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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: DNLI4_HUMAN A0A024RE06_HUMAN
LinkDB: DNLI4_HUMAN A0A024RE06_HUMAN
Original site: DNLI4_HUMAN A0A024RE06_HUMAN 
ID   DNLI4_HUMAN             Reviewed;         911 AA.
AC   P49917; Q8IY66; Q8TEU5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   28-MAR-2018, entry version 198.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=LIG4;
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], AND PARTIAL PROTEIN SEQUENCE.
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 [GENOMIC DNA], AND VARIANTS SER-231 AND THR-857.
RG   NIEHS SNPs program;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=8798671; DOI=10.1074/jbc.271.39.24257;
RA   Robins P., Lindahl T.;
RT   "DNA ligase IV from HeLa cell nuclei.";
RL   J. Biol. Chem. 271:24257-24261(1996).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH XRCC4.
RX   PubMed=9809069; DOI=10.1016/S1097-2765(00)80147-1;
RA   Grawunder U., Zimmer D., Fugmann S., Schwarz K., Lieber M.R.;
RT   "DNA ligase IV is essential for V(D)J recombination and DNA double-
RT   strand break repair in human precursor lymphocytes.";
RL   Mol. Cell 2:477-484(1998).
RN   [7]
RP   INTERACTION WITH XRCC4.
RX   PubMed=9259561; DOI=10.1016/S0960-9822(06)00258-2;
RA   Critchlow S.E., Bowater R.P., Jackson S.P.;
RT   "Mammalian DNA double-strand break repair protein XRCC4 interacts with
RT   DNA ligase IV.";
RL   Curr. Biol. 7:588-598(1997).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH XRCC4; G22P1; G22P2 AND PRKDC.
RX   PubMed=10854421; DOI=10.1074/jbc.M000491200;
RA   Chen L., Trujillo K., Sung P., Tomkinson A.E.;
RT   "Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the
RT   DNA-dependent protein kinase.";
RL   J. Biol. Chem. 275:26196-26205(2000).
RN   [9]
RP   IDENTIFICATION IN A COMPLEX WITH G22P1; G22P2 AND PRKDC.
RX   PubMed=12547193; DOI=10.1016/S0022-2836(02)01328-1;
RA   Calsou P., Delteil C., Frit P., Drouet J., Salles B.;
RT   "Coordinated assembly of Ku and p460 subunits of the DNA-dependent
RT   protein kinase on DNA ends is necessary for XRCC4-ligase IV
RT   recruitment.";
RL   J. Mol. Biol. 326:93-103(2003).
RN   [10]
RP   INTERACTION WITH APLF.
RX   PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
RA   Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S.,
RA   Yasui A.;
RT   "A novel human AP endonuclease with conserved zinc-finger-like motifs
RT   involved in DNA strand break responses.";
RL   EMBO J. 26:2094-2103(2007).
RN   [11]
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   [12]
RP   SUBUNIT.
RX   PubMed=25941166; DOI=10.1038/cdd.2015.22;
RA   Craxton A., Somers J., Munnur D., Jukes-Jones R., Cain K.,
RA   Malewicz M.;
RT   "XLS (c9orf142) is a new component of mammalian DNA double-stranded
RT   break repair.";
RL   Cell Death Differ. 22:890-897(2015).
RN   [13]
RP   SUBUNIT.
RX   PubMed=25670504; DOI=10.1038/ncomms7233;
RA   Xing M., Yang M., Huo W., Feng F., Wei L., Jiang W., Ning S., Yan Z.,
RA   Li W., Wang Q., Hou M., Dong C., Guo R., Gao G., Ji J., Zha S.,
RA   Lan L., Liang H., Xu D.;
RT   "Interactome analysis identifies a new paralogue of XRCC4 in non-
RT   homologous end joining DNA repair pathway.";
RL   Nat. Commun. 6:6233-6233(2015).
RN   [14]
RP   SUBUNIT.
RX   PubMed=25574025; DOI=10.1126/science.1261971;
RA   Ochi T., Blackford A.N., Coates J., Jhujh S., Mehmood S., Tamura N.,
RA   Travers J., Wu Q., Draviam V.M., Robinson C.V., Blundell T.L.,
RA   Jackson S.P.;
RT   "DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to
RT   promote DNA double-strand break repair.";
RL   Science 347:185-188(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 748-784 IN COMPLEX WITH
RP   XRCC4.
