GenomeNet

Database: UniProt
Entry: P18858
LinkDB: P18858
Original site: P18858 
ID   DNLI1_HUMAN             Reviewed;         919 AA.
AC   P18858; B2RAI8; B4DTU4; Q2TB12; Q32P23;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   28-MAR-2018, entry version 194.
DE   RecName: Full=DNA ligase 1;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase I;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1;
GN   Name=LIG1;
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 1).
RC   TISSUE=T lymphoblast;
RX   PubMed=2204063; DOI=10.1073/pnas.87.17.6679;
RA   Barnes D.E., Johnston L.H., Kodama K., Tomkinson A.E., Lasko D.D.,
RA   Lindahl T.;
RT   "Human DNA ligase I cDNA: cloning and functional expression in
RT   Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6679-6683(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-24; TRP-62;
RP   GLU-249; SER-267; MET-349; ILE-369; VAL-480; ILE-614 AND LEU-677.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Placenta, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 716-753 (ISOFORM 1).
RX   PubMed=1881902; DOI=10.1073/pnas.88.17.7615;
RA   Petrini J.H.J., Huwiler K.G., Weaver D.T.;
RT   "A wild-type DNA ligase I gene is expressed in Bloom's syndrome
RT   cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7615-7619(1991).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-76 AND SER-141,
RP   AND 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76;
RP   THR-195 AND THR-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-76, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA   Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate
RT   reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT   Wnt signal transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-141; THR-195;
RP   SER-201; THR-233; SER-911 AND SER-913, AND IDENTIFICATION BY MASS
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66;
RP   SER-141; THR-195; SER-201; SER-911 AND SER-913, 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-49; SER-51;
RP   SER-66; SER-76; SER-141; THR-195; SER-201 AND SER-911, AND
RP   IDENTIFICATION 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-51; SER-66; SER-76;
RP   SER-141 AND THR-195, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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-47; SER-51; SER-66;
RP   SER-76; SER-141; THR-195; SER-199; SER-201; THR-207; SER-229; SER-230;
RP   THR-798; SER-801 AND SER-819, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [18]
RP   INTERACTION WITH PCNA.
RX   PubMed=24911150; DOI=10.1172/JCI74593;
RA   Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y.,
RA   Chioza B.A., Harlalka G.V., Mansour S., Sreekantan-Nair A.,
RA   Patton M.A., Muggenthaler M., Rich P., Wagner K., Coblentz R.,
RA   Stein C.K., Last J.I., Taylor A.M., Jackson A.P., Ogi T.,
RA   Lehmann A.R., Green C.M., Crosby A.H.;
RT   "Hypomorphic PCNA mutation underlies a human DNA repair disorder.";
RL   J. Clin. Invest. 124:3137-3146(2014).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-919 IN COMPLEX WITH
RP   NICKED DNA AND AMP, COFACTOR, AND ACTIVE SITE.
RX   PubMed=15565146; DOI=10.1038/nature03082;
RA   Pascal J.M., O'Brien P.J., Tomkinson A.E., Ellenberger T.;
RT   "Human DNA ligase I completely encircles and partially unwinds nicked
RT   DNA.";
RL   Nature 432:473-478(2004).
RN   [20]
RP   VARIANTS LYS-566 AND TRP-771.
RX   PubMed=1581963; DOI=10.1016/0092-8674(92)90450-Q;
RA   Barnes D.E., Tomkinson A.E., Lehmann A.R., Webster A.D.B., Lindahl T.;
RT   "Mutations in the DNA ligase I gene of an individual with
RT   immunodeficiencies and cellular hypersensitivity to DNA-damaging
RT   agents.";
RL   Cell 69:495-503(1992).
RN   [21]
RP   VARIANTS [LARGE SCALE ANALYSIS] GLU-152 AND LEU-612.
