DPOLM_HUMAN
ID DPOLM_HUMAN Reviewed; 494 AA.
AC Q9NP87; D3DVK4; Q6P5X8; Q86WQ9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=DNA-directed DNA/RNA polymerase mu;
DE Short=Pol Mu;
DE EC=2.7.7.7;
DE AltName: Full=Terminal transferase;
GN Name=POLM; Synonyms=polmu;
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=Placenta;
RX PubMed=10747040; DOI=10.1093/emboj/19.7.1731;
RA Dominguez O., Ruiz J.F., Lain de Lera T., Garcia-Diaz M., Gonzalez M.A.,
RA Kirchhoff T., Martinez-A C., Bernad A., Blanco L.;
RT "DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator
RT in eukaryotic cells.";
RL EMBO J. 19:1731-1742(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10982892; DOI=10.1093/nar/28.18.3684;
RA Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S.,
RA Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.;
RT "Two novel human and mouse DNA polymerases of the polX family.";
RL Nucleic Acids Res. 28:3684-3693(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-107; ALA-220; PHE-246
RP AND PHE-484.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Blood, and Brain;
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 [7]
RP FUNCTION.
RX PubMed=12640116; DOI=10.1128/mcb.23.7.2309-2315.2003;
RA Nick McElhinny S.A., Ramsden D.A.;
RT "Polymerase mu is a DNA-directed DNA/RNA polymerase.";
RL Mol. Cell. Biol. 23:2309-2315(2003).
RN [8]
RP FUNCTION, AND SUGAR DISCRIMINATION SITE.
RX PubMed=12888504; DOI=10.1093/nar/gkg637;
RA Ruiz J.F., Juarez R., Garcia-Diaz M., Terrados G., Picher A.J.,
RA Gonzalez-Barrera S., Fernandez de Henestrosa A.R., Blanco L.;
RT "Lack of sugar discrimination by human Pol mu requires a single glycine
RT residue.";
RL Nucleic Acids Res. 31:4441-4449(2003).
RN [9]
RP FUNCTION.
RX PubMed=17483519; DOI=10.1093/nar/gkm243;
RA Capp J.P., Boudsocq F., Besnard A.G., Lopez B.S., Cazaux C., Hoffmann J.S.,
RA Canitrot Y.;
RT "Involvement of DNA polymerase mu in the repair of a specific subset of DNA
RT double-strand breaks in mammalian cells.";
RL Nucleic Acids Res. 35:3551-3560(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP STRUCTURE BY NMR OF 21-124, AND FUNCTION.
RX PubMed=17915942; DOI=10.1021/bi7007728;
RA DeRose E.F., Clarkson M.W., Gilmore S.A., Galban C.J., Tripathy A.,
RA Havener J.M., Mueller G.A., Ramsden D.A., London R.E., Lee A.L.;
RT "Solution structure of polymerase mu's BRCT Domain reveals an element
RT essential for its role in nonhomologous end joining.";
RL Biochemistry 46:12100-12110(2007).
RN [16]
RP STRUCTURE BY NMR OF 18-147.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of BRCT domain of DNA polymerase mu.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC strand breaks by non-homologous end joining (NHEJ). Participates in
CC immunoglobulin (Ig) light chain gene rearrangement in V(D)J
CC recombination. {ECO:0000269|PubMed:12640116,
CC ECO:0000269|PubMed:12888504, ECO:0000269|PubMed:17483519,
CC ECO:0000269|PubMed:17915942}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q9NP87; P14079: tax; Xeno; NbExp=3; IntAct=EBI-9675790, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NP87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP87-2; Sequence=VSP_055290;
CC Name=3;
CC IsoId=Q9NP87-3; Sequence=VSP_055288, VSP_055289, VSP_055291;
CC -!- TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in
CC thymus.
CC -!- MISCELLANEOUS: DPOLM has a reduced ability to distinguish dNTP and rNTP
CC as substrates, and elongates them on DNA primer strand with a similar
CC efficiency. It is able to polymerize nucleotides on RNA primer strands.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/polm/";
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DR EMBL; AJ131891; CAB65075.2; -; mRNA.
DR EMBL; AF176097; AAF26284.1; -; mRNA.
DR EMBL; AY899911; AAW65376.1; -; Genomic_DNA.
DR EMBL; AC017116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471128; EAW61122.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61123.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61124.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61126.1; -; Genomic_DNA.