RX   PubMed=11702069; DOI=10.1038/nsb725;
RA   Sibanda B.L., Critchlow S.E., Begun J., Pei X.Y., Jackson S.P.,
RA   Blundell T.L., Pellegrini L.;
RT   "Crystal structure of an Xrcc4-DNA ligase IV complex.";
RL   Nat. Struct. Biol. 8:1015-1019(2001).
RN   [16]
RP   STRUCTURE BY NMR OF 654-759.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first BRCT domain of human DNA ligase IV.";
RL   Submitted (DEC-2006) to the PDB data bank.
RN   [17]
RP   VARIANT LEUKEMIA HIS-278.
RX   PubMed=10395545; DOI=10.1016/S0960-9822(99)80311-X;
RA   Riballo E., Critchlow S.E., Teo S.-H., Doherty A.J., Priestley A.,
RA   Broughton B.C., Kysela B., Beamish H., Plowman N., Arlett C.F.,
RA   Lehmann A.R., Jackson S.P., Jeggo P.A.;
RT   "Identification of a defect in DNA ligase IV in a radiosensitive
RT   leukaemia patient.";
RL   Curr. Biol. 9:699-702(1999).
RN   [18]
RP   CHARACTERIZATION OF VARIANT HIS-278.
RX   PubMed=11349135; DOI=10.1074/jbc.M103866200;
RA   Riballo E., Doherty A.J., Dai Y., Stiff T., Oettinger M.A.,
RA   Jeggo P.A., Kysela B.;
RT   "Cellular and biochemical impact of a mutation in DNA ligase IV
RT   conferring clinical radiosensitivity.";
RL   J. Biol. Chem. 276:31124-31132(2001).
RN   [19]
RP   VARIANTS LIG4S HIS-278 AND GLU-469.
RX   PubMed=11779494; DOI=10.1016/S1097-2765(01)00408-7;
RA   O'Driscoll M., Cerosaletti K.M., Girard P.-M., Dai Y., Stumm M.,
RA   Kysela B., Hirsch B., Gennery A., Palmer S.E., Seidel J., Gatti R.A.,
RA   Varon R., Oettinger M.A., Neitzel H., Jeggo P.A., Concannon P.;
RT   "DNA ligase IV mutations identified in patients exhibiting
RT   developmental delay and immunodeficiency.";
RL   Mol. Cell 8:1175-1185(2001).
RN   [20]
RP   VARIANTS VAL-3 AND ILE-9, AND ASSOCIATION WITH RESISTANCE TO MULTIPLE
RP   MYELOMA.
RX   PubMed=12471202; DOI=10.1136/jmg.39.12.900;
RA   Roddam P.L., Rollinson S., O'Driscoll M., Jeggo P.A., Jack A.,
RA   Morgan G.J.;
RT   "Genetic variants of NHEJ DNA ligase IV can affect the risk of
RT   developing multiple myeloma, a tumour characterised by aberrant class
RT   switch recombination.";
RL   J. Med. Genet. 39:900-905(2002).
RN   [21]
RP   VARIANT RSSCID GLN-433 DEL.
RX   PubMed=16357942; DOI=10.1172/JCI26121;
RA   van der Burg M., van Veelen L.R., Verkaik N.S., Wiegant W.W.,
RA   Hartwig N.G., Barendregt B.H., Brugmans L., Raams A., Jaspers N.G.J.,
RA   Zdzienicka M.Z., van Dongen J.J.M., van Gent D.C.;
RT   "A new type of radiosensitive T-B-NK(+) severe combined
RT   immunodeficiency caused by a LIG4 mutation.";
RL   J. Clin. Invest. 116:137-145(2006).
RN   [22]
RP   VARIANT PRO-774.
RX   PubMed=25728776; DOI=10.1016/j.ajhg.2015.01.013;
RA   Murray J.E., van der Burg M., Ijspeert H., Carroll P., Wu Q., Ochi T.,
RA   Leitch A., Miller E.S., Kysela B., Jawad A., Bottani A., Brancati F.,
RA   Cappa M., Cormier-Daire V., Deshpande C., Faqeih E.A., Graham G.E.,
RA   Ranza E., Blundell T.L., Jackson A.P., Stewart G.S., Bicknell L.S.;
RT   "Mutations in the NHEJ component XRCC4 cause primordial dwarfism.";
RL   Am. J. Hum. Genet. 96:412-424(2015).