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: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15565146};
CC   -!- SUBUNIT: Interacts with PCNA. {ECO:0000269|PubMed:24911150}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P18858-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P18858-2; Sequence=VSP_056139, VSP_056140;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P18858-3; Sequence=VSP_057320, VSP_057321;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=LIG1base; Note=LIG1 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/LIG1base/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/lig1/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
CC       URL="https://en.wikipedia.org/wiki/DNA_ligase";
DR   EMBL; M36067; AAA59518.1; -; mRNA.
DR   EMBL; AF527418; AAM77697.1; -; Genomic_DNA.
DR   EMBL; AK300370; BAG62106.1; -; mRNA.
DR   EMBL; AK314210; BAG36885.1; -; mRNA.
DR   EMBL; AC011466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KC877741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52316.1; -; Genomic_DNA.
DR   EMBL; BC108318; AAI08319.1; -; mRNA.
DR   EMBL; BC110622; AAI10623.1; -; mRNA.
DR   CCDS; CCDS12711.1; -. [P18858-1]
DR   CCDS; CCDS74409.1; -. [P18858-3]
DR   PIR; A36048; A41275.
DR   RefSeq; NP_000225.1; NM_000234.2. [P18858-1]
DR   RefSeq; NP_001275992.1; NM_001289063.1. [P18858-3]
DR   RefSeq; NP_001275993.1; NM_001289064.1.
DR   RefSeq; NP_001307899.1; NM_001320970.1.
DR   RefSeq; NP_001307900.1; NM_001320971.1.
DR   UniGene; Hs.1770; -.
DR   PDB; 1X9N; X-ray; 3.00 A; A=233-919.
DR   PDBsum; 1X9N; -.
DR   ProteinModelPortal; P18858; -.
DR   SMR; P18858; -.
DR   BioGrid; 110166; 16.
DR   CORUM; P18858; -.
DR   DIP; DIP-24215N; -.
DR   ELM; P18858; -.
DR   IntAct; P18858; 7.
DR   MINT; P18858; -.
DR   STRING; 9606.ENSP00000263274; -.
DR   BindingDB; P18858; -.
DR   ChEMBL; CHEMBL5694; -.
DR   DrugBank; DB00290; Bleomycin.
DR   iPTMnet; P18858; -.
DR   PhosphoSitePlus; P18858; -.
DR   BioMuta; LIG1; -.
DR   DMDM; 118773; -.
DR   EPD; P18858; -.
DR   MaxQB; P18858; -.
DR   PaxDb; P18858; -.
DR   PeptideAtlas; P18858; -.
DR   PRIDE; P18858; -.
DR   Ensembl; ENST00000263274; ENSP00000263274; ENSG00000105486. [P18858-1]
DR   Ensembl; ENST00000427526; ENSP00000442841; ENSG00000105486. [P18858-3]
DR   Ensembl; ENST00000601091; ENSP00000471836; ENSG00000105486. [P18858-2]
DR   Ensembl; ENST00000613670; ENSP00000483027; ENSG00000105486. [P18858-2]
DR   GeneID; 3978; -.
DR   KEGG; hsa:3978; -.
DR   UCSC; uc002pia.2; human. [P18858-1]
DR   CTD; 3978; -.
DR   DisGeNET; 3978; -.
DR   EuPathDB; HostDB:ENSG00000105486.13; -.
DR   GeneCards; LIG1; -.
DR   HGNC; HGNC:6598; LIG1.
DR   HPA; CAB037015; -.
DR   HPA; HPA041431; -.
DR   HPA; HPA048071; -.
DR   MIM; 126391; gene.
DR   neXtProt; NX_P18858; -.
DR   OpenTargets; ENSG00000105486; -.
DR   PharmGKB; PA30372; -.
DR   eggNOG; KOG0967; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133792; -.
DR   HOGENOM; HOG000036006; -.
DR   HOVERGEN; HBG005514; -.
DR   InParanoid; P18858; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; EOG091G06OS; -.
DR   PhylomeDB; P18858; -.
DR   TreeFam; TF300342; -.
