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Database: UniProt
Entry: P49916
LinkDB: P49916
Original site: P49916 
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   25-OCT-2017, entry version 192.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E.,
RA   Haseltine W.A., 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.,
RA   Walter C.A., Schultz R.A., Besterman J.M., Husain I.;
RT   "Mammalian DNA ligase III: molecular cloning, chromosomal
RT   localization, and expression in spermatocytes undergoing meiotic
RT   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.,
RA   Mindrinos M., 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION
RP   BY 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
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION
RP   BY 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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
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.,
RA   Buerckstuemmer T., 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-216; SER-242
RP   AND SER-913, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [18]
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
RT   against oxidative stress and improves mitochondrial DNA base excision
RT   repair.";
RL   DNA Repair 16:44-53(2014).
RN   [19]
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
RT   BRCT domain of human DNA ligase IIIalpha.";
RL   Protein Expr. Purif. 21:401-411(2001).
RN   [20]
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   [21]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 257-833 IN COMPLEX WITH DNA
RP   AND AMP, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND
RP   MUTAGENESIS OF 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
RT   two DNA-bound states.";
RL   Biochemistry 49:6165-6176(2010).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 924-1009 IN COMPLEX WITH
RP   XRCC1, 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-?
RT   BRCT-mediated dimer complexes.";
RL   Nucleic Acids Res. 39:7816-7827(2011).
RN   [23]
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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Isoform 3 functions as heterodimer with DNA-repair
CC       protein XRCC1 in the nucleus and can correct defective DNA strand-
CC       break repair and sister chromatid exchange following treatment
CC       with ionizing radiation and alkylating agents. Isoform 1 is
CC       targeted to mitochondria, where it functions as DNA ligase in
CC       mitochondrial base-excision DNA repair (PubMed:10207110,
CC       PubMed:24674627). {ECO:0000269|PubMed:10207110,
CC       ECO:0000269|PubMed:24674627}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135,
CC       ECO:0000269|PubMed:10207110, 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
CC       DNA-repair protein XRCC1. {ECO:0000269|PubMed:21652643,
CC       ECO:0000269|PubMed:7760816}.
CC   -!- INTERACTION:
CC       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
CC       mitochondrial transit peptide. {ECO:0000269|PubMed:10207110}.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Nucleus
CC       {ECO:0000305|PubMed:10207110}. Note=Lacks the N-terminal
CC       mitochondrial 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         Note=Produced by alternative splicing.;
CC       Name=2;
CC         IsoId=P49916-2; Sequence=VSP_001302;
CC         Note=Produced by alternative splicing.;
CC       Name=3; Synonyms=Alpha;
CC         IsoId=P49916-3; Sequence=VSP_057464;
CC         Note=Produced by alternative initiation of isoform 1.;
CC       Name=4; Synonyms=Beta;
CC         IsoId=P49916-4; Sequence=VSP_057464, VSP_001302;
CC         Note=Produced by alternative initiation of isoform 2.;
CC   -!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
CC   -!- DOMAIN: The PARP-type zinc finger is required for DNA ligase
CC       activity. {ECO:0000269|PubMed:20518483}.
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/";
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   UniGene; Hs.100299; -.
DR   UniGene; Hs.556108; -.
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   PDBsum; 1IMO; -.
DR   PDBsum; 1IN1; -.
DR   PDBsum; 1UW0; -.
DR   PDBsum; 3L2P; -.
DR   PDBsum; 3PC7; -.
DR   PDBsum; 3PC8; -.
DR   PDBsum; 3QVG; -.
DR   ProteinModelPortal; P49916; -.
DR   SMR; P49916; -.
DR   BioGrid; 110168; 65.
DR   CORUM; P49916; -.
DR   IntAct; P49916; 30.
DR   MINT; MINT-4531178; -.
DR   STRING; 9606.ENSP00000367787; -.
DR   DrugBank; DB00290; Bleomycin.
DR   iPTMnet; P49916; -.
DR   PhosphoSitePlus; P49916; -.
DR   BioMuta; LIG3; -.
DR   DMDM; 251757259; -.
DR   EPD; P49916; -.
DR   MaxQB; P49916; -.
DR   PaxDb; P49916; -.
DR   PeptideAtlas; P49916; -.
DR   PRIDE; P49916; -.
DR   DNASU; 3980; -.
DR   Ensembl; ENST00000262327; ENSP00000262327; ENSG00000005156. [P49916-2]
DR   Ensembl; ENST00000378526; ENSP00000367787; ENSG00000005156. [P49916-1]
DR   GeneID; 3980; -.
DR   KEGG; hsa:3980; -.
DR   UCSC; uc002hij.4; human. [P49916-1]
DR   CTD; 3980; -.
DR   DisGeNET; 3980; -.
DR   EuPathDB; HostDB:ENSG00000005156.11; -.
DR   GeneCards; LIG3; -.
DR   HGNC; HGNC:6600; LIG3.
DR   HPA; HPA006723; -.
DR   MIM; 600940; gene.
DR   neXtProt; NX_P49916; -.