CC   -!- FUNCTION: Efficiently joins single-strand breaks in a double-
CC       stranded polydeoxynucleotide in an ATP-dependent reaction.
CC       Involved in DNA non-homologous end joining (NHEJ) required for
CC       double-strand break repair and V(D)J recombination. The LIG4-XRCC4
CC       complex is responsible for the NHEJ ligation step, and XRCC4
CC       enhances the joining activity of LIG4. Binding of the LIG4-XRCC4
CC       complex to DNA ends is dependent on the assembly of the DNA-
CC       dependent protein kinase complex DNA-PK to these DNA ends.
CC       {ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:9809069}.
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; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with XRCC4. The LIG4-XRCC4 complex has probably
CC       a 1:2 stoichiometry. The LIG4-XRCC4 complex associates in a DNA-
CC       dependent manner with the DNA-PK complex composed of PRKDC,
CC       XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end
CC       joining (NHEJ) complex. Additional components of the NHEJ complex
CC       include NHEJ1/XLF and PAXX. Interacts with APLF.
CC       {ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:11702069,
CC       ECO:0000269|PubMed:12547193, ECO:0000269|PubMed:17396150,
CC       ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504,
CC       ECO:0000269|PubMed:25941166, ECO:0000269|PubMed:9259561,
CC       ECO:0000269|PubMed:9809069}.
CC   -!- INTERACTION:
CC       Q8IW19:APLF; NbExp=2; IntAct=EBI-847896, EBI-1256044;
CC       Q96SD1:DCLRE1C; NbExp=16; IntAct=EBI-847896, EBI-11694104;
CC       Q9H9Q4:NHEJ1; NbExp=4; IntAct=EBI-847896, EBI-847807;
CC       Q13426:XRCC4; NbExp=13; IntAct=EBI-847896, EBI-717592;
CC       Q13426-2:XRCC4; NbExp=11; IntAct=EBI-847896, EBI-15891375;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
CC   -!- DISEASE: LIG4 syndrome (LIG4S) [MIM:606593]: Characterized by
CC       immunodeficiency and developmental and growth delay. Patients
CC       display unusual facial features, microcephaly, growth and/or
CC       developmental delay, pancytopenia, and various skin abnormalities.
CC       {ECO:0000269|PubMed:11779494}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Severe combined immunodeficiency autosomal recessive T-
CC       cell-negative/B-cell-negative/NK-cell-positive with sensitivity to
CC       ionizing radiation (RSSCID) [MIM:602450]: A form of severe
CC       combined immunodeficiency, a genetically and clinically
CC       heterogeneous group of rare congenital disorders characterized by
CC       impairment of both humoral and cell-mediated immunity, leukopenia,
CC       and low or absent antibody levels. Patients present in infancy
CC       with recurrent, persistent infections by opportunistic organisms.
CC       The common characteristic of all types of SCID is absence of T-
CC       cell-mediated cellular immunity due to a defect in T-cell
CC       development. Individuals affected by RS-SCID show defects in the
CC       DNA repair machinery necessary for coding joint formation and the
CC       completion of V(D)J recombination. A subset of cells from such
CC       patients show increased radiosensitivity.
CC       {ECO:0000269|PubMed:16357942}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL77435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA58467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=LIG4base; Note=LIG4 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/LIG4base/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/lig4/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
CC       URL="https://en.wikipedia.org/wiki/DNA_ligase";
DR   EMBL; X83441; CAA58467.1; ALT_INIT; mRNA.
DR   EMBL; AF479264; AAL77435.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL157762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC037491; AAH37491.1; -; mRNA.
DR   CCDS; CCDS9508.1; -.
DR   PIR; I37079; I37079.
DR   RefSeq; NP_001091738.1; NM_001098268.1.
DR   RefSeq; NP_001317524.1; NM_001330595.1.
DR   RefSeq; NP_002303.2; NM_002312.3.
DR   RefSeq; NP_996820.1; NM_206937.1.
DR   RefSeq; XP_005254113.1; XM_005254056.1.
DR   RefSeq; XP_005254114.1; XM_005254057.4.
DR   RefSeq; XP_005254115.1; XM_005254058.3.
DR   RefSeq; XP_006720014.1; XM_006719951.3.
DR   RefSeq; XP_006720015.1; XM_006719952.1.
DR   RefSeq; XP_011519393.1; XM_011521091.2.
DR   RefSeq; XP_011519394.1; XM_011521092.2.