DR EMBL; BC049202; AAH49202.2; -; mRNA.
DR EMBL; BC062590; AAH62590.1; -; mRNA.
DR CCDS; CCDS34625.1; -. [Q9NP87-1]
DR CCDS; CCDS64635.1; -. [Q9NP87-2]
DR CCDS; CCDS64636.1; -. [Q9NP87-3]
DR RefSeq; NP_001271259.1; NM_001284330.1. [Q9NP87-3]
DR RefSeq; NP_001271260.1; NM_001284331.1. [Q9NP87-2]
DR RefSeq; NP_037416.1; NM_013284.3. [Q9NP87-1]
DR PDB; 2DUN; NMR; -; A=24-143.
DR PDB; 2HTF; NMR; -; A=21-124.
DR PDB; 4LZD; X-ray; 1.85 A; A=132-397, A=411-494.
DR PDB; 4LZG; X-ray; 1.60 A; A=132-397, A=411-494.
DR PDB; 4M04; X-ray; 1.90 A; A=132-397, A=411-494.
DR PDB; 4M0A; X-ray; 1.85 A; A=132-397, A=411-494.
DR PDB; 4YCX; X-ray; 2.10 A; A=134-494.
DR PDB; 4YD1; X-ray; 1.75 A; A=134-494.
DR PDB; 4YD2; X-ray; 2.47 A; A=134-397, A=411-494.
DR PDB; 5TWP; X-ray; 2.00 A; A=134-397, A=411-494.
DR PDB; 5TWQ; X-ray; 1.80 A; A=134-397, A=411-494.
DR PDB; 5TWR; X-ray; 1.90 A; A=134-397, A=411-494.
DR PDB; 5TWS; X-ray; 1.85 A; A=134-397, A=411-494.
DR PDB; 5TXX; X-ray; 1.95 A; A=132-494.
DR PDB; 5TXZ; X-ray; 1.65 A; A=132-494.
DR PDB; 5TYB; X-ray; 1.85 A; A=132-494.
DR PDB; 5TYC; X-ray; 2.10 A; A=132-494.
DR PDB; 5TYD; X-ray; 1.90 A; A=132-494.
DR PDB; 5TYE; X-ray; 2.05 A; A=132-494.
DR PDB; 5TYF; X-ray; 1.97 A; A=132-494.
DR PDB; 5TYG; X-ray; 1.73 A; A=132-494.
DR PDB; 5TYU; X-ray; 2.05 A; A=132-494.
DR PDB; 5TYV; X-ray; 1.93 A; A=132-494.
DR PDB; 5TYW; X-ray; 1.88 A; A=132-494.
DR PDB; 5TYX; X-ray; 1.95 A; A=132-494.
DR PDB; 5TYY; X-ray; 1.93 A; A=132-494.
DR PDB; 5TYZ; X-ray; 1.98 A; A=132-494.
DR PDB; 5VZ7; X-ray; 1.55 A; A=134-397, A=411-494.
DR PDB; 5VZ8; X-ray; 1.60 A; A=134-397, A=411-494.
DR PDB; 5VZ9; X-ray; 1.65 A; A=134-397, A=411-494.
DR PDB; 5VZA; X-ray; 1.50 A; A=134-397, A=411-494.
DR PDB; 5VZB; X-ray; 1.50 A; A=134-397, A=411-494.
DR PDB; 5VZC; X-ray; 1.55 A; A=134-397, A=411-494.
DR PDB; 5VZD; X-ray; 1.60 A; A=134-397, A=411-494.
DR PDB; 5VZE; X-ray; 1.51 A; A=134-397, A=411-494.
DR PDB; 5VZF; X-ray; 1.65 A; A=134-397, A=411-494.
DR PDB; 5VZG; X-ray; 1.85 A; A=134-397, A=411-494.
DR PDB; 5VZH; X-ray; 1.95 A; A=134-397, A=411-494.
DR PDB; 5VZI; X-ray; 1.50 A; A=134-397, A=411-494.
DR PDB; 5W4F; X-ray; 1.98 A; A/D=2-30.
DR PDB; 5ZLC; X-ray; 2.00 A; A=132-397, A=411-494.
DR PDB; 6AEC; X-ray; 1.72 A; A=132-397, A=411-494.
DR PDB; 6AEH; X-ray; 1.64 A; A=132-397, A=411-494.
DR PDB; 6AK5; X-ray; 1.70 A; A=132-397, A=411-494.
