DR PDB; 5ULX; X-ray; 1.96 A; A=26-445. DR PDBsum; 1T3N; -. DR PDBsum; 1ZET; -. DR PDBsum; 2ALZ; -. DR PDBsum; 2DPI; -. DR PDBsum; 2DPJ; -. DR PDBsum; 2FLL; -. DR PDBsum; 2FLN; -. DR PDBsum; 2FLP; -. DR PDBsum; 2KHU; -. DR PDBsum; 2KHW; -. DR PDBsum; 2KTF; -. DR PDBsum; 2L0F; -. DR PDBsum; 2L0G; -. DR PDBsum; 2MBB; -. DR PDBsum; 3EPG; -. DR PDBsum; 3EPI; -. DR PDBsum; 3G6V; -. DR PDBsum; 3G6X; -. DR PDBsum; 3G6Y; -. DR PDBsum; 3GV5; -. DR PDBsum; 3GV7; -. DR PDBsum; 3GV8; -. DR PDBsum; 3H40; -. DR PDBsum; 3H4B; -. DR PDBsum; 3H4D; -. DR PDBsum; 3NGD; -. DR PDBsum; 3OSN; -. DR PDBsum; 3Q8P; -. DR PDBsum; 3Q8Q; -. DR PDBsum; 3Q8R; -. DR PDBsum; 3Q8S; -. DR PDBsum; 4EBC; -. DR PDBsum; 4EBD; -. DR PDBsum; 4EBE; -. DR PDBsum; 4EYH; -. DR PDBsum; 4EYI; -. DR PDBsum; 4FS1; -. DR PDBsum; 4FS2; -. DR PDBsum; 5KT2; -. DR PDBsum; 5KT3; -. DR PDBsum; 5KT4; -. DR PDBsum; 5KT5; -. DR PDBsum; 5KT6; -. DR PDBsum; 5KT7; -. DR PDBsum; 5ULW; -. DR PDBsum; 5ULX; -. DR AlphaFoldDB; Q9UNA4; -. DR SMR; Q9UNA4; -. DR BioGRID; 116370; 28. DR IntAct; Q9UNA4; 25. DR MINT; Q9UNA4; -. DR STRING; 9606.ENSP00000462664; -. DR BindingDB; Q9UNA4; -. DR ChEMBL; CHEMBL5391; -. DR GlyGen; Q9UNA4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UNA4; -. DR PhosphoSitePlus; Q9UNA4; -. DR BioMuta; POLI; -. DR DMDM; 327478565; -. DR EPD; Q9UNA4; -. DR jPOST; Q9UNA4; -. DR MassIVE; Q9UNA4; -. DR MaxQB; Q9UNA4; -. DR PaxDb; 9606-ENSP00000462664; -. DR PeptideAtlas; Q9UNA4; -. DR ProteomicsDB; 85277; -. DR Pumba; Q9UNA4; -. DR Antibodypedia; 1864; 543 antibodies from 31 providers. DR DNASU; 11201; -. DR Ensembl; ENST00000579534.6; ENSP00000462664.1; ENSG00000101751.11. DR GeneID; 11201; -. DR KEGG; hsa:11201; -. DR MANE-Select; ENST00000579534.6; ENSP00000462664.1; NM_007195.3; NP_009126.2. DR UCSC; uc002lfj.5; human. DR AGR; HGNC:9182; -. DR CTD; 11201; -. DR DisGeNET; 11201; -. DR GeneCards; POLI; -. DR HGNC; HGNC:9182; POLI. DR HPA; ENSG00000101751; Low tissue specificity. DR MIM; 605252; gene. DR neXtProt; NX_Q9UNA4; -. DR OpenTargets; ENSG00000101751; -. DR PharmGKB; PA33502; -. DR VEuPathDB; HostDB:ENSG00000101751; -. DR eggNOG; KOG2095; Eukaryota. DR GeneTree; ENSGT00940000159487; -. DR HOGENOM; CLU_012348_9_0_1; -. DR InParanoid; Q9UNA4; -. DR OMA; GNCDVMT; -. DR OrthoDB; 2918002at2759; -. DR PhylomeDB; Q9UNA4; -. DR TreeFam; TF324222; -. DR BRENDA; 2.7.7.7; 2681. DR PathwayCommons; Q9UNA4; -. DR Reactome; R-HSA-5656121; Translesion synthesis by POLI. DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis. DR SignaLink; Q9UNA4; -. DR BioGRID-ORCS; 11201; 16 hits in 1160 CRISPR screens. DR ChiTaRS; POLI; human. DR EvolutionaryTrace; Q9UNA4; -. DR GeneWiki; POLI; -. DR GenomeRNAi; 11201; -. DR Pharos; Q9UNA4; Tchem. DR PRO; PR:Q9UNA4; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q9UNA4; Protein. DR Bgee; ENSG00000101751; Expressed in calcaneal tendon and 191 other cell types or tissues. DR ExpressionAtlas; Q9UNA4; baseline and differential. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome. DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central. DR CDD; cd01703; PolY_Pol_iota; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.40.1170.60; -; 1. DR Gene3D; 6.10.250.1630; -; 2. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1. DR IDEAL; IID00106; -. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001126; UmuC. DR PANTHER; PTHR46404; DNA POLYMERASE IOTA; 1. DR PANTHER; PTHR46404:SF1; DNA POLYMERASE IOTA; 1. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR PIRSF; PIRSF036603; DPol_eta; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1. DR PROSITE; PS50173; UMUC; 1. DR Genevisible; Q9UNA4; HS. PE 1: Evidence at protein level; KW 3D-structure; DNA damage; DNA repair; DNA replication; DNA synthesis; KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Manganese; KW Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus; KW Reference proteome; Schiff base; Transferase; Ubl conjugation. FT CHAIN 1..740 FT /note="DNA polymerase iota" FT /id="PRO_0000173988" FT DOMAIN 55..268 FT /note="UmuC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..314 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0000269|PubMed:27555320, ECO:0007744|PDB:1T3N, FT ECO:0007744|PDB:5KT2, ECO:0007744|PDB:5KT4, FT ECO:0007744|PDB:5KT6" FT REGION 325..439 FT /note="DNA-binding" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0000269|PubMed:27555320, ECO:0007744|PDB:1T3N, FT ECO:0007744|PDB:5KT2, ECO:0007744|PDB:5KT4, FT ECO:0007744|PDB:5KT6" FT REGION 581..615 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 527..544 FT /note="Ubiquitin-binding 1 (UBM1)" FT /evidence="ECO:0000250|UniProtKB:Q6R3M4" FT MOTIF 708..725 FT /note="Ubiquitin-binding 2 (UBM2)" FT /evidence="ECO:0000250|UniProtKB:Q6R3M4" FT COMPBIAS 583..615 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 677..703 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 152 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216" FT BINDING 59 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0000269|PubMed:27555320, ECO:0007744|PDB:1T3N, FT ECO:0007744|PDB:5KT4" FT BINDING 59 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:27555320, FT ECO:0007744|PDB:5KT5" FT BINDING 60 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0000269|PubMed:27555320, ECO:0007744|PDB:1T3N, FT ECO:0007744|PDB:5KT4" FT BINDING 60 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:27555320, FT ECO:0007744|PDB:5KT5" FT BINDING 64 FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61560" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0007744|PDB:1T3N" FT BINDING 96 FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61560" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0007744|PDB:1T3N" FT BINDING 151 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:15254543, FT ECO:0000269|PubMed:27555320, ECO:0007744|PDB:1T3N, FT ECO:0007744|PDB:5KT4" FT BINDING 151 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:27555320, FT ECO:0007744|PDB:5KT5" FT VARIANT 96 FT /note="R -> G (large decrease in catalytic activity FT efficiency which is partially rescued by the presence of FT Mn(2+) instead Mg(2+); dbSNP:rs3218778)" FT /evidence="ECO:0000269|PubMed:27555320, ECO:0000269|Ref.1" FT /id="VAR_021239" FT VARIANT 261 FT /note="I -> M (in dbSNP:rs3218784)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_021240" FT VARIANT 276 FT /note="E -> K (in dbSNP:rs3218783)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_021241" FT VARIANT 474 FT /note="H -> R (in dbSNP:rs3730823)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_021242" FT VARIANT 532 FT /note="F -> S (in dbSNP:rs3218786)" FT /evidence="ECO:0000269|PubMed:11230166, ECO:0000269|Ref.1" FT /id="VAR_021243" FT VARIANT 560 FT /note="C -> R (in dbSNP:rs3218787)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_021244" FT VARIANT 731 