DR   BRENDA; 6.5.1.1; 2681.
DR   Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
DR   Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere.
DR   Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR   Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair.
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   Reactome; R-HSA-69183; Processive synthesis on the lagging strand.
DR   SIGNOR; P18858; -.
DR   ChiTaRS; LIG1; human.
DR   EvolutionaryTrace; P18858; -.
DR   GeneWiki; LIG1; -.
DR   GenomeRNAi; 3978; -.
DR   PRO; PR:P18858; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000105486; -.
DR   CleanEx; HS_LIG1; -.
DR   ExpressionAtlas; P18858; baseline and differential.
DR   Genevisible; P18858; HS.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0003909; F:DNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0006284; P:base-excision repair; IDA:BHF-UCL.
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; TAS:Reactome.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR   GO; GO:0006298; P:mismatch repair; TAS:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   Gene3D; 1.10.3260.10; -; 1.
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; IPR012340; NA-bd_OB-fold.
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   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome.
FT   CHAIN         1    919       DNA ligase 1.
FT                                /FTId=PRO_0000059570.
FT   REGION      449    458       Interaction with target DNA.
FT   REGION      642    644       Interaction with target DNA.
FT   ACT_SITE    568    568       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       621    621       Magnesium 1. {ECO:0000305}.
FT   METAL       720    720       Magnesium 2. {ECO:0000305}.
FT   BINDING     566    566       ATP. {ECO:0000244|PDB:1X9N,
FT                                ECO:0000269|PubMed:15565146}.
FT   BINDING     573    573       ATP. {ECO:0000244|PDB:1X9N,
FT                                ECO:0000269|PubMed:15565146}.
FT   BINDING     589    589       ATP.
FT   BINDING     725    725       ATP. {ECO:0000244|PDB:1X9N,
FT                                ECO:0000269|PubMed:15565146}.
FT   BINDING     738    738       ATP. {ECO:0000250}.
FT   BINDING     744    744       ATP. {ECO:0000244|PDB:1X9N,
FT                                ECO:0000269|PubMed:15565146}.
FT   SITE        305    305       Interaction with target DNA.
FT   SITE        590    590       Interaction with target DNA.
FT   SITE        770    770       Interaction with target DNA.
FT   SITE        795    795       Interaction with target DNA.
FT   MOD_RES      47     47       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      49     49       Phosphoserine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES      51     51       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      66     66       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:17693683,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      76     76       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:17693683,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     141    141       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     195    195       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     199    199       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     201    201       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     207    207       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     226    226       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P37913}.
FT   MOD_RES     229    229       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     230    230       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     233    233       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648}.
FT   MOD_RES     798    798       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     801    801       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     819    819       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     911    911       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     913    913       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332}.
FT   VAR_SEQ       7     36       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057320.
FT   VAR_SEQ     153    153       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057321.
FT   VAR_SEQ     796    801       LGTGFS -> VLGNWG (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056139.
FT   VAR_SEQ     802    919       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_056140.
FT   VARIANT      24     24       A -> V (in dbSNP:rs3730855).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018802.
FT   VARIANT      52     52       P -> L (in dbSNP:rs4987181).
FT                                /FTId=VAR_020194.
FT   VARIANT      62     62       R -> W (in dbSNP:rs3730863).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018803.
FT   VARIANT      72     72       D -> G (in dbSNP:rs4987070).
FT                                /FTId=VAR_020195.
FT   VARIANT     152    152       K -> E (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs780748107).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036511.
FT   VARIANT     249    249       G -> E (in dbSNP:rs3730911).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016766.
FT   VARIANT     267    267       N -> S (in dbSNP:rs3730933).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016767.
FT   VARIANT     349    349       V -> M (in dbSNP:rs3730947).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018804.
FT   VARIANT     369    369       V -> I (in dbSNP:rs3730966).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018805.
FT   VARIANT     409    409       R -> H (in dbSNP:rs4987068).
FT                                /FTId=VAR_016768.