DR   RefSeq; XP_016876058.1; XM_017020569.1.
DR   RefSeq; XP_016876059.1; XM_017020570.1.
DR   RefSeq; XP_016876060.1; XM_017020571.1.
DR   RefSeq; XP_016876062.1; XM_017020573.1.
DR   UniGene; Hs.166091; -.
DR   PDB; 1IK9; X-ray; 2.30 A; C=748-784.
DR   PDB; 2E2W; NMR; -; A=654-759.
DR   PDB; 3II6; X-ray; 2.40 A; X/Y=654-911.
DR   PDB; 3VNN; X-ray; 2.90 A; A=268-406.
DR   PDB; 3W1B; X-ray; 2.40 A; A=1-609.
DR   PDB; 3W1G; X-ray; 2.55 A; A=1-609.
DR   PDB; 3W5O; X-ray; 2.84 A; A/B=1-609.
DR   PDB; 4HTO; X-ray; 2.81 A; A=1-240.
DR   PDB; 4HTP; X-ray; 2.25 A; A/B=1-240.
DR   PDBsum; 1IK9; -.
DR   PDBsum; 2E2W; -.
DR   PDBsum; 3II6; -.
DR   PDBsum; 3VNN; -.
DR   PDBsum; 3W1B; -.
DR   PDBsum; 3W1G; -.
DR   PDBsum; 3W5O; -.
DR   PDBsum; 4HTO; -.
DR   PDBsum; 4HTP; -.
DR   ProteinModelPortal; P49917; -.
DR   SMR; P49917; -.
DR   BioGrid; 110169; 130.
DR   CORUM; P49917; -.
DR   DIP; DIP-37958N; -.
DR   IntAct; P49917; 12.
DR   MINT; P49917; -.
DR   STRING; 9606.ENSP00000349393; -.
DR   iPTMnet; P49917; -.
DR   PhosphoSitePlus; P49917; -.
DR   BioMuta; LIG4; -.
DR   DMDM; 88911290; -.
DR   EPD; P49917; -.
DR   MaxQB; P49917; -.
DR   PaxDb; P49917; -.
DR   PeptideAtlas; P49917; -.
DR   PRIDE; P49917; -.
DR   DNASU; 3981; -.
DR   Ensembl; ENST00000356922; ENSP00000349393; ENSG00000174405.
DR   Ensembl; ENST00000405925; ENSP00000385955; ENSG00000174405.
DR   Ensembl; ENST00000442234; ENSP00000402030; ENSG00000174405.
DR   Ensembl; ENST00000611712; ENSP00000484288; ENSG00000174405.
DR   GeneID; 3981; -.
DR   KEGG; hsa:3981; -.
DR   UCSC; uc001vqn.4; human.
DR   CTD; 3981; -.
DR   DisGeNET; 3981; -.
DR   EuPathDB; HostDB:ENSG00000174405.13; -.
DR   GeneCards; LIG4; -.
DR   HGNC; HGNC:6601; LIG4.
DR   HPA; HPA001334; -.
DR   MalaCards; LIG4; -.
DR   MIM; 601837; gene.
DR   MIM; 602450; phenotype.
DR   MIM; 606593; phenotype.
DR   neXtProt; NX_P49917; -.
DR   OpenTargets; ENSG00000174405; -.
DR   Orphanet; 235; Dubowitz syndrome.
DR   Orphanet; 99812; LIG4 syndrome.
DR   Orphanet; 39041; Omenn syndrome.
DR   PharmGKB; PA30375; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   GeneTree; ENSGT00860000133881; -.
DR   HOGENOM; HOG000007831; -.
DR   HOVERGEN; HBG005516; -.
DR   InParanoid; P49917; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG091G03K0; -.
DR   PhylomeDB; P49917; -.
DR   TreeFam; TF312980; -.
DR   BRENDA; 6.5.1.1; 2681.
DR   Reactome; R-HSA-164843; 2-LTR circle formation.
DR   Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR   SignaLink; P49917; -.
DR   SIGNOR; P49917; -.
DR   ChiTaRS; LIG4; human.
DR   EvolutionaryTrace; P49917; -.
DR   GeneWiki; LIG4; -.
DR   GenomeRNAi; 3981; -.
DR   PRO; PR:P49917; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000174405; -.
DR   CleanEx; HS_LIG4; -.
DR   ExpressionAtlas; P49917; baseline and differential.
DR   Genevisible; P49917; HS.
