DNLI1_HUMAN
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 03-AUG-2022, entry version 222.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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; GLU-249;
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [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 project:
RT 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 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, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; THR-195
RP AND THR-233, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [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., Li S.-J.,
RA 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 reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT 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., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-66; SER-141;
RP THR-195; SER-201; SER-911 AND SER-913, AND IDENTIFICATION BY MASS
RP 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; SER-66;
RP SER-76; SER-141; THR-195; SER-201 AND SER-911, AND IDENTIFICATION BY MASS
RP 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 [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., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-76; SER-141
RP AND THR-195, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-51; SER-66; SER-76;
RP SER-141; THR-195; SER-199; SER-201; THR-207; SER-229; SER-230; THR-798;
RP SER-801 AND SER-819, 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 INTERACTION WITH PCNA.
RX PubMed=24911150; DOI=10.1172/jci74593;
RA Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y., Chioza B.A.,
RA Harlalka G.V., Mansour S., Sreekantan-Nair A., Patton M.A.,
RA Muggenthaler M., Rich P., Wagner K., Coblentz R., Stein C.K., Last J.I.,
RA Taylor A.M., Jackson A.P., Ogi T., 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 NICKED DNA
RP 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 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., 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).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair.
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};
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 Name=3;
CC IsoId=P18858-3; Sequence=VSP_057320, VSP_057321;
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";
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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 PDB; 1X9N; X-ray; 3.00 A; A=233-919.
DR PDB; 5YY9; X-ray; 2.65 A; C/D=118-130.
DR PDB; 6P09; X-ray; 2.05 A; A=262-904.
DR PDB; 6P0A; X-ray; 2.05 A; A=262-904.
DR PDB; 6P0B; X-ray; 2.20 A; A=262-904.
DR PDB; 6P0C; X-ray; 1.55 A; A=262-904.
DR PDB; 6P0D; X-ray; 1.75 A; A=262-904.
DR PDB; 6P0E; X-ray; 1.85 A; A=262-904.
DR PDB; 6Q1V; X-ray; 1.85 A; A=262-904.
DR PDB; 7KR3; X-ray; 2.78 A; A=262-904.
DR PDB; 7KR4; X-ray; 2.20 A; A=262-904.
DR PDB; 7L34; X-ray; 1.90 A; A=262-906.
DR PDB; 7L35; X-ray; 2.00 A; A=262-906.
DR PDBsum; 1X9N; -.
DR PDBsum; 5YY9; -.
DR PDBsum; 6P09; -.
DR PDBsum; 6P0A; -.
DR PDBsum; 6P0B; -.
DR PDBsum; 6P0C; -.
DR PDBsum; 6P0D; -.
DR PDBsum; 6P0E; -.
DR PDBsum; 6Q1V; -.
DR PDBsum; 7KR3; -.
DR PDBsum; 7KR4; -.
DR PDBsum; 7L34; -.
DR PDBsum; 7L35; -.
DR AlphaFoldDB; P18858; -.
DR SMR; P18858; -.
DR BioGRID; 110166; 69.
DR CORUM; P18858; -.
DR DIP; DIP-24215N; -.
DR ELM; P18858; -.
DR IntAct; P18858; 9.
DR MINT; P18858; -.
DR STRING; 9606.ENSP00000263274; -.
DR BindingDB; P18858; -.
DR ChEMBL; CHEMBL5694; -.
DR DrugBank; DB00290; Bleomycin.
DR iPTMnet; P18858; -.
DR MetOSite; P18858; -.
DR PhosphoSitePlus; P18858; -.
DR BioMuta; LIG1; -.
DR DMDM; 118773; -.
DR CPTAC; CPTAC-930; -.
DR EPD; P18858; -.
DR jPOST; P18858; -.
DR MassIVE; P18858; -.
DR MaxQB; P18858; -.
DR PaxDb; P18858; -.
DR PeptideAtlas; P18858; -.
DR PRIDE; P18858; -.
DR ProteomicsDB; 5130; -.
DR ProteomicsDB; 53617; -. [P18858-1]
DR Antibodypedia; 18267; 535 antibodies from 39 providers.
DR CPTC; P18858; 1 antibody.
DR DNASU; 3978; -.
DR Ensembl; ENST00000263274.12; ENSP00000263274.6; ENSG00000105486.14. [P18858-1]
DR Ensembl; ENST00000427526.6; ENSP00000442841.1; ENSG00000105486.14. [P18858-3]
DR Ensembl; ENST00000601091.5; ENSP00000471836.1; ENSG00000105486.14. [P18858-2]
DR Ensembl; ENST00000613670.4; ENSP00000483027.1; ENSG00000105486.14. [P18858-2]
DR GeneID; 3978; -.
DR KEGG; hsa:3978; -.
DR MANE-Select; ENST00000263274.12; ENSP00000263274.6; NM_000234.3; NP_000225.1.
DR UCSC; uc002pia.2; human. [P18858-1]
DR CTD; 3978; -.
DR DisGeNET; 3978; -.
DR GeneCards; LIG1; -.
DR HGNC; HGNC:6598; LIG1.
DR HPA; ENSG00000105486; Tissue enhanced (bone).
DR MIM; 126391; gene.
DR neXtProt; NX_P18858; -.
DR OpenTargets; ENSG00000105486; -.
