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DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4)

 DNLI4_HUMAN             Reviewed;         911 AA.
P49917; Q8IY66; Q8TEU5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 2.
25-OCT-2017, entry version 196.
RecName: Full=DNA ligase 4;
EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
AltName: Full=DNA ligase IV;
AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
Name=LIG4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Prostate;
PubMed=7760816; DOI=10.1128/MCB.15.6.3206;
Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C.,
Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E.,
Haseltine W.A., Lindahl T.;
"Molecular cloning and expression of human cDNAs encoding a novel DNA
ligase IV and DNA ligase III, an enzyme active in DNA repair and
recombination.";
Mol. Cell. Biol. 15:3206-3216(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-231 AND THR-857.
NIEHS SNPs program;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
CHARACTERIZATION.
PubMed=8798671; DOI=10.1074/jbc.271.39.24257;
Robins P., Lindahl T.;
"DNA ligase IV from HeLa cell nuclei.";
J. Biol. Chem. 271:24257-24261(1996).
[6]
FUNCTION, AND INTERACTION WITH XRCC4.
PubMed=9809069; DOI=10.1016/S1097-2765(00)80147-1;
Grawunder U., Zimmer D., Fugmann S., Schwarz K., Lieber M.R.;
"DNA ligase IV is essential for V(D)J recombination and DNA double-
strand break repair in human precursor lymphocytes.";
Mol. Cell 2:477-484(1998).
[7]
INTERACTION WITH XRCC4.
PubMed=9259561; DOI=10.1016/S0960-9822(06)00258-2;
Critchlow S.E., Bowater R.P., Jackson S.P.;
"Mammalian DNA double-strand break repair protein XRCC4 interacts with
DNA ligase IV.";
Curr. Biol. 7:588-598(1997).
[8]
FUNCTION, AND INTERACTION WITH XRCC4; G22P1; G22P2 AND PRKDC.
PubMed=10854421; DOI=10.1074/jbc.M000491200;
Chen L., Trujillo K., Sung P., Tomkinson A.E.;
"Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the
DNA-dependent protein kinase.";
J. Biol. Chem. 275:26196-26205(2000).
[9]
IDENTIFICATION IN A COMPLEX WITH G22P1; G22P2 AND PRKDC.
PubMed=12547193; DOI=10.1016/S0022-2836(02)01328-1;
Calsou P., Delteil C., Frit P., Drouet J., Salles B.;
"Coordinated assembly of Ku and p460 subunits of the DNA-dependent
protein kinase on DNA ends is necessary for XRCC4-ligase IV
recruitment.";
J. Mol. Biol. 326:93-103(2003).
[10]
INTERACTION WITH APLF.
PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S.,
Yasui A.;
"A novel human AP endonuclease with conserved zinc-finger-like motifs
involved in DNA strand break responses.";
EMBO J. 26:2094-2103(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
SUBUNIT.
PubMed=25941166; DOI=10.1038/cdd.2015.22;
Craxton A., Somers J., Munnur D., Jukes-Jones R., Cain K.,
Malewicz M.;
"XLS (c9orf142) is a new component of mammalian DNA double-stranded
break repair.";
Cell Death Differ. 22:890-897(2015).
[13]
SUBUNIT.
PubMed=25670504; DOI=10.1038/ncomms7233;
Xing M., Yang M., Huo W., Feng F., Wei L., Jiang W., Ning S., Yan Z.,
Li W., Wang Q., Hou M., Dong C., Guo R., Gao G., Ji J., Zha S.,
Lan L., Liang H., Xu D.;
"Interactome analysis identifies a new paralogue of XRCC4 in non-
homologous end joining DNA repair pathway.";
Nat. Commun. 6:6233-6233(2015).
[14]
SUBUNIT.
PubMed=25574025; DOI=10.1126/science.1261971;
Ochi T., Blackford A.N., Coates J., Jhujh S., Mehmood S., Tamura N.,
Travers J., Wu Q., Draviam V.M., Robinson C.V., Blundell T.L.,
Jackson S.P.;
"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to
promote DNA double-strand break repair.";
Science 347:185-188(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 748-784 IN COMPLEX WITH
XRCC4.
PubMed=11702069; DOI=10.1038/nsb725;
Sibanda B.L., Critchlow S.E., Begun J., Pei X.Y., Jackson S.P.,
Blundell T.L., Pellegrini L.;
"Crystal structure of an Xrcc4-DNA ligase IV complex.";
Nat. Struct. Biol. 8:1015-1019(2001).
[16]
STRUCTURE BY NMR OF 654-759.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first BRCT domain of human DNA ligase IV.";
Submitted (DEC-2006) to the PDB data bank.
[17]
VARIANT LEUKEMIA HIS-278.
