POLK_HUMAN
ID POLK_HUMAN Reviewed; 870 AA.
AC Q9UBT6; B2RBD2; Q5Q9G5; Q5Q9G6; Q5Q9G7; Q5Q9G8; Q86VJ8; Q8IZY0; Q8IZY1;
AC Q8NB30; Q96L01; Q96Q86; Q96Q87; Q9UHC5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DNA polymerase kappa;
DE EC=2.7.7.7 {ECO:0000269|PubMed:11024016};
DE AltName: Full=DINB protein;
DE Short=DINP;
GN Name=POLK; Synonyms=DINB1;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10620008; DOI=10.1046/j.1365-2443.1999.00289.x;
RA Ogi T., Kato T. Jr., Kato R., Ohmori H.;
RT "Mutation enhancement by DINB1, a mammalian homologue of the Escherichia
RT coli mutagenesis protein dinB.";
RL Genes Cells 4:607-618(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=10518552; DOI=10.1073/pnas.96.21.11922;
RA Gerlach V.L., Aravind L., Gotway G., Schultz R.A., Koonin E.V.,
RA Friedberg E.C.;
RT "Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV),
RT members of the UmuC/DinB superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11922-11927(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Testis;
RX PubMed=15661663; DOI=10.1016/j.dnarep.2004.10.006;
RA Guo C., Gao T., Confer N., Velasco-Miguel S., Friedberg E.C.;
RT "Multiple PolK (POLK) transcripts in mammalian testis.";
RL DNA Repair 4:397-402(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Poltoratsky V.P., Scharff M.D.;
RT "Homo sapiens DINP protein mRNA, complete cds.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Revert-Ros F., Saus J.;
RT "A bidirectional promoter for the genes encoding DNA polymerase kappa and
RT Goodpasture autoantigen binding protein: identification of a novel pol
RT kappa alternative spliced variant.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-595 AND ASN-832.
RG NIEHS SNPs program;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-313 (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Spleen;
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231.
RA Ogi T., Yamamoto Y., Ohmori H.;
RT "Homo sapiens genomic sequence, containing DINB1 gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP MUTAGENESIS OF ASP-198 AND GLU-199.
RX PubMed=11024016; DOI=10.1074/jbc.m004413200;
RA Gerlach V.L., Feaver W.J., Fischhaber P.L., Friedberg E.C.;
RT "Purification and characterization of pol kappa, a DNA polymerase encoded
RT by the human DINB1 gene.";
RL J. Biol. Chem. 276:92-98(2001).
RN [13]
RP FUNCTION.
RX PubMed=12145297; DOI=10.1074/jbc.m206027200;
RA Fischhaber P.L., Gerlach V.L., Feaver W.J., Hatahet Z., Wallace S.S.,
RA Friedberg E.C.;
RT "Human DNA polymerase kappa bypasses and extends beyond thymine glycols
RT during translesion synthesis in vitro, preferentially incorporating correct
RT nucleotides.";
RL J. Biol. Chem. 277:37604-37611(2002).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=12414988; DOI=10.1242/jcs.00162;
RA Bergoglio V., Bavoux C., Verbiest V., Hoffmann J.-S., Cazaux C.;
RT "Localisation of human DNA polymerase kappa to replication foci.";
RL J. Cell Sci. 115:4413-4418(2002).
RN [15]
RP INTERACTION WITH PCNA.
RX PubMed=11784855; DOI=10.1128/mcb.22.3.784-791.2002;
RA Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L.,
RA Prakash S.;
RT "Stimulation of DNA synthesis activity of human DNA polymerase kappa by
RT PCNA.";
RL Mol. Cell. Biol. 22:784-791(2002).
RN [16]
RP FUNCTION.
RX PubMed=12444249; DOI=10.1073/pnas.252524999;
RA Haracska L., Prakash L., Prakash S.;
RT "Role of human DNA polymerase kappa as an extender in translesion
RT synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16000-16005(2002).
RN [17]
RP FUNCTION.
RX PubMed=12952891; DOI=10.1101/gad.1108603;
RA Wolfle W.T., Washington M.T., Prakash L., Prakash S.;
RT "Human DNA polymerase kappa uses template-primer misalignment as a novel
RT means for extending mispaired termini and for generating single-base
RT deletions.";
RL Genes Dev. 17:2191-2199(2003).
RN [18]
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 [19]
RP FUNCTION.