DR PDB; 6AK6; X-ray; 1.75 A; A=132-397, A=411-494.
DR PDB; 6AK8; X-ray; 1.74 A; A=132-397, A=411-494.
DR PDB; 6AK9; X-ray; 1.91 A; A=132-397, A=411-494.
DR PDB; 6AKH; X-ray; 1.75 A; A=132-397, A=411-494.
DR PDB; 6IPD; X-ray; 1.70 A; A=132-397, A=411-494.
DR PDB; 6IPE; X-ray; 1.70 A; A=132-397, A=411-494.
DR PDB; 6IPF; X-ray; 1.77 A; A=132-397, A=411-494.
DR PDB; 6IPG; X-ray; 1.62 A; A=132-397, A=411-494.
DR PDB; 6IPH; X-ray; 1.65 A; A=132-397, A=411-494.
DR PDB; 6IPI; X-ray; 1.80 A; A=132-397, A=411-494.
DR PDB; 6IPJ; X-ray; 1.98 A; A=132-397, A=411-494.
DR PDB; 6IPK; X-ray; 2.15 A; A=132-397, A=411-494.
DR PDB; 6IPL; X-ray; 1.64 A; A=132-397, A=411-494.
DR PDB; 6IPM; X-ray; 1.72 A; A=132-397, A=411-494.
DR PDB; 6IPN; X-ray; 1.60 A; A=132-397, A=411-494.
DR PDB; 6P1M; X-ray; 1.65 A; A=134-397, A=411-494.
DR PDB; 6P1N; X-ray; 1.60 A; A=134-397, A=411-494.
DR PDB; 6P1O; X-ray; 1.65 A; A=134-397, A=411-494.
DR PDB; 6P1P; X-ray; 1.75 A; A=134-397, A=411-494.
DR PDB; 6P1Q; X-ray; 1.90 A; A=134-397, A=411-494.
DR PDB; 6P1R; X-ray; 1.70 A; A=134-397, A=411-494.
DR PDB; 6P1S; X-ray; 1.75 A; A=134-397, A=411-494.
DR PDB; 6P1T; X-ray; 1.70 A; A=134-397, A=411-494.
DR PDB; 6P1U; X-ray; 1.75 A; A=134-397, A=411-494.
DR PDB; 6P1V; X-ray; 1.95 A; A=134-397, A=411-494.
DR PDB; 6P1W; X-ray; 1.75 A; A=134-397, A=411-494.
DR PDB; 6VEZ; X-ray; 1.88 A; A=132-494.
DR PDB; 6VF0; X-ray; 1.58 A; A=132-494.
DR PDB; 6VF1; X-ray; 1.68 A; A=132-494.
DR PDB; 6VF2; X-ray; 1.60 A; A=132-494.
DR PDB; 6VF3; X-ray; 1.52 A; A=132-494.
DR PDB; 6VF4; X-ray; 1.75 A; A=132-494.
DR PDB; 6VF5; X-ray; 1.60 A; A=132-494.
DR PDB; 6VF6; X-ray; 1.69 A; A=132-494.
DR PDB; 6VF7; X-ray; 1.87 A; A=132-494.
DR PDB; 6VF8; X-ray; 1.70 A; A=132-494.
DR PDB; 6VF9; X-ray; 1.56 A; A=132-494.
DR PDB; 6VFA; X-ray; 1.76 A; A=132-494.
DR PDB; 6VFB; X-ray; 1.55 A; A=132-494.
DR PDB; 6VFC; X-ray; 1.59 A; A=132-494.
DR PDB; 6WIC; X-ray; 1.55 A; A=132-397, A=411-494.
DR PDB; 6WID; X-ray; 1.50 A; A=132-397, A=411-494.
DR PDB; 6WIE; X-ray; 1.50 A; A=132-397, A=411-494.
DR PDB; 7CO6; X-ray; 1.90 A; A=1-494.
DR PDB; 7CO8; X-ray; 1.70 A; A=1-494.
DR PDB; 7CO9; X-ray; 1.60 A; A=1-494.
DR PDB; 7COA; X-ray; 1.70 A; A=1-494.
DR PDB; 7COB; X-ray; 1.80 A; A=1-494.
DR PDB; 7COC; X-ray; 1.90 A; A=1-494.
DR PDB; 7COD; X-ray; 1.80 A; A=1-494.
DR PDB; 7KST; X-ray; 1.60 A; A=132-494.
