ID   DNLI3_HUMAN             Reviewed;        1009 AA.
AC   P49916; E5KLB5; E5KLB6; Q16714; Q6NVK3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=DNA ligase 3;
DE            EC=6.5.1.1 {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:20518483};
DE   AltName: Full=DNA ligase III;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 3;
DE   Flags: Precursor;
GN   Name=LIG3;
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 3), AND INTERACTION WITH XRCC1.
RC   TISSUE=Prostate;
RX   PubMed=7760816; DOI=10.1128/mcb.15.6.3206;
RA   Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C., Yu G.-L.,
RA   Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E., Haseltine W.A.,
RA   Lindahl T.;
RT   "Molecular cloning and expression of human cDNAs encoding a novel DNA
RT   ligase IV and DNA ligase III, an enzyme active in DNA repair and
RT   recombination.";
RL   Mol. Cell. Biol. 15:3206-3216(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   TISSUE=Testis;
RX   PubMed=7565692; DOI=10.1128/mcb.15.10.5412;
RA   Chen J., Tomkinson A.E., Ramos W., Mackey Z.B., Danehower S., Walter C.A.,
RA   Schultz R.A., Besterman J.M., Husain I.;
RT   "Mammalian DNA ligase III: molecular cloning, chromosomal localization, and
RT   expression in spermatocytes undergoing meiotic recombination.";
RL   Mol. Cell. Biol. 15:5412-5422(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-768.
RX   PubMed=20843780; DOI=10.1093/nar/gkq750;
RA   Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
RA   Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M.,
RA   Speed T.P., Scharfe C.;
RT   "Identification of rare DNA variants in mitochondrial disorders with
RT   improved array-based sequencing.";
RL   Nucleic Acids Res. 39:44-58(2011).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-867.
RG   NIEHS SNPs program;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP   INITIATION.
RX   PubMed=10207110; DOI=10.1128/mcb.19.5.3869;
RA   Lakshmipathy U., Campbell C.;
RT   "The human DNA ligase III gene encodes nuclear and mitochondrial
RT   proteins.";
RL   Mol. Cell. Biol. 19:3869-3876(1999).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, 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   [12]
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   [13]
RP   INTERACTION WITH POLB.
RX   PubMed=19336415; DOI=10.1093/nar/gkp201;
RA   Guo Z., Zheng L., Dai H., Zhou M., Xu H., Shen B.;
RT   "Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase
RT   activity and interaction with PCNA and the cellular base excision repair
RT   capacity.";
RL   Nucleic Acids Res. 37:3431-3441(2009).
RN   [14]
RP   IDENTIFICATION BY 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-216; SER-242 AND
RP   SER-913, AND IDENTIFICATION BY 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   [19]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24674627; DOI=10.1016/j.dnarep.2014.01.015;
RA   Akbari M., Keijzers G., Maynard S., Scheibye-Knudsen M., Desler C.,
RA   Hickson I.D., Bohr V.A.;
RT   "Overexpression of DNA ligase III in mitochondria protects cells against
RT   oxidative stress and improves mitochondrial DNA base excision repair.";
RL   DNA Repair 16:44-53(2014).
RN   [20]
RP   STRUCTURE BY NMR OF 924-1009.
RX   PubMed=11281714; DOI=10.1006/prep.2001.1391;
RA   Thornton K.H., Krishnan V.V., West M.G., Popham J., Ramirez M.,
RA   Thelen M.P., Cosman M.;
RT   "Expression, purification, and biophysical characterization of the BRCT
RT   domain of human DNA ligase IIIalpha.";
RL   Protein Expr. Purif. 21:401-411(2001).
RN   [21]
RP   STRUCTURE BY NMR OF 1-204 IN COMPLEX WITH ZINC.
RX   PubMed=15288782; DOI=10.1016/j.jmb.2004.06.035;
RA   Kulczyk A.W., Yang J.C., Neuhaus D.;
RT   "Solution structure and DNA binding of the zinc-finger domain from DNA
RT   ligase IIIalpha.";
RL   J. Mol. Biol. 341:723-738(2004).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 257-833 IN COMPLEX WITH DNA AND
RP   AMP, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF
RP   LYS-410 AND ARG-414.