RX PubMed=15533436; DOI=10.1016/j.jmb.2004.09.064;
RA Yasui M., Suzuki N., Miller H., Matsuda T., Matsui S., Shibutani S.;
RT "Translesion synthesis past 2'-deoxyxanthosine, a nitric oxide-derived DNA
RT adduct, by mammalian DNA polymerases.";
RL J. Mol. Biol. 344:665-674(2004).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28297716; DOI=10.1038/nature21671;
RA Xiang Y., Laurent B., Hsu C.H., Nachtergaele S., Lu Z., Sheng W., Xu C.,
RA Chen H., Ouyang J., Wang S., Ling D., Hsu P.H., Zou L., Jambhekar A.,
RA He C., Shi Y.;
RT "RNA m(6)A methylation regulates the ultraviolet-induced DNA damage
RT response.";
RL Nature 543:573-576(2017).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 68-526.
RX PubMed=15296733; DOI=10.1016/j.str.2004.05.011;
RA Uljon S.N., Johnson R.E., Edwards T.A., Prakash S., Prakash L.,
RA Aggarwal A.K.;
RT "Crystal structure of the catalytic core of human DNA polymerase kappa.";
RL Structure 12:1395-1404(2004).
CC -!- FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an
CC important role in translesion synthesis, where the normal high-fidelity
CC DNA polymerases cannot proceed and DNA synthesis stalls. Depending on
CC the context, it inserts the correct base, but causes frequent base
CC transitions, transversions and frameshifts. Lacks 3'-5' proofreading
CC exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate
CC at abasic sites, but does not have lyase activity.
CC {ECO:0000269|PubMed:10620008, ECO:0000269|PubMed:11024016,
CC ECO:0000269|PubMed:12145297, ECO:0000269|PubMed:12444249,
CC ECO:0000269|PubMed:12952891, ECO:0000269|PubMed:14630940,
CC ECO:0000269|PubMed:15533436, ECO:0000269|PubMed:28297716}.
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:11024016};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11024016};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11024016};
CC Note=Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
CC {ECO:0000269|PubMed:11024016};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:11024016};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:11024016};
CC -!- SUBUNIT: Interacts with REV1 (By similarity). Interacts with PCNA
CC (PubMed:11784855). {ECO:0000250|UniProtKB:Q9QUG2,
CC ECO:0000269|PubMed:11784855}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12414988,
CC ECO:0000269|PubMed:28297716}. Note=Detected throughout the nucleus and
CC at replication foci (PubMed:12414988). Recruited to DNA damage sites in
CC response to ultraviolet irradiation: N6-methyladenosine (m6A)-
CC containing mRNAs accumulate in the vicinity of DNA damage sites and
CC their presence is required to recruit POLK (PubMed:28297716).
CC {ECO:0000269|PubMed:12414988, ECO:0000269|PubMed:28297716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q9UBT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBT6-2; Sequence=VSP_012801, VSP_012802;
CC Name=3;
CC IsoId=Q9UBT6-3; Sequence=VSP_012803;
CC Name=4;
CC IsoId=Q9UBT6-4; Sequence=VSP_012804, VSP_012805, VSP_012806;
CC Name=5;
CC IsoId=Q9UBT6-5; Sequence=VSP_053406, VSP_053409;
CC Name=6;
CC IsoId=Q9UBT6-6; Sequence=VSP_053407, VSP_053408;
CC Name=7;
CC IsoId=Q9UBT6-7; Sequence=VSP_012804, VSP_053407, VSP_053408;
CC Name=8;
CC IsoId=Q9UBT6-8; Sequence=VSP_012804;
CC -!- TISSUE SPECIFICITY: Detected at low levels in testis, spleen, prostate
CC and ovary. Detected at very low levels in kidney, colon, brain, heart,
CC liver, lung, placenta, pancreas and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10518552, ECO:0000269|PubMed:10620008}.
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 -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/polk/";
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; AB027564; BAA86943.1; -; mRNA.
DR EMBL; AF163570; AAF02540.1; -; mRNA.
DR EMBL; AY769929; AAV80827.1; -; mRNA.
DR EMBL; AY769931; AAV80829.1; -; mRNA.
DR EMBL; AY769930; AAV80828.1; -; mRNA.
DR EMBL; AY769932; AAV80830.1; -; mRNA.
DR EMBL; AF194973; AAF23270.1; -; mRNA.
DR EMBL; AF315602; AAN15780.1; -; mRNA.
DR EMBL; AF318313; AAN15781.1; -; mRNA.
DR EMBL; AK091659; BAC03714.1; -; mRNA.
DR EMBL; AK314610; BAG37179.1; -; mRNA.
DR EMBL; AY273797; AAP12648.1; -; Genomic_DNA.