DR   GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR   GO; GO:0032807; C:DNA ligase IV complex; IMP:UniProtKB.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
DR   GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; IC:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:UniProtKB.
DR   GO; GO:0003909; F:DNA ligase activity; IDA:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006266; P:DNA ligation; IDA:UniProtKB.
DR   GO; GO:0051102; P:DNA ligation involved in DNA recombination; ISS:UniProtKB.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
DR   GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IMP:BHF-UCL.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR   GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IDA:UniProtKB.
DR   GO; GO:2001252; P:positive regulation of chromosome organization; IMP:BHF-UCL.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:0002328; P:pro-B cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0010165; P:response to X-ray; IMP:UniProtKB.
DR   GO; GO:0000012; P:single strand break repair; IDA:UniProtKB.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR   GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR   GO; GO:0033153; P:T cell receptor V(D)J recombination; ISS:UniProtKB.
DR   GO; GO:0033151; P:V(D)J recombination; IDA:UniProtKB.
DR   CDD; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
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; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 2.
DR   Pfam; PF00533; BRCT; 2.
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; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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; ATP-binding; Cell cycle; Cell division;
KW   Complete proteome; Direct protein sequencing; Disease mutation;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Polymorphism;
KW   Reference proteome; Repeat; SCID.
FT   CHAIN         1    911       DNA ligase 4.
FT                                /FTId=PRO_0000059576.
FT   DOMAIN      654    743       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      808    911       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    273    273       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       331    331       Magnesium 1. {ECO:0000255}.
FT   METAL       427    427       Magnesium 2. {ECO:0000255}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   BINDING     278    278       ATP. {ECO:0000250}.
FT   BINDING     293    293       ATP. {ECO:0000250}.
FT   BINDING     432    432       ATP. {ECO:0000250}.
FT   BINDING     443    443       ATP. {ECO:0000250}.
FT   BINDING     449    449       ATP. {ECO:0000250}.
FT   VARIANT       3      3       A -> V (associated with resistance to
FT                                multiple myeloma; dbSNP:rs1805389).
FT                                {ECO:0000269|PubMed:12471202}.
FT                                /FTId=VAR_029352.
FT   VARIANT       9      9       T -> I (associated with resistance to
FT                                multiple myeloma; dbSNP:rs1805388).
FT                                {ECO:0000269|PubMed:12471202}.
FT                                /FTId=VAR_033884.
FT   VARIANT      62     62       D -> H (in dbSNP:rs3093763).
FT                                /FTId=VAR_029353.
FT   VARIANT     231    231       P -> S (in dbSNP:rs3093765).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_018808.
FT   VARIANT     278    278       R -> H (in LIG4S and leukemia; impairs
FT                                activity; dbSNP:rs104894421).
FT                                {ECO:0000269|PubMed:10395545,
FT                                ECO:0000269|PubMed:11349135,
FT                                ECO:0000269|PubMed:11779494}.
FT                                /FTId=VAR_012774.
FT   VARIANT     433    433       Missing (in RSSCID).
FT                                {ECO:0000269|PubMed:16357942}.
FT                                /FTId=VAR_044123.
FT   VARIANT     461    461       E -> G (in dbSNP:rs2232640).
FT                                /FTId=VAR_044124.
FT   VARIANT     469    469       G -> E (in LIG4S; dbSNP:rs104894420).
FT                                {ECO:0000269|PubMed:11779494}.
FT                                /FTId=VAR_012775.
FT   VARIANT     539    539       L -> F (in dbSNP:rs3742212).
FT                                /FTId=VAR_016771.
FT   VARIANT     658    658       I -> V (in dbSNP:rs2232641).
FT                                /FTId=VAR_016772.
FT   VARIANT     774    774       L -> P (found in a patient with
FT                                microcephalic primordial dwarfism;
FT                                unknown pathological significance).
FT                                {ECO:0000269|PubMed:25728776}.
FT                                /FTId=VAR_075826.
FT   VARIANT     857    857       A -> T (in dbSNP:rs2232642).
FT                                {ECO:0000269|Ref.2}.
FT                                /FTId=VAR_016773.
FT   CONFLICT    246    246       F -> S (in Ref. 1; CAA58467).
FT                                {ECO:0000305}.
FT   HELIX        10     12       {ECO:0000244|PDB:4HTP}.
FT   HELIX        16     28       {ECO:0000244|PDB:4HTP}.