RX   PubMed=20518483; DOI=10.1021/bi100503w;
RA   Cotner-Gohara E., Kim I.K., Hammel M., Tainer J.A., Tomkinson A.E.,
RA   Ellenberger T.;
RT   "Human DNA ligase III recognizes DNA ends by dynamic switching between two
RT   DNA-bound states.";
RL   Biochemistry 49:6165-6176(2010).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 924-1009 IN COMPLEX WITH XRCC1,
RP   AND INTERACTION WITH XRCC1.
RX   PubMed=21652643; DOI=10.1093/nar/gkr419;
RA   Cuneo M.J., Gabel S.A., Krahn J.M., Ricker M.A., London R.E.;
RT   "The structural basis for partitioning of the XRCC1/DNA ligase III-? BRCT-
RT   mediated dimer complexes.";
RL   Nucleic Acids Res. 39:7816-7827(2011).
RN   [24]
RP   VARIANT [LARGE SCALE ANALYSIS] ASN-717.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [25]
RP   VARIANTS MTDPS20 267-ARG--CYS-1009 DEL; ASN-537; LEU-609; 811-ARG--CYS-1009
RP   DEL; ARG-964 AND TYR-999, CHARACTERIZATION OF VARIANTS MTDPS20 ASN-537;
RP   LEU-609; ARG-964 AND TYR-999, INVOLVEMENT IN MTDPS20, AND INTERACTION WITH
RP   POLG.
RX   PubMed=33855352; DOI=10.1093/brain/awab056;
RA   Bonora E., Chakrabarty S., Kellaris G., Tsutsumi M., Bianco F.,
RA   Bergamini C., Ullah F., Isidori F., Liparulo I., Diquigiovanni C.,
RA   Masin L., Rizzardi N., Cratere M.G., Boschetti E., Papa V., Maresca A.,
RA   Cenacchi G., Casadio R., Martelli P., Matera I., Ceccherini I., Fato R.,
RA   Raiola G., Arrigo S., Signa S., Sementa A.R., Severino M., Striano P.,
RA   Fiorillo C., Goto T., Uchino S., Oyazato Y., Nakamura H., Mishra S.K.,
RA   Yeh Y.S., Kato T., Nozu K., Tanboon J., Morioka I., Nishino I., Toda T.,
RA   Goto Y.I., Ohtake A., Kosaki K., Yamaguchi Y., Nonaka I., Iijima K.,
RA   Mimaki M., Kurahashi H., Raams A., MacInnes A., Alders M., Engelen M.,
RA   Linthorst G., de Koning T., den Dunnen W., Dijkstra G., van Spaendonck K.,
RA   van Gent D.C., Aronica E.M., Picco P., Carelli V., Seri M., Katsanis N.,
RA   Duijkers F.A.M., Taniguchi-Ikeda M., De Giorgio R.;
RT   "Biallelic variants in LIG3 cause a novel mitochondrial
RT   neurogastrointestinal encephalomyopathy.";
RL   Brain 144:1451-1466(2021).
RN   [26]
RP   VARIANT MTDPS20 29-TRP--CYS-1009 DEL, AND INVOLVEMENT IN MTDPS20.
RX   PubMed=34165507; DOI=10.1093/brain/awab238;
RA   Invernizzi F., Legati A., Nasca A., Lamantea E., Garavaglia B., Gusic M.,
RA   Kopajtich R., Prokisch H., Zeviani M., Lamperti C., Ghezzi D.;
RT   "Myopathic mitochondrial DNA depletion syndrome associated with biallelic
RT   variants in LIG3.";
RL   Brain 144:e74-e74(2021).