DR EMBL; AC010245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95763.1; -; Genomic_DNA.
DR EMBL; BC014955; AAH14955.1; -; mRNA.
DR EMBL; BC050718; AAH50718.1; -; mRNA.
DR EMBL; AB036934; BAB58975.1; -; Genomic_DNA.
DR EMBL; AB036935; BAB58976.1; -; Genomic_DNA.
DR CCDS; CCDS4030.1; -. [Q9UBT6-1]
DR RefSeq; NP_001332851.1; NM_001345922.1. [Q9UBT6-8]
DR RefSeq; NP_057302.1; NM_016218.3. [Q9UBT6-1]
DR RefSeq; XP_016865048.1; XM_017009559.1. [Q9UBT6-1]
DR RefSeq; XP_016865049.1; XM_017009560.1. [Q9UBT6-1]
DR RefSeq; XP_016865052.1; XM_017009563.1. [Q9UBT6-8]
DR PDB; 1T94; X-ray; 2.40 A; A/B=68-526.
DR PDB; 2LSI; NMR; -; B=562-577.
DR PDB; 2OH2; X-ray; 3.05 A; A/B=19-526.
DR PDB; 2W7O; X-ray; 3.16 A; A/B=19-526.
DR PDB; 2W7P; X-ray; 3.71 A; A/B=19-526.
DR PDB; 3IN5; X-ray; 3.20 A; A/B=19-526.
DR PDB; 3PZP; X-ray; 3.34 A; A/B=19-528.
DR PDB; 4BA9; X-ray; 2.73 A; A/B/C/D/E/F=563-575.
DR PDB; 4GK5; X-ray; 3.21 A; G=564-573.
DR PDB; 4U6P; X-ray; 2.59 A; A/B=1-526.
DR PDB; 4U7C; X-ray; 2.80 A; A/B=27-518.
DR PDB; 5T14; X-ray; 3.00 A; A/B=1-527.
DR PDB; 5W2A; X-ray; 2.90 A; A/B=1-526.
DR PDB; 5W2C; X-ray; 2.50 A; A/B=1-526.
DR PDB; 6BRX; X-ray; 2.80 A; A/B=1-526.
DR PDB; 6BS1; X-ray; 3.15 A; A/B=1-526.
DR PDB; 6CST; X-ray; 2.00 A; A/B=1-526.
DR PDB; 7NV0; EM; 3.40 A; A=1-870.
DR PDB; 7NV1; EM; 6.40 A; A=1-870.
DR PDBsum; 1T94; -.
DR PDBsum; 2LSI; -.
DR PDBsum; 2OH2; -.
DR PDBsum; 2W7O; -.
DR PDBsum; 2W7P; -.
DR PDBsum; 3IN5; -.
DR PDBsum; 3PZP; -.
DR PDBsum; 4BA9; -.
DR PDBsum; 4GK5; -.
DR PDBsum; 4U6P; -.
DR PDBsum; 4U7C; -.
DR PDBsum; 5T14; -.
DR PDBsum; 5W2A; -.
DR PDBsum; 5W2C; -.
DR PDBsum; 6BRX; -.
DR PDBsum; 6BS1; -.
DR PDBsum; 6CST; -.
DR PDBsum; 7NV0; -.
DR PDBsum; 7NV1; -.
DR AlphaFoldDB; Q9UBT6; -.
DR SMR; Q9UBT6; -.
DR BioGRID; 119532; 52.
DR CORUM; Q9UBT6; -.
DR IntAct; Q9UBT6; 34.
DR STRING; 9606.ENSP00000241436; -.
DR BindingDB; Q9UBT6; -.
DR ChEMBL; CHEMBL5365; -.
DR DrugBank; DB07435; 1,2,3-TRIHYDROXY-1,2,3,4-TETRAHYDROBENZO[A]PYRENE.
DR DrugBank; DB07652; 1-[2-DEOXYRIBOFURANOSYL]-2,4-DIFLUORO-5-METHYL-BENZENE-5'MONOPHOSPHATE.
DR DrugBank; DB08237; 2'-deoxy-N-(naphthalen-1-ylmethyl)guanosine 5'-(dihydrogen phosphate).
DR iPTMnet; Q9UBT6; -.
DR PhosphoSitePlus; Q9UBT6; -.
DR BioMuta; POLK; -.
DR DMDM; 59798438; -.
DR EPD; Q9UBT6; -.
DR jPOST; Q9UBT6; -.
DR MassIVE; Q9UBT6; -.
DR MaxQB; Q9UBT6; -.
DR PaxDb; Q9UBT6; -.