FT   HELIX        32     53       {ECO:0000244|PDB:4HTP}.
FT   TURN         54     56       {ECO:0000244|PDB:4HTP}.
FT   HELIX        65     71       {ECO:0000244|PDB:4HTP}.
FT   HELIX        73     75       {ECO:0000244|PDB:4HTP}.
FT   HELIX        86     96       {ECO:0000244|PDB:4HTP}.
FT   HELIX       104    110       {ECO:0000244|PDB:4HTP}.
FT   HELIX       125    133       {ECO:0000244|PDB:4HTP}.
FT   TURN        134    136       {ECO:0000244|PDB:3W1B}.
FT   HELIX       145    160       {ECO:0000244|PDB:4HTP}.
FT   HELIX       164    176       {ECO:0000244|PDB:4HTP}.
FT   HELIX       180    191       {ECO:0000244|PDB:4HTP}.
FT   HELIX       200    207       {ECO:0000244|PDB:4HTP}.
FT   HELIX       211    218       {ECO:0000244|PDB:4HTP}.
FT   HELIX       221    227       {ECO:0000244|PDB:4HTP}.
FT   STRAND      250    253       {ECO:0000244|PDB:3W1B}.
FT   HELIX       256    258       {ECO:0000244|PDB:3W1B}.
FT   HELIX       259    262       {ECO:0000244|PDB:3W1B}.
FT   TURN        263    265       {ECO:0000244|PDB:3W1B}.
FT   STRAND      268    272       {ECO:0000244|PDB:3W1B}.
FT   STRAND      276    284       {ECO:0000244|PDB:3W1B}.
FT   STRAND      287    292       {ECO:0000244|PDB:3W1B}.
FT   HELIX       299    302       {ECO:0000244|PDB:3W1B}.
FT   STRAND      308    311       {ECO:0000244|PDB:3W1B}.
FT   HELIX       312    315       {ECO:0000244|PDB:3W1B}.
FT   HELIX       316    318       {ECO:0000244|PDB:3W1B}.
FT   STRAND      324    336       {ECO:0000244|PDB:3W1B}.
FT   TURN        337    340       {ECO:0000244|PDB:3W1B}.
FT   STRAND      341    343       {ECO:0000244|PDB:3W1B}.
FT   HELIX       351    356       {ECO:0000244|PDB:3W1B}.
FT   STRAND      359    372       {ECO:0000244|PDB:3W1B}.
FT   STRAND      378    380       {ECO:0000244|PDB:3VNN}.
FT   HELIX       382    392       {ECO:0000244|PDB:3W1B}.
FT   TURN        397    399       {ECO:0000244|PDB:3W1B}.
FT   STRAND      400    402       {ECO:0000244|PDB:3W1B}.
FT   STRAND      405    408       {ECO:0000244|PDB:3W1B}.
FT   HELIX       411    423       {ECO:0000244|PDB:3W1B}.
FT   STRAND      429    432       {ECO:0000244|PDB:3W1B}.
FT   STRAND      443    450       {ECO:0000244|PDB:3W1B}.
FT   HELIX       458    460       {ECO:0000244|PDB:3W1B}.
FT   STRAND      462    471       {ECO:0000244|PDB:3W1B}.
FT   HELIX       474    478       {ECO:0000244|PDB:3W1B}.
FT   STRAND      479    488       {ECO:0000244|PDB:3W1B}.
FT   STRAND      500    507       {ECO:0000244|PDB:3W1B}.
FT   HELIX       513    522       {ECO:0000244|PDB:3W1B}.
FT   HELIX       523    525       {ECO:0000244|PDB:3W1B}.
FT   STRAND      536    539       {ECO:0000244|PDB:3W1G}.
FT   STRAND      546    548       {ECO:0000244|PDB:3W1B}.
FT   HELIX       551    553       {ECO:0000244|PDB:3W1B}.
FT   STRAND      556    560       {ECO:0000244|PDB:3W1B}.
FT   STRAND      562    566       {ECO:0000244|PDB:3W1B}.
FT   STRAND      568    570       {ECO:0000244|PDB:3W1B}.
FT   STRAND      573    578       {ECO:0000244|PDB:3W1B}.
FT   STRAND      580    584       {ECO:0000244|PDB:3W1B}.
FT   HELIX       590    592       {ECO:0000244|PDB:3W1B}.
FT   HELIX       596    603       {ECO:0000244|PDB:3W1B}.