FT   VARIANT     480    480       M -> V (in dbSNP:rs3730980).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016769.
FT   VARIANT     566    566       E -> K (found in a patient with a
FT                                syndrome of immunodeficiency and
FT                                increased cellular sensitivity to DNA-
FT                                damaging agents due to LIG1 deficiency;
FT                                compound heterozygote carrying W-771;
FT                                dbSNP:rs121434560).
FT                                {ECO:0000269|PubMed:1581963}.
FT                                /FTId=VAR_002262.
FT   VARIANT     612    612       S -> L (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs780324684).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036512.
FT   VARIANT     614    614       T -> I (in dbSNP:rs3731003).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016770.
FT   VARIANT     677    677       R -> L (in dbSNP:rs3731008).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018806.
FT   VARIANT     771    771       R -> W (found in a patient with a
FT                                syndrome of immunodeficiency and
FT                                increased cellular sensitivity to DNA-
FT                                damaging agents due to LIG1 deficiency;
FT                                compound heterozygote carrying K-566;
FT                                dbSNP:rs121434561).
FT                                {ECO:0000269|PubMed:1581963}.
FT                                /FTId=VAR_002263.
FT   HELIX       263    265       {ECO:0000244|PDB:1X9N}.
FT   HELIX       275    278       {ECO:0000244|PDB:1X9N}.
FT   HELIX       289    300       {ECO:0000244|PDB:1X9N}.
FT   HELIX       305    322       {ECO:0000244|PDB:1X9N}.
FT   HELIX       324    326       {ECO:0000244|PDB:1X9N}.
FT   HELIX       327    335       {ECO:0000244|PDB:1X9N}.
FT   HELIX       341    343       {ECO:0000244|PDB:1X9N}.
FT   HELIX       351    362       {ECO:0000244|PDB:1X9N}.
FT   HELIX       366    376       {ECO:0000244|PDB:1X9N}.
FT   HELIX       379    382       {ECO:0000244|PDB:1X9N}.
FT   HELIX       401    413       {ECO:0000244|PDB:1X9N}.
FT   HELIX       419    433       {ECO:0000244|PDB:1X9N}.
FT   HELIX       438    446       {ECO:0000244|PDB:1X9N}.
FT   HELIX       456    469       {ECO:0000244|PDB:1X9N}.
FT   TURN        483    486       {ECO:0000244|PDB:1X9N}.
FT   HELIX       489    509       {ECO:0000244|PDB:1X9N}.
FT   HELIX       513    527       {ECO:0000244|PDB:1X9N}.
FT   HELIX       529    531       {ECO:0000244|PDB:1X9N}.
FT   STRAND      544    550       {ECO:0000244|PDB:1X9N}.
FT   HELIX       551    557       {ECO:0000244|PDB:1X9N}.
FT   TURN        558    560       {ECO:0000244|PDB:1X9N}.
FT   STRAND      563    578       {ECO:0000244|PDB:1X9N}.
FT   STRAND      584    587       {ECO:0000244|PDB:1X9N}.
FT   TURN        595    597       {ECO:0000244|PDB:1X9N}.
FT   HELIX       599    603       {ECO:0000244|PDB:1X9N}.
FT   HELIX       606    608       {ECO:0000244|PDB:1X9N}.
FT   STRAND      616    625       {ECO:0000244|PDB:1X9N}.
FT   TURN        627    629       {ECO:0000244|PDB:1X9N}.
FT   HELIX       635    638       {ECO:0000244|PDB:1X9N}.
FT   HELIX       648    650       {ECO:0000244|PDB:1X9N}.
FT   STRAND      653    665       {ECO:0000244|PDB:1X9N}.
FT   HELIX       675    685       {ECO:0000244|PDB:1X9N}.
FT   TURN        690    692       {ECO:0000244|PDB:1X9N}.
FT   STRAND      693    695       {ECO:0000244|PDB:1X9N}.