DR   OpenTargets; ENSG00000005156; -.
DR   PharmGKB; PA30374; -.
DR   eggNOG; KOG4437; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133792; -.
DR   HOGENOM; HOG000007653; -.
DR   HOVERGEN; HBG005515; -.
DR   InParanoid; P49916; -.
DR   KO; K10776; -.
DR   OMA; VFDCIYF; -.
DR   OrthoDB; EOG091G0XBU; -.
DR   PhylomeDB; P49916; -.
DR   TreeFam; TF316220; -.
DR   BRENDA; 6.5.1.1; 2681.
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   SIGNOR; P49916; -.
DR   ChiTaRS; LIG3; human.
DR   EvolutionaryTrace; P49916; -.
DR   GeneWiki; LIG3; -.
DR   GenomeRNAi; 3980; -.
DR   PRO; PR:P49916; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000005156; -.
DR   CleanEx; HS_LIG3; -.
DR   ExpressionAtlas; P49916; baseline and differential.
DR   Genevisible; P49916; HS.
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: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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: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   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.30.1740.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 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   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; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 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; PARP_ZN_FINGER_1; 1.
DR   PROSITE; PS50064; PARP_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transit peptide;
KW   Zinc; Zinc-finger.
FT   TRANSIT       1     42       Mitochondrion. {ECO:0000255}.
FT   CHAIN        43   1009       DNA ligase 3.
FT                                /FTId=PRO_0000059574.
FT   DOMAIN      933   1009       BRCT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ZN_FING      93    185       PARP-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00264,
FT                                ECO:0000269|PubMed:15288782}.
FT   REGION      277    280       Interaction with DNA.
FT                                {ECO:0000269|PubMed:20518483}.
FT   REGION      318    323       Interaction with DNA.
FT                                {ECO:0000269|PubMed:20518483}.
FT   REGION      388    391       Interaction with DNA.
FT                                {ECO:0000269|PubMed:20518483}.
FT   REGION      421    427       Interaction with DNA.
FT                                {ECO:0000269|PubMed:20518483}.
FT   ACT_SITE    508    508       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135,
FT                                ECO:0000269|PubMed:20518483}.
FT   METAL       560    560       Magnesium 1. {ECO:0000250}.
FT   METAL       655    655       Magnesium 2. {ECO:0000250}.
FT   BINDING     506    506       ATP. {ECO:0000244|PDB:3L2P, ECO:0000305}.
FT   BINDING     513    513       ATP. {ECO:0000244|PDB:3L2P, ECO:0000305}.
FT   BINDING     528    528       ATP. {ECO:0000250}.
FT   BINDING     660    660       ATP. {ECO:0000244|PDB:3L2P, ECO:0000305}.
FT   BINDING     671    671       ATP. {ECO:0000250}.
FT   BINDING     675    675       ATP. {ECO:0000250}.
FT   MOD_RES     210    210       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     216    216       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     227    227       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     242    242       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     913    913       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ       1     87       Missing (in isoform 3 and isoform 4).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_057464.
FT   VAR_SEQ     933   1009       VLLDIFTGVRLYLPPSTPDFSRLRRYFVAFDGDLVQEFDMT
FT                                SATHVLGSRDKNPAAQQVSPEWIWACIRKRRLVAPC -> R
FT                                RPASEQRGRTVPAGRR (in isoform 2 and
FT                                isoform 4). {ECO:0000303|PubMed:7565692,
FT                                ECO:0000305}.
FT                                /FTId=VSP_001302.
FT   VARIANT     224    224       R -> W (in dbSNP:rs3744356).
FT                                /FTId=VAR_020196.
FT   VARIANT     717    717       D -> N (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs757797167).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036513.
FT   VARIANT     768    768       Y -> H (in dbSNP:rs200981995).
FT                                {ECO:0000269|PubMed:20843780}.
FT                                /FTId=VAR_072387.
FT   VARIANT     867    867       R -> H (in dbSNP:rs3136025).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_018807.
FT   VARIANT     898    898       K -> T (in dbSNP:rs4986974).
FT                                /FTId=VAR_021938.
FT   VARIANT     986    986       P -> S (in dbSNP:rs4986973).
FT                                /FTId=VAR_020197.
FT   MUTAGEN     410    410       K->E: Nearly abolishes ligase activity
FT                                with blunt-ended DNA, but not with nicked
FT                                DNA. {ECO:0000269|PubMed:20518483}.
FT   MUTAGEN     414    414       R->E: Abolishes ligase activity with
FT                                blunt-ended DNA, but not with nicked DNA.
FT                                {ECO:0000269|PubMed:20518483}.
FT   STRAND       92     97       {ECO:0000244|PDB:1UW0}.
FT   STRAND      117    124       {ECO:0000244|PDB:1UW0}.
FT   HELIX       140    149       {ECO:0000244|PDB:1UW0}.
FT   STRAND      152    154       {ECO:0000244|PDB:1UW0}.
FT   STRAND      161    165       {ECO:0000244|PDB:1UW0}.
FT   TURN        166    168       {ECO:0000244|PDB:1UW0}.