FT   TURN        658    661       {ECO:0000244|PDB:3II6}.
FT   STRAND      663    666       {ECO:0000244|PDB:3II6}.
FT   STRAND      671    673       {ECO:0000244|PDB:2E2W}.
FT   HELIX       675    684       {ECO:0000244|PDB:3II6}.
FT   STRAND      687    692       {ECO:0000244|PDB:2E2W}.
FT   STRAND      697    701       {ECO:0000244|PDB:3II6}.
FT   HELIX       707    714       {ECO:0000244|PDB:3II6}.
FT   HELIX       723    732       {ECO:0000244|PDB:3II6}.
FT   HELIX       740    742       {ECO:0000244|PDB:3II6}.
FT   STRAND      743    745       {ECO:0000244|PDB:3II6}.
FT   HELIX       748    753       {ECO:0000244|PDB:3II6}.
FT   TURN        754    757       {ECO:0000244|PDB:3II6}.
FT   STRAND      764    767       {ECO:0000244|PDB:1IK9}.
FT   HELIX       771    779       {ECO:0000244|PDB:1IK9}.
FT   HELIX       789    802       {ECO:0000244|PDB:3II6}.
FT   HELIX       809    811       {ECO:0000244|PDB:3II6}.
FT   TURN        812    815       {ECO:0000244|PDB:3II6}.
FT   STRAND      817    820       {ECO:0000244|PDB:3II6}.
FT   STRAND      823    825       {ECO:0000244|PDB:3II6}.
FT   HELIX       829    831       {ECO:0000244|PDB:3II6}.
FT   HELIX       837    847       {ECO:0000244|PDB:3II6}.
FT   STRAND      851    855       {ECO:0000244|PDB:3II6}.
FT   STRAND      862    865       {ECO:0000244|PDB:3II6}.
FT   HELIX       872    880       {ECO:0000244|PDB:3II6}.
FT   STRAND      887    890       {ECO:0000244|PDB:3II6}.
FT   HELIX       892    899       {ECO:0000244|PDB:3II6}.
FT   HELIX       906    908       {ECO:0000244|PDB:3II6}.
SQ   SEQUENCE   911 AA;  103971 MW;  2122813E1EFA63B9 CRC64;
     MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH DALHKNHKDV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTHG
     DAGDFAMIAY FVLKPRCLQK GSLTIQQVND LLDSIASNNS AKRKDLIKKS LLQLITQSSA
     LEQKWLIRMI IKDLKLGVSQ QTIFSVFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI
     TLFSAFKPML AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD
     QFGASPTEGS LTPFIHNAFK ADIQICILDG EMMAYNPNTQ TFMQKGTKFD IKRMVEDSDL
     QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI EIVQKTQAHT KNEVIDALNE
     AIDKREEGIM VKQPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDILIVGGY WGKGSRGGMM
     SHFLCAVAEK PPPGEKPSVF HTLSRVGSGC TMKELYDLGL KLAKYWKPFH RKAPPSSILC
     GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE
     QLRGKASGKL ASKHLYIGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT NVNKISNIFE
     DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIILSNKHDV
     VKPAWLLECF KTKSFVPWQP RFMIHMCPST KEHFAREYDC YGDSYFIDTD LNQLKEVFSG
     IKNSNEQTPE EMASLIADLE YRYSWDCSPL SMFRRHTVYL DSYAVINDLS TKNEGTRLAI
     KALELRFHGA KVVSCLAEGV SHVIIGEDHS RVADFKAFRR TFKRKFKILK ESWVTDSIDK
     CELQEENQYL I
//
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Ontology (48)   
   GO (48)   
Disease (3)   
   OMIM (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (14)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (9)   
Protein sequence (15)   
   RefSeq(pep) (15)   
DNA sequence (4)   
   EMBL (4)   
3D Structure (9)   
   PDB (9)   
Protein domain (21)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (4)   
   SMART (1)   
Literature (20)   
   PubMed (20)   
Enzyme (1)   
   BRENDA (1)   
All databases (136)   

Download RDF
ID   A0A024RE06_HUMAN        Unreviewed;       911 AA.