CC   -!- FUNCTION: Isoform 3 functions as a heterodimer with DNA-repair protein
CC       XRCC1 in the nucleus and can correct defective DNA strand-break repair
CC       and sister chromatid exchange following treatment with ionizing
CC       radiation and alkylating agents. Isoform 1 is targeted to mitochondria,
CC       where it functions as a DNA ligase in mitochondrial base-excision DNA
CC       repair (PubMed:10207110, PubMed:24674627).
CC       {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135, ECO:0000269|PubMed:10207110,
CC         ECO:0000269|PubMed:20518483};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Isoform 3 interacts (via BRCT domain) with the nuclear DNA-
CC       repair protein XRCC1. Interacts with POLG (PubMed:33855352). Interacts
CC       with POLB (PubMed:19336415). {ECO:0000269|PubMed:19336415,
CC       ECO:0000269|PubMed:21652643, ECO:0000269|PubMed:33855352,
CC       ECO:0000269|PubMed:7760816}.
CC   -!- INTERACTION:
CC       P49916; P61244: MAX; NbExp=2; IntAct=EBI-1753381, EBI-751711;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC       {ECO:0000269|PubMed:10207110, ECO:0000269|PubMed:24674627}.
CC       Note=Contains an N-terminal mitochondrial transit peptide.
CC       {ECO:0000269|PubMed:10207110}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC       {ECO:0000305|PubMed:10207110}. Note=Contains an N-terminal
CC       mitochondrial transit peptide. {ECO:0000305|PubMed:10207110}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC       {ECO:0000269|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial
CC       transit peptide. {ECO:0000269|PubMed:10207110}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus
CC       {ECO:0000305|PubMed:10207110}. Note=Lacks the N-terminal mitochondrial
CC       transit peptide. {ECO:0000305|PubMed:10207110}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC       Name=1;
CC         IsoId=P49916-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P49916-2; Sequence=VSP_001302;
CC       Name=3; Synonyms=Alpha;
CC         IsoId=P49916-3; Sequence=VSP_057464;
CC       Name=4; Synonyms=Beta;
CC         IsoId=P49916-4; Sequence=VSP_057464, VSP_001302;
CC   -!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
CC   -!- DOMAIN: The PARP-type zinc finger is required for DNA ligase activity.
CC       {ECO:0000269|PubMed:20518483}.
CC   -!- DISEASE: Mitochondrial DNA depletion syndrome 20, MNGIE type (MTDPS20)
CC       [MIM:619780]: An autosomal recessive mitochondrial disorder
CC       characterized by severe gut dysmotility, muscle weakness and atrophy,
CC       neurological abnormalities including epilepsy, migraine, stroke-like
CC       episodes, learning difficulties or cognitive decline, and neurogenic
CC       bladder. Brain imaging usually shows diffuse leukoencephalopathy and
CC       may show cerebellar atrophy. Disease onset can range from infancy to
CC       the teenage years. {ECO:0000269|PubMed:33855352,
CC       ECO:0000269|PubMed:34165507}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing.
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation of
CC       isoform 1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation of
CC       isoform 2. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
CC       URL="https://en.wikipedia.org/wiki/DNA_ligase";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/mpg/";
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DR   EMBL; X84740; CAA59230.1; -; mRNA.
DR   EMBL; U40671; AAA85022.1; -; mRNA.
DR   EMBL; HQ204826; ADP89974.1; -; Genomic_DNA.
DR   EMBL; HQ204826; ADP89975.1; -; Genomic_DNA.
DR   EMBL; HQ204827; ADP89976.1; -; Genomic_DNA.
DR   EMBL; HQ204827; ADP89977.1; -; Genomic_DNA.
DR   EMBL; HQ204828; ADP89978.1; -; Genomic_DNA.
DR   EMBL; HQ204828; ADP89979.1; -; Genomic_DNA.
DR   EMBL; HQ204829; ADP89980.1; -; Genomic_DNA.
DR   EMBL; HQ204829; ADP89981.1; -; Genomic_DNA.
DR   EMBL; HQ204830; ADP89982.1; -; Genomic_DNA.