FT   HELIX       171    185       {ECO:0000244|PDB:1UW0}.
FT   STRAND      188    190       {ECO:0000244|PDB:1UW0}.
FT   HELIX       259    261       {ECO:0000244|PDB:3L2P}.
FT   HELIX       263    274       {ECO:0000244|PDB:3L2P}.
FT   HELIX       279    291       {ECO:0000244|PDB:3L2P}.
FT   HELIX       303    310       {ECO:0000244|PDB:3L2P}.
FT   TURN        312    314       {ECO:0000244|PDB:3L2P}.
FT   HELIX       323    334       {ECO:0000244|PDB:3L2P}.
FT   HELIX       338    344       {ECO:0000244|PDB:3L2P}.
FT   HELIX       345    347       {ECO:0000244|PDB:3L2P}.
FT   HELIX       350    359       {ECO:0000244|PDB:3L2P}.
FT   STRAND      362    364       {ECO:0000244|PDB:3L2P}.
FT   HELIX       374    385       {ECO:0000244|PDB:3L2P}.
FT   HELIX       390    401       {ECO:0000244|PDB:3L2P}.
FT   HELIX       407    416       {ECO:0000244|PDB:3L2P}.
FT   STRAND      421    423       {ECO:0000244|PDB:3L2P}.
FT   HELIX       426    431       {ECO:0000244|PDB:3L2P}.
FT   HELIX       437    443       {ECO:0000244|PDB:3L2P}.
FT   HELIX       447    459       {ECO:0000244|PDB:3L2P}.
FT   STRAND      485    488       {ECO:0000244|PDB:3L2P}.
FT   HELIX       492    498       {ECO:0000244|PDB:3L2P}.
FT   STRAND      503    507       {ECO:0000244|PDB:3L2P}.
FT   STRAND      511    519       {ECO:0000244|PDB:3L2P}.
FT   STRAND      522    526       {ECO:0000244|PDB:3L2P}.
FT   HELIX       535    537       {ECO:0000244|PDB:3L2P}.
FT   TURN        538    540       {ECO:0000244|PDB:3L2P}.
FT   HELIX       541    543       {ECO:0000244|PDB:3L2P}.
FT   HELIX       545    548       {ECO:0000244|PDB:3L2P}.
FT   STRAND      553    564       {ECO:0000244|PDB:3L2P}.
FT   TURN        566    568       {ECO:0000244|PDB:3L2P}.
FT   HELIX       574    577       {ECO:0000244|PDB:3L2P}.
FT   HELIX       579    584       {ECO:0000244|PDB:3L2P}.
FT   STRAND      590    600       {ECO:0000244|PDB:3L2P}.
FT   HELIX       610    620       {ECO:0000244|PDB:3L2P}.
FT   TURN        625    627       {ECO:0000244|PDB:3L2P}.
FT   STRAND      628    630       {ECO:0000244|PDB:3L2P}.
FT   STRAND      633    636       {ECO:0000244|PDB:3L2P}.
FT   HELIX       639    651       {ECO:0000244|PDB:3L2P}.
FT   STRAND      657    663       {ECO:0000244|PDB:3L2P}.
FT   STRAND      671    676       {ECO:0000244|PDB:3L2P}.
FT   TURN        678    680       {ECO:0000244|PDB:3L2P}.
FT   STRAND      688    698       {ECO:0000244|PDB:3L2P}.
FT   STRAND      710    716       {ECO:0000244|PDB:3L2P}.
FT   TURN        718    720       {ECO:0000244|PDB:3L2P}.
FT   STRAND      721    729       {ECO:0000244|PDB:3L2P}.
FT   HELIX       735    740       {ECO:0000244|PDB:3L2P}.
FT   TURN        741    743       {ECO:0000244|PDB:3L2P}.
FT   STRAND      780    787       {ECO:0000244|PDB:3L2P}.
FT   STRAND      789    791       {ECO:0000244|PDB:3L2P}.
FT   STRAND      795    797       {ECO:0000244|PDB:3L2P}.
FT   STRAND      800    804       {ECO:0000244|PDB:3L2P}.
FT   STRAND      816    819       {ECO:0000244|PDB:3L2P}.
FT   HELIX       822    830       {ECO:0000244|PDB:3L2P}.
FT   HELIX       924    927       {ECO:0000244|PDB:1IMO}.
FT   TURN        930    932       {ECO:0000244|PDB:3QVG}.
FT   STRAND      936    938       {ECO:0000244|PDB:1IMO}.
FT   STRAND      942    944       {ECO:0000244|PDB:3QVG}.
FT   HELIX       952    961       {ECO:0000244|PDB:3PC7}.
FT   HELIX       969    974       {ECO:0000244|PDB:3PC7}.
FT   STRAND      976    980       {ECO:0000244|PDB:3PC7}.
FT   STRAND      982    984       {ECO:0000244|PDB:3QVG}.
FT   STRAND      988    991       {ECO:0000244|PDB:3PC7}.
FT   HELIX       993   1002       {ECO:0000244|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
//
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