DR PDB; 7KSU; X-ray; 1.65 A; A=127-494.
DR PDB; 7KSV; X-ray; 1.64 A; A=132-494.
DR PDB; 7KSW; X-ray; 1.49 A; A=132-494.
DR PDB; 7KSX; X-ray; 1.57 A; A=132-494.
DR PDB; 7KSY; X-ray; 1.58 A; A=132-494.
DR PDB; 7KSZ; X-ray; 1.42 A; A=127-494.
DR PDB; 7KT0; X-ray; 1.36 A; A=127-494.
DR PDB; 7KT1; X-ray; 1.67 A; A=127-494.
DR PDB; 7KT2; X-ray; 1.50 A; A=127-494.
DR PDB; 7KT3; X-ray; 1.88 A; A=132-397, A=411-494.
DR PDB; 7KT4; X-ray; 1.92 A; A=132-397, A=411-494.
DR PDB; 7KT5; X-ray; 1.46 A; A=132-397, A=411-494.
DR PDB; 7KT6; X-ray; 1.87 A; A=132-397, A=411-494.
DR PDB; 7KT7; X-ray; 1.76 A; A=132-397, A=411-494.
DR PDB; 7KT8; X-ray; 1.70 A; A=132-397, A=411-494.
DR PDB; 7KT9; X-ray; 1.48 A; A=132-397, A=411-494.
DR PDB; 7KTA; X-ray; 1.84 A; A=132-397, A=411-494.
DR PDB; 7KTE; X-ray; 1.48 A; A=132-397, A=411-494.
DR PDB; 7KTF; X-ray; 1.49 A; A=132-397, A=411-494.
DR PDB; 7KTG; X-ray; 1.45 A; A=132-397, A=411-494.
DR PDB; 7KTN; X-ray; 1.33 A; A=132-397, A=411-494.
DR PDBsum; 2DUN; -.
DR PDBsum; 2HTF; -.
DR PDBsum; 4LZD; -.
DR PDBsum; 4LZG; -.
DR PDBsum; 4M04; -.
DR PDBsum; 4M0A; -.
DR PDBsum; 4YCX; -.
DR PDBsum; 4YD1; -.
DR PDBsum; 4YD2; -.
DR PDBsum; 5TWP; -.
DR PDBsum; 5TWQ; -.
DR PDBsum; 5TWR; -.
DR PDBsum; 5TWS; -.
DR PDBsum; 5TXX; -.
DR PDBsum; 5TXZ; -.
DR PDBsum; 5TYB; -.
DR PDBsum; 5TYC; -.
DR PDBsum; 5TYD; -.
DR PDBsum; 5TYE; -.
DR PDBsum; 5TYF; -.
DR PDBsum; 5TYG; -.
DR PDBsum; 5TYU; -.
DR PDBsum; 5TYV; -.
DR PDBsum; 5TYW; -.
DR PDBsum; 5TYX; -.
DR PDBsum; 5TYY; -.
DR PDBsum; 5TYZ; -.
DR PDBsum; 5VZ7; -.
DR PDBsum; 5VZ8; -.
DR PDBsum; 5VZ9; -.
DR PDBsum; 5VZA; -.
DR PDBsum; 5VZB; -.
DR PDBsum; 5VZC; -.
DR PDBsum; 5VZD; -.
DR PDBsum; 5VZE; -.
DR PDBsum; 5VZF; -.
DR PDBsum; 5VZG; -.
DR PDBsum; 5VZH; -.
DR PDBsum; 5VZI; -.
DR PDBsum; 5W4F; -.
DR PDBsum; 5ZLC; -.
DR PDBsum; 6AEC; -.
DR PDBsum; 6AEH; -.
DR PDBsum; 6AK5; -.
DR PDBsum; 6AK6; -.
DR PDBsum; 6AK8; -.
DR PDBsum; 6AK9; -.
DR PDBsum; 6AKH; -.
DR PDBsum; 6IPD; -.
DR PDBsum; 6IPE; -.
DR PDBsum; 6IPF; -.
DR PDBsum; 6IPG; -.
DR PDBsum; 6IPH; -.
DR PDBsum; 6IPI; -.
DR PDBsum; 6IPJ; -.
DR PDBsum; 6IPK; -.
DR PDBsum; 6IPL; -.
DR PDBsum; 6IPM; -.
DR PDBsum; 6IPN; -.
DR PDBsum; 6P1M; -.