DR   EMBL; HQ204830; ADP89983.1; -; Genomic_DNA.
DR   EMBL; HQ204831; ADP89984.1; -; Genomic_DNA.
DR   EMBL; HQ204831; ADP89985.1; -; Genomic_DNA.
DR   EMBL; HQ204832; ADP89986.1; -; Genomic_DNA.
DR   EMBL; HQ204832; ADP89987.1; -; Genomic_DNA.
DR   EMBL; HQ204833; ADP89988.1; -; Genomic_DNA.
DR   EMBL; HQ204833; ADP89989.1; -; Genomic_DNA.
DR   EMBL; HQ204834; ADP89990.1; -; Genomic_DNA.
DR   EMBL; HQ204834; ADP89991.1; -; Genomic_DNA.
DR   EMBL; HQ204835; ADP89992.1; -; Genomic_DNA.
DR   EMBL; HQ204835; ADP89993.1; -; Genomic_DNA.
DR   EMBL; HQ204836; ADP89994.1; -; Genomic_DNA.
DR   EMBL; HQ204836; ADP89995.1; -; Genomic_DNA.
DR   EMBL; HQ204837; ADP89996.1; -; Genomic_DNA.
DR   EMBL; HQ204837; ADP89997.1; -; Genomic_DNA.
DR   EMBL; HQ204838; ADP89998.1; -; Genomic_DNA.
DR   EMBL; HQ204838; ADP89999.1; -; Genomic_DNA.
DR   EMBL; HQ204839; ADP90000.1; -; Genomic_DNA.
DR   EMBL; HQ204839; ADP90001.1; -; Genomic_DNA.
DR   EMBL; HQ204840; ADP90002.1; -; Genomic_DNA.
DR   EMBL; HQ204840; ADP90003.1; -; Genomic_DNA.
DR   EMBL; HQ204841; ADP90004.1; -; Genomic_DNA.
DR   EMBL; HQ204841; ADP90005.1; -; Genomic_DNA.
DR   EMBL; HQ204842; ADP90006.1; -; Genomic_DNA.
DR   EMBL; HQ204842; ADP90007.1; -; Genomic_DNA.
DR   EMBL; HQ204843; ADP90008.1; -; Genomic_DNA.
DR   EMBL; HQ204843; ADP90009.1; -; Genomic_DNA.
DR   EMBL; HQ204844; ADP90010.1; -; Genomic_DNA.
DR   EMBL; HQ204844; ADP90011.1; -; Genomic_DNA.
DR   EMBL; HQ204845; ADP90012.1; -; Genomic_DNA.
DR   EMBL; HQ204845; ADP90013.1; -; Genomic_DNA.
DR   EMBL; HQ204846; ADP90014.1; -; Genomic_DNA.
DR   EMBL; HQ204846; ADP90015.1; -; Genomic_DNA.
DR   EMBL; HQ204847; ADP90016.1; -; Genomic_DNA.
DR   EMBL; HQ204847; ADP90017.1; -; Genomic_DNA.
DR   EMBL; HQ204848; ADP90018.1; -; Genomic_DNA.
DR   EMBL; HQ204848; ADP90019.1; -; Genomic_DNA.
DR   EMBL; HQ204849; ADP90020.1; -; Genomic_DNA.
DR   EMBL; HQ204849; ADP90021.1; -; Genomic_DNA.
DR   EMBL; HQ204850; ADP90022.1; -; Genomic_DNA.
DR   EMBL; HQ204850; ADP90023.1; -; Genomic_DNA.
DR   EMBL; HQ204851; ADP90024.1; -; Genomic_DNA.
DR   EMBL; HQ204851; ADP90025.1; -; Genomic_DNA.
DR   EMBL; HQ204852; ADP90026.1; -; Genomic_DNA.
DR   EMBL; HQ204852; ADP90027.1; -; Genomic_DNA.
DR   EMBL; HQ204853; ADP90028.1; -; Genomic_DNA.
DR   EMBL; HQ204853; ADP90029.1; -; Genomic_DNA.