FT   HELIX       704    716       {ECO:0000244|PDB:1X9N}.
FT   STRAND      718    730       {ECO:0000244|PDB:1X9N}.
FT   TURN        735    737       {ECO:0000244|PDB:1X9N}.
FT   STRAND      739    746       {ECO:0000244|PDB:1X9N}.
FT   HELIX       747    751       {ECO:0000244|PDB:1X9N}.
FT   STRAND      755    767       {ECO:0000244|PDB:1X9N}.
FT   STRAND      774    784       {ECO:0000244|PDB:1X9N}.
FT   TURN        785    788       {ECO:0000244|PDB:1X9N}.
FT   STRAND      789    796       {ECO:0000244|PDB:1X9N}.
FT   HELIX       802    814       {ECO:0000244|PDB:1X9N}.
FT   STRAND      816    819       {ECO:0000244|PDB:1X9N}.
FT   STRAND      827    829       {ECO:0000244|PDB:1X9N}.
FT   STRAND      833    836       {ECO:0000244|PDB:1X9N}.
FT   STRAND      841    854       {ECO:0000244|PDB:1X9N}.
FT   TURN        857    861       {ECO:0000244|PDB:1X9N}.
FT   STRAND      867    872       {ECO:0000244|PDB:1X9N}.
FT   STRAND      874    878       {ECO:0000244|PDB:1X9N}.
FT   HELIX       884    886       {ECO:0000244|PDB:1X9N}.
FT   HELIX       890    900       {ECO:0000244|PDB:1X9N}.
SQ   SEQUENCE   919 AA;  101736 MW;  B2854DAE38A8D4AD CRC64;
     MQRSIMSFFH PKKEGKAKKP EKEASNSSRE TEPPPKAALK EWNGVVSESD SPVKRPGRKA
     ARVLGSEGEE EDEALSPAKG QKPALDCSQV SPPRPATSPE NNASLSDTSP MDSSPSGIPK
     RRTARKQLPK RTIQEVLEEQ SEDEDREAKR KKEEEEEETP KESLTEAEVA TEKEGEDGDQ
     PTTPPKPLKT SKAETPTESV SEPEVATKQE LQEEEEQTKP PRRAPKTLSS FFTPRKPAVK
     KEVKEEEPGA PGKEGAAEGP LDPSGYNPAK NNYHPVEDAC WKPGQKVPYL AVARTFEKIE
     EVSARLRMVE TLSNLLRSVV ALSPPDLLPV LYLSLNHLGP PQQGLELGVG DGVLLKAVAQ
     ATGRQLESVR AEAAEKGDVG LVAENSRSTQ RLMLPPPPLT ASGVFSKFRD IARLTGSAST
     AKKIDIIKGL FVACRHSEAR FIARSLSGRL RLGLAEQSVL AALSQAVSLT PPGQEFPPAM
     VDAGKGKTAE ARKTWLEEQG MILKQTFCEV PDLDRIIPVL LEHGLERLPE HCKLSPGIPL
     KPMLAHPTRG ISEVLKRFEE AAFTCEYKYD GQRAQIHALE GGEVKIFSRN QEDNTGKYPD
     IISRIPKIKL PSVTSFILDT EAVAWDREKK QIQPFQVLTT RKRKEVDASE IQVQVCLYAF
     DLIYLNGESL VREPLSRRRQ LLRENFVETE GEFVFATSLD TKDIEQIAEF LEQSVKDSCE
     GLMVKTLDVD ATYEIAKRSH NWLKLKKDYL DGVGDTLDLV VIGAYLGRGK RAGRYGGFLL
     ASYDEDSEEL QAICKLGTGF SDEELEEHHQ SLKALVLPSP RPYVRIDGAV IPDHWLDPSA
     VWEVKCADLS LSPIYPAARG LVDSDKGISL RFPRFIRVRE DKQPEQATTS AQVACLYRKQ
     SQIQNQQGED SGSDPEDTY
//
DBGET integrated database retrieval system