AC   A0A024RE06;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   28-MAR-2018, entry version 39.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG4 {ECO:0000313|EMBL:EAX09095.1};
GN   ORFNames=hCG_27194 {ECO:0000313|EMBL:EAX09095.1};
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 {ECO:0000313|EMBL:EAX09095.1};
RN   [1] {ECO:0000313|EMBL:EAX09095.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
RA   Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
RA   Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
RA   Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
RA   Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
RA   Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
RA   Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
RA   Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
RA   Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
RA   Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
RA   Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
RA   Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
RA   Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
RA   Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
RA   Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
RA   Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
RA   Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
RA   Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
RA   Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
RA   Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
RA   Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
RA   Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
RA   Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
RA   Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
RA   McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
RA   Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
RA   Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
RA   Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
RA   Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
RA   Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
RA   Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
RA   Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
RA   Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
RA   Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
RA   Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
RA   Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
RA   Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
RA   Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
RA   McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
RA   Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAX09095.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton 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.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CH471085; EAX09094.1; -; Genomic_DNA.
DR   EMBL; CH471085; EAX09095.1; -; Genomic_DNA.
DR   EMBL; CH471085; EAX09096.1; -; Genomic_DNA.
DR   RefSeq; NP_001091738.1; NM_001098268.1.
DR   RefSeq; NP_002303.2; NM_002312.3.
DR   RefSeq; NP_996820.1; NM_206937.1.
DR   RefSeq; XP_005254113.1; XM_005254056.1.
DR   RefSeq; XP_005254114.1; XM_005254057.4.
DR   RefSeq; XP_005254115.1; XM_005254058.3.
DR   RefSeq; XP_006720014.1; XM_006719951.3.
DR   RefSeq; XP_006720015.1; XM_006719952.1.
DR   RefSeq; XP_011519393.1; XM_011521091.2.
DR   RefSeq; XP_011519394.1; XM_011521092.2.
DR   RefSeq; XP_016876058.1; XM_017020569.1.
DR   RefSeq; XP_016876059.1; XM_017020570.1.
DR   RefSeq; XP_016876060.1; XM_017020571.1.
DR   UniGene; Hs.166091; -.
DR   GeneID; 3981; -.
DR   KEGG; hsa:3981; -.
DR   CTD; 3981; -.
DR   EuPathDB; HostDB:ENSG00000174405.13; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   OrthoDB; EOG091G03K0; -.
DR   ChiTaRS; LIG4; human.
DR   GenomeRNAi; 3981; -.
DR   Bgee; ENSG00000174405; -.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR   GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051102; P:DNA ligation involved in DNA recombination; IEA:Ensembl.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:Ensembl.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0045190; P:isotype switching; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0002328; P:pro-B cell differentiation; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0033153; P:T cell receptor V(D)J recombination; IEA:Ensembl.
DR   CDD; cd00027; BRCT; 2.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
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; IPR021536; DNA_ligase_IV_dom.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF7; PTHR10459:SF7; 2.
DR   Pfam; PF00533; BRCT; 2.
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; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 2.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:EAX09095.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      355    489       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      654    743       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      808    911       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   911 AA;  103971 MW;  2122813E1EFA63B9 CRC64;
     MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH DALHKNHKDV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTHG
     DAGDFAMIAY FVLKPRCLQK GSLTIQQVND LLDSIASNNS AKRKDLIKKS LLQLITQSSA
     LEQKWLIRMI IKDLKLGVSQ QTIFSVFHND AAELHNVTTD LEKVCRQLHD PSVGLSDISI
     TLFSAFKPML AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD
     QFGASPTEGS LTPFIHNAFK ADIQICILDG EMMAYNPNTQ TFMQKGTKFD IKRMVEDSDL
     QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI EIVQKTQAHT KNEVIDALNE
     AIDKREEGIM VKQPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDILIVGGY WGKGSRGGMM
     SHFLCAVAEK PPPGEKPSVF HTLSRVGSGC TMKELYDLGL KLAKYWKPFH RKAPPSSILC
     GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE
     QLRGKASGKL ASKHLYIGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT NVNKISNIFE
     DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSENIRVK NIILSNKHDV
     VKPAWLLECF KTKSFVPWQP RFMIHMCPST KEHFAREYDC YGDSYFIDTD LNQLKEVFSG
     IKNSNEQTPE EMASLIADLE YRYSWDCSPL SMFRRHTVYL DSYAVINDLS TKNEGTRLAI
     KALELRFHGA KVVSCLAEGV SHVIIGEDHS RVADFKAFRR TFKRKFKILK ESWVTDSIDK
     CELQEENQYL I
//
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Ontology (27)   
   GO (27)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (13)   
   RefSeq(pep) (13)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (11)   
   Pfam (5)   
   PROSITE (4)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (68)   

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