DR   EMBL; HQ204854; ADP90030.1; -; Genomic_DNA.
DR   EMBL; HQ204854; ADP90031.1; -; Genomic_DNA.
DR   EMBL; HQ204855; ADP90032.1; -; Genomic_DNA.
DR   EMBL; HQ204855; ADP90033.1; -; Genomic_DNA.
DR   EMBL; HQ204856; ADP90034.1; -; Genomic_DNA.
DR   EMBL; HQ204856; ADP90035.1; -; Genomic_DNA.
DR   EMBL; HQ204857; ADP90036.1; -; Genomic_DNA.
DR   EMBL; HQ204857; ADP90037.1; -; Genomic_DNA.
DR   EMBL; HQ204858; ADP90038.1; -; Genomic_DNA.
DR   EMBL; HQ204858; ADP90039.1; -; Genomic_DNA.
DR   EMBL; HQ204859; ADP90040.1; -; Genomic_DNA.
DR   EMBL; HQ204859; ADP90041.1; -; Genomic_DNA.
DR   EMBL; HQ204860; ADP90042.1; -; Genomic_DNA.
DR   EMBL; HQ204860; ADP90043.1; -; Genomic_DNA.
DR   EMBL; HQ204861; ADP90044.1; -; Genomic_DNA.
DR   EMBL; HQ204861; ADP90045.1; -; Genomic_DNA.
DR   EMBL; HQ204862; ADP90046.1; -; Genomic_DNA.
DR   EMBL; HQ204862; ADP90047.1; -; Genomic_DNA.
DR   EMBL; HQ204863; ADP90048.1; -; Genomic_DNA.
DR   EMBL; HQ204863; ADP90049.1; -; Genomic_DNA.
DR   EMBL; HQ204864; ADP90050.1; -; Genomic_DNA.
DR   EMBL; HQ204864; ADP90051.1; -; Genomic_DNA.
DR   EMBL; HQ204865; ADP90052.1; -; Genomic_DNA.
DR   EMBL; HQ204865; ADP90053.1; -; Genomic_DNA.
DR   EMBL; AF491645; AAL91592.1; -; Genomic_DNA.
DR   EMBL; AC004223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471147; EAW80197.1; -; Genomic_DNA.
DR   EMBL; CH471147; EAW80199.1; -; Genomic_DNA.
DR   EMBL; BC068005; AAH68005.1; -; mRNA.
DR   CCDS; CCDS11284.2; -. [P49916-1]
DR   CCDS; CCDS11285.2; -. [P49916-2]
DR   PIR; I37292; I37292.
DR   RefSeq; NP_002302.2; NM_002311.4. [P49916-2]
DR   RefSeq; NP_039269.2; NM_013975.3. [P49916-1]
DR   RefSeq; XP_016880113.1; XM_017024624.1. [P49916-1]
DR   PDB; 1IMO; NMR; -; A=924-1009.
DR   PDB; 1IN1; NMR; -; A=924-1009.
DR   PDB; 1UW0; NMR; -; A=88-204.
DR   PDB; 3L2P; X-ray; 3.00 A; A=257-833.
DR   PDB; 3PC7; X-ray; 1.65 A; A/B=924-1009.
DR   PDB; 3PC8; X-ray; 2.31 A; C/D=924-1008.
DR   PDB; 3QVG; X-ray; 2.26 A; A/C=924-1008.
DR   PDB; 6WH1; X-ray; 2.40 A; B=932-1008.
DR   PDBsum; 1IMO; -.
DR   PDBsum; 1IN1; -.
DR   PDBsum; 1UW0; -.
DR   PDBsum; 3L2P; -.
DR   PDBsum; 3PC7; -.
DR   PDBsum; 3PC8; -.
DR   PDBsum; 3QVG; -.
DR   PDBsum; 6WH1; -.
DR   AlphaFoldDB; P49916; -.
DR   BMRB; P49916; -.
DR   EMDB; EMD-21958; -.