DR PDBsum; 6P1N; -.
DR PDBsum; 6P1O; -.
DR PDBsum; 6P1P; -.
DR PDBsum; 6P1Q; -.
DR PDBsum; 6P1R; -.
DR PDBsum; 6P1S; -.
DR PDBsum; 6P1T; -.
DR PDBsum; 6P1U; -.
DR PDBsum; 6P1V; -.
DR PDBsum; 6P1W; -.
DR PDBsum; 6VEZ; -.
DR PDBsum; 6VF0; -.
DR PDBsum; 6VF1; -.
DR PDBsum; 6VF2; -.
DR PDBsum; 6VF3; -.
DR PDBsum; 6VF4; -.
DR PDBsum; 6VF5; -.
DR PDBsum; 6VF6; -.
DR PDBsum; 6VF7; -.
DR PDBsum; 6VF8; -.
DR PDBsum; 6VF9; -.
DR PDBsum; 6VFA; -.
DR PDBsum; 6VFB; -.
DR PDBsum; 6VFC; -.
DR PDBsum; 6WIC; -.
DR PDBsum; 6WID; -.
DR PDBsum; 6WIE; -.
DR PDBsum; 7CO6; -.
DR PDBsum; 7CO8; -.
DR PDBsum; 7CO9; -.
DR PDBsum; 7COA; -.
DR PDBsum; 7COB; -.
DR PDBsum; 7COC; -.
DR PDBsum; 7COD; -.
DR PDBsum; 7KST; -.
DR PDBsum; 7KSU; -.
DR PDBsum; 7KSV; -.
DR PDBsum; 7KSW; -.
DR PDBsum; 7KSX; -.
DR PDBsum; 7KSY; -.
DR PDBsum; 7KSZ; -.
DR PDBsum; 7KT0; -.
DR PDBsum; 7KT1; -.
DR PDBsum; 7KT2; -.
DR PDBsum; 7KT3; -.
DR PDBsum; 7KT4; -.
DR PDBsum; 7KT5; -.
DR PDBsum; 7KT6; -.
DR PDBsum; 7KT7; -.
DR PDBsum; 7KT8; -.
DR PDBsum; 7KT9; -.
DR PDBsum; 7KTA; -.
DR PDBsum; 7KTE; -.
DR PDBsum; 7KTF; -.
DR PDBsum; 7KTG; -.
DR PDBsum; 7KTN; -.
DR AlphaFoldDB; Q9NP87; -.
DR BMRB; Q9NP87; -.
DR SMR; Q9NP87; -.
DR BioGRID; 118168; 22.
DR ELM; Q9NP87; -.
DR IntAct; Q9NP87; 6.
DR MINT; Q9NP87; -.
DR BindingDB; Q9NP87; -.
DR ChEMBL; CHEMBL1914260; -.
DR iPTMnet; Q9NP87; -.
DR PhosphoSitePlus; Q9NP87; -.
DR BioMuta; POLM; -.
DR DMDM; 17366980; -.
DR EPD; Q9NP87; -.
DR jPOST; Q9NP87; -.
DR MassIVE; Q9NP87; -.
DR MaxQB; Q9NP87; -.
DR PaxDb; Q9NP87; -.
DR PeptideAtlas; Q9NP87; -.
DR PRIDE; Q9NP87; -.
DR ProteomicsDB; 67013; -.
DR ProteomicsDB; 70190; -.
DR ProteomicsDB; 81932; -. [Q9NP87-1]
DR Antibodypedia; 13228; 145 antibodies from 31 providers.
DR DNASU; 27434; -.
DR Ensembl; ENST00000242248.10; ENSP00000242248.5; ENSG00000122678.17. [Q9NP87-1]
DR Ensembl; ENST00000335195.10; ENSP00000335141.6; ENSG00000122678.17. [Q9NP87-2]
DR Ensembl; ENST00000395831.7; ENSP00000379174.3; ENSG00000122678.17. [Q9NP87-3]
DR GeneID; 27434; -.
DR KEGG; hsa:27434; -.
DR MANE-Select; ENST00000242248.10; ENSP00000242248.5; NM_013284.4; NP_037416.1.
DR UCSC; uc003tjt.5; human. [Q9NP87-1]
DR CTD; 27434; -.
DR DisGeNET; 27434; -.
DR GeneCards; POLM; -.
DR HGNC; HGNC:9185; POLM.