DR PeptideAtlas; Q9UBT6; -.
DR PRIDE; Q9UBT6; -.
DR ProteomicsDB; 63605; -.
DR ProteomicsDB; 63606; -.
DR ProteomicsDB; 63607; -.
DR ProteomicsDB; 84057; -. [Q9UBT6-1]
DR ProteomicsDB; 84058; -. [Q9UBT6-2]
DR ProteomicsDB; 84059; -. [Q9UBT6-3]
DR ProteomicsDB; 84060; -. [Q9UBT6-4]
DR Antibodypedia; 12396; 341 antibodies from 31 providers.
DR DNASU; 51426; -.
DR Ensembl; ENST00000241436.8; ENSP00000241436.4; ENSG00000122008.15. [Q9UBT6-1]
DR Ensembl; ENST00000504026.5; ENSP00000425075.1; ENSG00000122008.15. [Q9UBT6-6]
DR Ensembl; ENST00000508526.5; ENSP00000426853.1; ENSG00000122008.15. [Q9UBT6-3]
DR Ensembl; ENST00000509126.2; ENSP00000423532.1; ENSG00000122008.15. [Q9UBT6-5]
DR Ensembl; ENST00000510815.6; ENSP00000422094.2; ENSG00000122008.15. [Q9UBT6-4]
DR Ensembl; ENST00000515295.5; ENSP00000424174.1; ENSG00000122008.15. [Q9UBT6-2]
DR GeneID; 51426; -.
DR KEGG; hsa:51426; -.
DR UCSC; uc003kdw.4; human. [Q9UBT6-1]
DR CTD; 51426; -.
DR DisGeNET; 51426; -.
DR GeneCards; POLK; -.
DR HGNC; HGNC:9183; POLK.
DR HPA; ENSG00000122008; Low tissue specificity.
DR MalaCards; POLK; -.
DR MIM; 605650; gene.
DR neXtProt; NX_Q9UBT6; -.
DR OpenTargets; ENSG00000122008; -.
DR PharmGKB; PA33503; -.
DR VEuPathDB; HostDB:ENSG00000122008; -.
DR eggNOG; KOG2094; Eukaryota.
DR GeneTree; ENSGT00940000156667; -.
DR HOGENOM; CLU_012348_11_3_1; -.
DR InParanoid; Q9UBT6; -.
DR OMA; ETSWHNF; -.
DR PhylomeDB; Q9UBT6; -.
DR TreeFam; TF314387; -.
DR BRENDA; 2.7.7.7; 2681.
DR PathwayCommons; Q9UBT6; -.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
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 SignaLink; Q9UBT6; -.
DR BioGRID-ORCS; 51426; 17 hits in 1083 CRISPR screens.
DR ChiTaRS; POLK; human.
DR EvolutionaryTrace; Q9UBT6; -.
DR GeneWiki; POLK; -.
DR GenomeRNAi; 51426; -.
DR Pharos; Q9UBT6; Tbio.
DR PRO; PR:Q9UBT6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UBT6; protein.
DR Bgee; ENSG00000122008; Expressed in calcaneal tendon and 186 other tissues.
DR ExpressionAtlas; Q9UBT6; baseline and differential.
DR Genevisible; Q9UBT6; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:UniProtKB.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:UniProtKB.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_01113; DNApol_IV; 1.
DR IDEAL; IID00105; -.
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; IPR022880; DNApol_IV.
DR InterPro; IPR024728; PolY_HhH_motif.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF11798; IMS_HHH; 1.