DR   EMDB; EMD-22130; -.
DR   EMDB; EMD-22307; -.
DR   EMDB; EMD-23299; -.
DR   EMDB; EMD-23301; -.
DR   SASBDB; P49916; -.
DR   SMR; P49916; -.
DR   BioGRID; 110168; 212.
DR   ComplexPortal; CPX-793; XRCC1 DNA repair complex.
DR   CORUM; P49916; -.
DR   IntAct; P49916; 68.
DR   MINT; P49916; -.
DR   STRING; 9606.ENSP00000367787; -.
DR   BindingDB; P49916; -.
DR   ChEMBL; CHEMBL4295773; -.
DR   DrugBank; DB00290; Bleomycin.
DR   GlyGen; P49916; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; P49916; -.
DR   PhosphoSitePlus; P49916; -.
DR   SwissPalm; P49916; -.
DR   BioMuta; LIG3; -.
DR   DMDM; 251757259; -.
DR   EPD; P49916; -.
DR   jPOST; P49916; -.
DR   MassIVE; P49916; -.
DR   MaxQB; P49916; -.
DR   PaxDb; 9606-ENSP00000367787; -.
DR   PeptideAtlas; P49916; -.
DR   ProteomicsDB; 56181; -. [P49916-1]
DR   ProteomicsDB; 56182; -. [P49916-2]
DR   Pumba; P49916; -.
DR   Antibodypedia; 1860; 372 antibodies from 34 providers.
DR   CPTC; P49916; 1 antibody.
DR   DNASU; 3980; -.
DR   Ensembl; ENST00000262327.9; ENSP00000262327.4; ENSG00000005156.12. [P49916-2]
DR   Ensembl; ENST00000378526.9; ENSP00000367787.3; ENSG00000005156.12. [P49916-1]
DR   GeneID; 3980; -.
DR   KEGG; hsa:3980; -.
DR   MANE-Select; ENST00000378526.9; ENSP00000367787.3; NM_013975.4; NP_039269.2.
DR   UCSC; uc002hij.4; human. [P49916-1]
DR   AGR; HGNC:6600; -.
DR   CTD; 3980; -.
DR   DisGeNET; 3980; -.
DR   GeneCards; LIG3; -.
DR   HGNC; HGNC:6600; LIG3.
DR   HPA; ENSG00000005156; Low tissue specificity.
DR   MalaCards; LIG3; -.
DR   MIM; 600940; gene.
DR   MIM; 619780; phenotype.
DR   neXtProt; NX_P49916; -.
DR   OpenTargets; ENSG00000005156; -.
DR   Orphanet; 298; Mitochondrial neurogastrointestinal encephalomyopathy.
DR   PharmGKB; PA30374; -.
DR   VEuPathDB; HostDB:ENSG00000005156; -.
DR   eggNOG; KOG4437; Eukaryota.
DR   GeneTree; ENSGT00940000156492; -.
DR   HOGENOM; CLU_011787_0_0_1; -.
DR   InParanoid; P49916; -.
DR   OMA; YLFGGKM; -.
DR   OrthoDB; 162082at2759; -.
DR   PhylomeDB; P49916; -.
DR   TreeFam; TF316220; -.
DR   BRENDA; 6.5.1.1; 2681.
DR   PathwayCommons; P49916; -.
DR   Reactome; R-HSA-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR   Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR   Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
DR   Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   SignaLink; P49916; -.
DR   SIGNOR; P49916; -.
DR   BioGRID-ORCS; 3980; 105 hits in 1161 CRISPR screens.
DR   ChiTaRS; LIG3; human.
DR   EvolutionaryTrace; P49916; -.
DR   GeneWiki; LIG3; -.
DR   GenomeRNAi; 3980; -.
DR   Pharos; P49916; Tbio.
DR   PRO; PR:P49916; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P49916; Protein.
DR   Bgee; ENSG00000005156; Expressed in buccal mucosa cell and 184 other cell types or tissues.
DR   ExpressionAtlas; P49916; baseline and differential.