DR HPA; ENSG00000122678; Low tissue specificity.
DR MIM; 606344; gene.
DR neXtProt; NX_Q9NP87; -.
DR OpenTargets; ENSG00000122678; -.
DR PharmGKB; PA33505; -.
DR VEuPathDB; HostDB:ENSG00000122678; -.
DR eggNOG; KOG2534; Eukaryota.
DR GeneTree; ENSGT00940000158490; -.
DR HOGENOM; CLU_008698_0_1_1; -.
DR InParanoid; Q9NP87; -.
DR OMA; WTGSQLF; -.
DR OrthoDB; 1212057at2759; -.
DR PhylomeDB; Q9NP87; -.
DR TreeFam; TF103012; -.
DR BRENDA; 2.7.7.7; 2681.
DR PathwayCommons; Q9NP87; -.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR SignaLink; Q9NP87; -.
DR BioGRID-ORCS; 27434; 18 hits in 1083 CRISPR screens.
DR EvolutionaryTrace; Q9NP87; -.
DR GeneWiki; DNA_polymerase_mu; -.
DR GenomeRNAi; 27434; -.
DR Pharos; Q9NP87; Tbio.
DR PRO; PR:Q9NP87; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NP87; protein.
DR Bgee; ENSG00000122678; Expressed in granulocyte and 91 other tissues.
DR ExpressionAtlas; Q9NP87; baseline and differential.
DR Genevisible; Q9NP87; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F: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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR027249; DNA/RNApol_mu.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR InterPro; IPR001726; TdT/Mu.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PIRSF; PIRSF000817; DNA_NT; 1.
DR PIRSF; PIRSF501176; DNApol_mu; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00871; DNAPOLXTDT.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA damage; DNA recombination;
KW DNA repair; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..494
FT /note="DNA-directed DNA/RNA polymerase mu"
FT /id="PRO_0000218787"
FT DOMAIN 22..122
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..332
FT /note="Involved in ssDNA binding"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 433
FT /note="Responsible for the low discrimination between dNTP
FT and rNTP"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 234..276
FT /note="YQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQ -> APAPP
FT GPEHPSPAVRCRCPAAGGGGSCGAGPAWGHRHADRRLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055288"
FT VAR_SEQ 277..356
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055289"
FT VAR_SEQ 279..356
FT /note="GLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHD
FT VDFLITHPKEGQEAGLLPRVMCRLQD -> APPGPEHPSPAVRCRCPAAGGGGSCGAGP
FT AWGHRHADRRLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055290"
FT VAR_SEQ 467..494
FT /note="KTFFQAASEEDIFRHLGLEYLPPEQRNA -> GSSSGKTPRSRKSCFCCRRH
FT FSKRLQRKTSSDTWALSTFLQSRETPEPACVPHFHSGNWAAPNLATECLQADMLPPDPH
FT LHPSPPRPGSSGGQLCLQDQLSPCWCAAGCDEVGALSASLITV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055291"
FT VARIANT 107
FT /note="E -> D (in dbSNP:rs28382635)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022287"
FT VARIANT 220
FT /note="G -> A (in dbSNP:rs28382644)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022288"
FT VARIANT 246
FT /note="V -> F (in dbSNP:rs28382653)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022289"
FT VARIANT 484
FT /note="L -> F (in dbSNP:rs28382661)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022290"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:2DUN"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2DUN"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:2DUN"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2DUN"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2DUN"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:2DUN"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2DUN"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2DUN"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2DUN"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:7KT0"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 292..309
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:7KTN"
FT TURN 340..345
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:7KTN"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:6VF1"
FT STRAND 387..396
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 411..421
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 427..435
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:7KTN"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:7KTN"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:7KTN"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:7KTN"
SQ SEQUENCE 494 AA; 54816 MW; B944059725F8B61F CRC64;
MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL ARSKGFRVLD
ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL DISWLTESLG AGQPVPVECR
HRLEVAGPRK GPLSPAWMPA YACQRPTPLT HHNTGLSEAL EILAEAAGFE GSEGRLLTFC
RAASVLKALP SPVTTLSQLQ GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF
TQIFGVGVKT ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV MCRLQDQGLI
LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA AVGGSTRPCP SWKAVRVDLV
VAPVSQFPFA LLGWTGSKLF QRELRRFSRK EKGLWLNSHG LFDPEQKTFF QAASEEDIFR
HLGLEYLPPE QRNA