FT /note="A -> T (in dbSNP:rs8305)" FT /evidence="ECO:0000269|PubMed:10458907, ECO:0000269|Ref.6" FT /id="VAR_021245" FT MUTAGEN 1..25 FT /note="Missing: Small decrease in catalytic activity FT efficiency which is partially rescued by the presence of FT Mn(2+) instead Mg(2+)." FT /evidence="ECO:0000269|PubMed:27555320" FT CONFLICT 15 FT /note="Missing (in Ref. 3; AAD50381, 4; CAB66605 and 6; FT AAF63383)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="S -> T (in Ref. 4; CAB66605)" FT /evidence="ECO:0000305" FT CONFLICT 433 FT /note="V -> A (in Ref. 6; AAF63383)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="D -> G (in Ref. 6; AAF63383)" FT /evidence="ECO:0000305" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:3H40" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:3OSN" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:3H4D" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:2FLN" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 125..141 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:3OSN" FT TURN 149..151 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 158..167 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 193..216 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 228..235 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:3EPG" FT TURN 239..241 FT /evidence="ECO:0007829|PDB:3EPG" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 251..257 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 269..277 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 283..288 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 291..310 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 325..332 FT /evidence="ECO:0007829|PDB:3OSN" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:2ALZ" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 342..360 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 362..374 FT /evidence="ECO:0007829|PDB:3OSN" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:1ZET" FT STRAND 383..388 FT /evidence="ECO:0007829|PDB:3OSN" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:1ZET" FT HELIX 401..404 FT /evidence="ECO:0007829|PDB:1T3N" FT HELIX 405..419 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:3OSN" FT STRAND 427..439 FT /evidence="ECO:0007829|PDB:3OSN" FT HELIX 529..534 FT /evidence="ECO:0007829|PDB:2MBB" FT HELIX 537..544 FT /evidence="ECO:0007829|PDB:2MBB" FT STRAND 704..707 FT /evidence="ECO:0007829|PDB:2L0G" FT HELIX 710..713 FT /evidence="ECO:0007829|PDB:2KHU" FT HELIX 718..731 FT /evidence="ECO:0007829|PDB:2KHU" SQ SEQUENCE 740 AA; 83006 MW; C1A5BF0894E91FDF CRC64; MEKLGVEPEE EGGGDDDEED AEAWAMELAD VGAAASSQGV HDQVLPTPNA SSRVIVHVDL DCFYAQVEMI SNPELKDKPL GVQQKYLVVT CNYEARKLGV KKLMNVRDAK EKCPQLVLVN GEDLTRYREM SYKVTELLEE FSPVVERLGF DENFVDLTEM VEKRLQQLQS DELSAVTVSG HVYNNQSINL LDVLHIRLLV GSQIAAEMRE AMYNQLGLTG CAGVASNKLL AKLVSGVFKP NQQTVLLPES CQHLIHSLNH IKEIPGIGYK TAKCLEALGI NSVRDLQTFS PKILEKELGI SVAQRIQKLS FGEDNSPVIL SGPPQSFSEE DSFKKCSSEV EAKNKIEELL ASLLNRVCQD GRKPHTVRLI IRRYSSEKHY GRESRQCPIP SHVIQKLGTG NYDVMTPMVD ILMKLFRNMV NVKMPFHLTL LSVCFCNLKA LNTAKKGLID YYLMPSLSTT SRSGKHSFKM KDTHMEDFPK DKETNRDFLP SGRIESTRTR ESPLDTTNFS KEKDINEFPL CSLPEGVDQE VFKQLPVDIQ EEILSGKSRE KFQGKGSVSC PLHASRGVLS FFSKKQMQDI PINPRDHLSS SKQVSSVSPC EPGTSGFNSS SSSYMSSQKD YSYYLDNRLK DERISQGPKE PQGFHFTNSN PAVSAFHSFP NLQSEQLFSR NHTTDSHKQT VATDSHEGLT ENREPDSVDE KITFPSDIDP QVFYELPEAV QKELLAEWKR AGSDFHIGHK //