DR   GO; GO:0070421; C:DNA ligase III-XRCC1 complex; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:BHF-UCL.
DR   GO; GO:0003909; F:DNA ligase activity; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006288; P:base-excision repair, DNA ligation; IDA:BHF-UCL.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; TAS:Reactome.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:BHF-UCL.
DR   GO; GO:0006302; P:double-strand break repair; IDA:BHF-UCL.
DR   GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IGI:BHF-UCL.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:0043504; P:mitochondrial DNA repair; IMP:BHF-UCL.
DR   GO; GO:0007005; P:mitochondrion organization; IDA:BHF-UCL.
DR   GO; GO:0090298; P:negative regulation of mitochondrial DNA replication; IMP:CACAO.
DR   CDD; cd07902; Adenylation_DNA_ligase_III; 1.
DR   CDD; cd18431; BRCT_DNA_ligase_III; 1.
DR   CDD; cd07967; OBF_DNA_ligase_III; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR031916; LIG3_BRCT.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   Pfam; PF16759; LIG3_BRCT; 1.
DR   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR   PROSITE; PS00347; ZF_PARP_1; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
DR   Genevisible; P49916; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Alternative splicing; ATP-binding;
KW   Cell cycle; Cell division; Disease variant; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Primary mitochondrial disease; Reference proteome; Transit peptide; Zinc;
KW   Zinc-finger.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..1009
FT                   /note="DNA ligase 3"
FT                   /id="PRO_0000059574"
FT   DOMAIN          933..1009
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ZN_FING         93..185
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264,
FT                   ECO:0000269|PubMed:15288782"
FT   REGION          224..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..280
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   REGION          318..323
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   REGION          388..391
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   REGION          421..427
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   REGION          842..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..861
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..896
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        508
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10135,
FT                   ECO:0000269|PubMed:20518483"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         506
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT   BINDING         513
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         560
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         655
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         660
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305, ECO:0007744|PDB:3L2P"
FT   BINDING         671
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         675
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..87
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057464"
FT   VAR_SEQ         933..1009
FT                   /note="VLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMTSATHVLGSRDK
FT                   NPAAQQVSPEWIWACIRKRRLVAPC -> RRPASEQRGRTVPAGRR (in isoform
FT                   2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:7565692, ECO:0000305"
FT                   /id="VSP_001302"
FT   VARIANT         29..1009
FT                   /note="Missing (in MTDPS20)"
FT                   /evidence="ECO:0000269|PubMed:34165507"
FT                   /id="VAR_087020"
FT   VARIANT         224
FT                   /note="R -> W (in dbSNP:rs3744356)"
FT                   /id="VAR_020196"
FT   VARIANT         267..1009
FT                   /note="Missing (in MTDPS20)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087021"
FT   VARIANT         537
FT                   /note="K -> N (in MTDPS20; may affect exon 9 splicing;
FT                   decreased interaction with POLG; does not rescue cerebellar
FT                   defects in a LIG3 deficiency zebrafish model)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087022"
FT   VARIANT         609
FT                   /note="P -> L (in MTDPS20; severely decreased protein
FT                   levels)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087023"
FT   VARIANT         717
FT                   /note="D -> N (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs757797167)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036513"
FT   VARIANT         768
FT                   /note="Y -> H (in dbSNP:rs200981995)"
FT                   /evidence="ECO:0000269|PubMed:20843780"
FT                   /id="VAR_072387"
FT   VARIANT         811..1009
FT                   /note="Missing (in MTDPS20)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087024"
FT   VARIANT         867
FT                   /note="R -> H (in dbSNP:rs3136025)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_018807"
FT   VARIANT         898
FT                   /note="K -> T (in dbSNP:rs4986974)"
FT                   /id="VAR_021938"
FT   VARIANT         964
FT                   /note="G -> R (in MTDPS20; severely decreased protein
FT                   levels; does not rescue cerebellar defects in a LIG3
FT                   deficiency zebrafish model)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087025"
FT   VARIANT         986
FT                   /note="P -> S (in dbSNP:rs4986973)"
FT                   /id="VAR_020197"
FT   VARIANT         999
FT                   /note="C -> Y (in MTDPS20; severely decreased protein
FT                   levels)"
FT                   /evidence="ECO:0000269|PubMed:33855352"
FT                   /id="VAR_087026"
FT   MUTAGEN         410
FT                   /note="K->E: Nearly abolishes ligase activity with
FT                   blunt-ended DNA, but not with nicked DNA."