DR SMART; SM00734; ZnF_Rad18; 2.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51908; ZF_UBZ4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA repair;
KW DNA replication; DNA synthesis; DNA-binding; DNA-directed DNA polymerase;
KW Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Repeat; Schiff base; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..870
FT /note="DNA polymerase kappa"
FT /id="PRO_0000173990"
FT DOMAIN 103..358
FT /note="UmuC"
FT ZN_FING 621..651
FT /note="UBZ4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT ZN_FING 776..806
FT /note="UBZ4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 816..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 646
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform 4, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15661663"
FT /id="VSP_012804"
FT VAR_SEQ 312..509
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_012803"
FT VAR_SEQ 453..489
FT /note="GRTVTIKLKNVNFEVKTRASTVSSVVSTAEEIFAIAK -> VFGYLVFPMKR
FT TGNTNKGALLAFYRLETKPCQPLSVH (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15661663"
FT /id="VSP_053406"
FT VAR_SEQ 453..472
FT /note="GRTVTIKLKNVNFEVKTRAS -> VLYFDMVSLVFKFFNSKMLP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012801"
FT VAR_SEQ 453..462
FT /note="GRTVTIKLKN -> KKYLPLLRNC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012805"
FT VAR_SEQ 453..461
FT /note="GRTVTIKLK -> VAQVEYRRL (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15661663"
FT /id="VSP_053407"
FT VAR_SEQ 462..870
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15661663"
FT /id="VSP_053408"
FT VAR_SEQ 463..870
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012806"
FT VAR_SEQ 473..870
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012802"
FT VAR_SEQ 490..870
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15661663"
FT /id="VSP_053409"
FT VARIANT 423
FT /note="S -> R (in dbSNP:rs35257416)"
FT /id="VAR_048886"
FT VARIANT 595
FT /note="T -> I (in dbSNP:rs5744713)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_021246"
FT VARIANT 612
FT /note="I -> V (in dbSNP:rs3822587)"
FT /id="VAR_021247"
FT VARIANT 635
FT /note="S -> N (in dbSNP:rs35501530)"
FT /id="VAR_048887"
FT VARIANT 832
FT /note="S -> N (in dbSNP:rs5744716)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_021248"
FT MUTAGEN 198
FT /note="D->A: Loss of DNA polymerase activity; when
FT associated with A-199."
FT /evidence="ECO:0000269|PubMed:11024016"
FT MUTAGEN 199
FT /note="E->A: Loss of DNA polymerase activity; when
FT associated with D-198."
FT /evidence="ECO:0000269|PubMed:11024016"
FT CONFLICT 21
FT /note="L -> F (in Ref. 11; BAB58975)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="I -> T (in Ref. 11; BAB58975)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> L (in Ref. 11; BAB58976)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> G (in Ref. 6; BAC03714)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="K -> N (in Ref. 4; AAF23270)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="M -> V (in Ref. 4; AAF23270)"
FT /evidence="ECO:0000305"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 48..73
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5W2A"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:6CST"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:1T94"
FT TURN 243..248
FT /evidence="ECO:0007829|PDB:1T94"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1T94"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:6CST"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:1T94"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 415..425
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 428..448
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 467..478
FT /evidence="ECO:0007829|PDB:6CST"
FT HELIX 481..499
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:6CST"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:7NV0"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:7NV0"
FT HELIX 567..574
FT /evidence="ECO:0007829|PDB:4BA9"
SQ SEQUENCE 870 AA; 98809 MW; 40CB259A65F6A796 CRC64;
MDSTKEKCDS YKDDLLLRMG LNDNKAGMEG LDKEKINKII MEATKGSRFY GNELKKEKQV
NQRIENMMQQ KAQITSQQLR KAQLQVDRFA MELEQSRNLS NTIVHIDMDA FYAAVEMRDN
PELKDKPIAV GSMSMLSTSN YHARRFGVRA AMPGFIAKRL CPQLIIVPPN FDKYRAVSKE
VKEILADYDP NFMAMSLDEA YLNITKHLEE RQNWPEDKRR YFIKMGSSVE NDNPGKEVNK
LSEHERSISP LLFEESPSDV QPPGDPFQVN FEEQNNPQIL QNSVVFGTSA QEVVKEIRFR
IEQKTTLTAS AGIAPNTMLA KVCSDKNKPN GQYQILPNRQ AVMDFIKDLP IRKVSGIGKV
TEKMLKALGI ITCTELYQQR ALLSLLFSET SWHYFLHISL GLGSTHLTRD GERKSMSVER
TFSEINKAEE QYSLCQELCS ELAQDLQKER LKGRTVTIKL KNVNFEVKTR ASTVSSVVST
AEEIFAIAKE LLKTEIDADF PHPLRLRLMG VRISSFPNEE DRKHQQRSII GFLQAGNQAL
SATECTLEKT DKDKFVKPLE MSHKKSFFDK KRSERKWSHQ DTFKCEAVNK QSFQTSQPFQ
VLKKKMNENL EISENSDDCQ ILTCPVCFRA QGCISLEALN KHVDECLDGP SISENFKMFS
CSHVSATKVN KKENVPASSL CEKQDYEAHP KIKEISSVDC IALVDTIDNS SKAESIDALS
NKHSKEECSS LPSKSFNIEH CHQNSSSTVS LENEDVGSFR QEYRQPYLCE VKTGQALVCP
VCNVEQKTSD LTLFNVHVDV CLNKSFIQEL RKDKFNPVNQ PKESSRSTGS SSGVQKAVTR
TKRPGLMTKY STSKKIKPNN PKHTLDIFFK