DR PharmGKB; PA30372; -.
DR VEuPathDB; HostDB:ENSG00000105486; -.
DR eggNOG; KOG0967; Eukaryota.
DR GeneTree; ENSGT00940000157783; -.
DR InParanoid; P18858; -.
DR OMA; WIKYKRD; -.
DR OrthoDB; 274264at2759; -.
DR PhylomeDB; P18858; -.
DR TreeFam; TF300342; -.
DR BRENDA; 6.5.1.1; 2681.
DR PathwayCommons; P18858; -.
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 SignaLink; P18858; -.
DR SIGNOR; P18858; -.
DR BioGRID-ORCS; 3978; 160 hits in 1082 CRISPR screens.
DR ChiTaRS; LIG1; human.
DR EvolutionaryTrace; P18858; -.
DR GeneWiki; LIG1; -.
DR GenomeRNAi; 3978; -.
DR Pharos; P18858; Tchem.
DR PRO; PR:P18858; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P18858; protein.
DR Bgee; ENSG00000105486; Expressed in right uterine tube and 112 other tissues.
DR ExpressionAtlas; P18858; baseline and differential.
DR Genevisible; P18858; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0006287; P:base-excision repair, gap-filling; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; TAS:Reactome.
DR GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; IBA:GO_Central.
DR Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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; Cell cycle;
KW Cell division; DNA damage; DNA recombination; DNA repair; DNA replication;
KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..919
FT /note="DNA ligase 1"
FT /id="PRO_0000059570"
FT REGION 1..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..458
FT /note="Interaction with target DNA"
FT REGION 642..644
FT /note="Interaction with target DNA"
FT COMPBIAS 9..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 568
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15565146,
FT ECO:0007744|PDB:1X9N"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15565146,
FT ECO:0007744|PDB:1X9N"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15565146,
FT ECO:0007744|PDB:1X9N"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15565146,
FT ECO:0007744|PDB:1X9N"
FT BINDING 744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15565146,
FT ECO:0007744|PDB:1X9N"
FT SITE 305
FT /note="Interaction with target DNA"
FT SITE 590
FT /note="Interaction with target DNA"
FT SITE 770
FT /note="Interaction with target DNA"
FT SITE 795
FT /note="Interaction with target DNA"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37913"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 798
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 7..36
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057320"
FT VAR_SEQ 153
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057321"
FT VAR_SEQ 796..801
FT /note="LGTGFS -> VLGNWG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056139"
FT VAR_SEQ 802..919
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056140"
FT VARIANT 24
FT /note="A -> V (in dbSNP:rs3730855)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018802"
FT VARIANT 52
FT /note="P -> L (in dbSNP:rs4987181)"
FT /id="VAR_020194"
FT VARIANT 62
FT /note="R -> W (in dbSNP:rs3730863)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018803"
FT VARIANT 72
FT /note="D -> G (in dbSNP:rs4987070)"
FT /id="VAR_020195"
FT VARIANT 152
FT /note="K -> E (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs780748107)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036511"
FT VARIANT 249
FT /note="G -> E (in dbSNP:rs3730911)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016766"
FT VARIANT 267
FT /note="N -> S (in dbSNP:rs3730933)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016767"
FT VARIANT 349
FT /note="V -> M (in dbSNP:rs3730947)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018804"
FT VARIANT 369
FT /note="V -> I (in dbSNP:rs3730966)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018805"
FT VARIANT 409
FT /note="R -> H (in dbSNP:rs4987068)"
FT /id="VAR_016768"
FT VARIANT 480
FT /note="M -> V (in dbSNP:rs3730980)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016769"
FT VARIANT 566
FT /note="E -> K (found in a patient with a syndrome of
FT immunodeficiency and increased cellular sensitivity to DNA-
FT damaging agents due to LIG1 deficiency; dbSNP:rs121434560)"
FT /evidence="ECO:0000269|PubMed:1581963"
FT /id="VAR_002262"
FT VARIANT 612
FT /note="S -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs780324684)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036512"
FT VARIANT 614
FT /note="T -> I (in dbSNP:rs3731003)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016770"
FT VARIANT 677
FT /note="R -> L (in dbSNP:rs3731008)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_018806"
FT VARIANT 771
FT /note="R -> W (found in a patient with a syndrome of
FT immunodeficiency and increased cellular sensitivity to DNA-
FT damaging agents due to LIG1 deficiency; unknown
FT pathological significance; dbSNP:rs121434561)"
FT /evidence="ECO:0000269|PubMed:1581963"
FT /id="VAR_002263"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7KR4"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 401..413
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 489..509
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:7L34"
FT HELIX 528..531
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 551..558
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 570..578
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 599..608
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 616..626
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 627..630
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 653..665
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 675..685
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 693..695
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 704..716
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 722..730
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:7KR4"
FT STRAND 756..766
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 769..771
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 774..784
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 785..788
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 789..796
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 802..812
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 813..815
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 816..819
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:1X9N"
FT STRAND 833..836
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 841..845
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 847..854
FT /evidence="ECO:0007829|PDB:6P0C"
FT TURN 857..861
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 867..872
FT /evidence="ECO:0007829|PDB:6P0C"
FT STRAND 874..878
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:6P0C"
FT HELIX 890..899
FT /evidence="ECO:0007829|PDB:6P0C"
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