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   MUTAGEN         414
FT                   /note="R->E: Abolishes ligase activity with blunt-ended
FT                   DNA, but not with nicked DNA."
FT                   /evidence="ECO:0000269|PubMed:20518483"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   HELIX           140..149
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   TURN            166..168
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   HELIX           171..185
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   STRAND          188..190
FT                   /evidence="ECO:0007829|PDB:1UW0"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           263..274
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           279..291
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           303..310
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            312..314
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           323..334
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           338..344
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           350..359
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           374..385
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           390..401
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           407..416
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          421..423
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           426..431
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           437..443
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           447..459
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          485..488
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           492..498
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          503..507
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          511..519
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          522..526
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           535..537
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            538..540
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           541..543
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           545..548
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          553..564
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            566..568
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           574..577
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           579..584
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          590..600
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           610..620
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            625..627
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          628..630
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          633..636
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           639..651
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          657..663
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          671..676
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            678..680
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          688..698
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          710..716
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            718..720
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          721..729
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           735..740
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   TURN            741..743
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          780..787
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          789..791
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          795..797
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          800..804
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   STRAND          816..819
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           822..830
FT                   /evidence="ECO:0007829|PDB:3L2P"
FT   HELIX           924..927
FT                   /evidence="ECO:0007829|PDB:1IMO"
FT   TURN            930..932
FT                   /evidence="ECO:0007829|PDB:3QVG"
FT   STRAND          936..938
FT                   /evidence="ECO:0007829|PDB:1IMO"
FT   STRAND          942..944
FT                   /evidence="ECO:0007829|PDB:3QVG"
FT   HELIX           952..961
FT                   /evidence="ECO:0007829|PDB:3PC7"
FT   HELIX           969..974
FT                   /evidence="ECO:0007829|PDB:3PC7"
FT   STRAND          976..980
FT                   /evidence="ECO:0007829|PDB:3PC7"
FT   STRAND          982..984
FT                   /evidence="ECO:0007829|PDB:3QVG"
FT   STRAND          988..991
FT                   /evidence="ECO:0007829|PDB:3PC7"
FT   HELIX           993..1002
FT                   /evidence="ECO:0007829|PDB:3PC7"
SQ   SEQUENCE   1009 AA;  112907 MW;  0E4057E33C3F19A6 CRC64;
     MSLAFKIFFP QTLRALSRKE LCLFRKHHWR DVRQFSQWSE TDLLHGHPLF LRRKPVLSFQ
     GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR GTAGCKKCKE KIVKGVCRIG
     KVVPNPFSES GGDMKEWYHI KCMFEKLERA RATTKKIEDL TELEGWEELE DNEKEQITQH
     IADLSSKAAG TPKKKAVVQA KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAP
     SSPTPKRSLS SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH
     GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV SETIRVFFEQ
     SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI ASRCTANDLK CIIRLIKHDL
     KMNSGAKHVL DALDPNAYEA FKASRNLQDV VERVLHNAQE VEKEPGQRRA LSVQASLMTP
     VQPMLAEACK SVEYAMKKCP NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH
     FKDYIPQAFP GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF
     NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI QEGLEGLVLK
     DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG QGSKGGMMSI FLMGCYDPGS
     QKWCTVTKCA GGHDDATLAR LQNELDMVKI SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA
     VWEITGAEFS KSEAHTADGI SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV
     VAGDEGSSTT GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS
     AMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP DFSRLRRYFV
     AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI RKRRLVAPC
//