PubMed=10395545; DOI=10.1016/S0960-9822(99)80311-X;
Riballo E., Critchlow S.E., Teo S.-H., Doherty A.J., Priestley A.,
Broughton B.C., Kysela B., Beamish H., Plowman N., Arlett C.F.,
Lehmann A.R., Jackson S.P., Jeggo P.A.;
"Identification of a defect in DNA ligase IV in a radiosensitive
leukaemia patient.";
Curr. Biol. 9:699-702(1999).
[18]
CHARACTERIZATION OF VARIANT HIS-278.
PubMed=11349135; DOI=10.1074/jbc.M103866200;
Riballo E., Doherty A.J., Dai Y., Stiff T., Oettinger M.A.,
Jeggo P.A., Kysela B.;
"Cellular and biochemical impact of a mutation in DNA ligase IV
conferring clinical radiosensitivity.";
J. Biol. Chem. 276:31124-31132(2001).
[19]
VARIANTS LIG4S HIS-278 AND GLU-469.
PubMed=11779494; DOI=10.1016/S1097-2765(01)00408-7;
O'Driscoll M., Cerosaletti K.M., Girard P.-M., Dai Y., Stumm M.,
Kysela B., Hirsch B., Gennery A., Palmer S.E., Seidel J., Gatti R.A.,
Varon R., Oettinger M.A., Neitzel H., Jeggo P.A., Concannon P.;
"DNA ligase IV mutations identified in patients exhibiting
developmental delay and immunodeficiency.";
Mol. Cell 8:1175-1185(2001).
[20]
VARIANTS VAL-3 AND ILE-9, AND ASSOCIATION WITH RESISTANCE TO MULTIPLE
MYELOMA.
PubMed=12471202; DOI=10.1136/jmg.39.12.900;
Roddam P.L., Rollinson S., O'Driscoll M., Jeggo P.A., Jack A.,
Morgan G.J.;
"Genetic variants of NHEJ DNA ligase IV can affect the risk of
developing multiple myeloma, a tumour characterised by aberrant class
switch recombination.";
J. Med. Genet. 39:900-905(2002).
[21]
VARIANT RSSCID GLN-433 DEL.
PubMed=16357942; DOI=10.1172/JCI26121;
van der Burg M., van Veelen L.R., Verkaik N.S., Wiegant W.W.,
Hartwig N.G., Barendregt B.H., Brugmans L., Raams A., Jaspers N.G.J.,
Zdzienicka M.Z., van Dongen J.J.M., van Gent D.C.;
"A new type of radiosensitive T-B-NK(+) severe combined
immunodeficiency caused by a LIG4 mutation.";
J. Clin. Invest. 116:137-145(2006).
[22]
VARIANT PRO-774.
PubMed=25728776; DOI=10.1016/j.ajhg.2015.01.013;
Murray J.E., van der Burg M., Ijspeert H., Carroll P., Wu Q., Ochi T.,
Leitch A., Miller E.S., Kysela B., Jawad A., Bottani A., Brancati F.,
Cappa M., Cormier-Daire V., Deshpande C., Faqeih E.A., Graham G.E.,
Ranza E., Blundell T.L., Jackson A.P., Stewart G.S., Bicknell L.S.;
"Mutations in the NHEJ component XRCC4 cause primordial dwarfism.";
Am. J. Hum. Genet. 96:412-424(2015).
-!- FUNCTION: Efficiently joins single-strand breaks in a double-
stranded polydeoxynucleotide in an ATP-dependent reaction.
Involved in DNA non-homologous end joining (NHEJ) required for
double-strand break repair and V(D)J recombination. The LIG4-XRCC4
complex is responsible for the NHEJ ligation step, and XRCC4
enhances the joining activity of LIG4. Binding of the LIG4-XRCC4
complex to DNA ends is dependent on the assembly of the DNA-
dependent protein kinase complex DNA-PK to these DNA ends.
{ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:9809069}.
-!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
AMP + diphosphate. {ECO:0000255|PROSITE-ProRule:PRU10135}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with XRCC4. The LIG4-XRCC4 complex has probably
a 1:2 stoichiometry. The LIG4-XRCC4 complex associates in a DNA-
dependent manner with the DNA-PK complex composed of PRKDC,
XRCC6/Ku70 and XRCC5/Ku86 to form the core non-homologous end
joining (NHEJ) complex. Additional components of the NHEJ complex
include NHEJ1/XLF and PAXX. Interacts with APLF.
{ECO:0000269|PubMed:10854421, ECO:0000269|PubMed:11702069,
ECO:0000269|PubMed:12547193, ECO:0000269|PubMed:17396150,
ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504,
ECO:0000269|PubMed:25941166, ECO:0000269|PubMed:9259561,
ECO:0000269|PubMed:9809069}.
-!- INTERACTION:
Q8IW19:APLF; NbExp=2; IntAct=EBI-847896, EBI-1256044;
Q96SD1:DCLRE1C; NbExp=16; IntAct=EBI-847896, EBI-11694104;
Q9H9Q4:NHEJ1; NbExp=4; IntAct=EBI-847896, EBI-847807;
Q13426:XRCC4; NbExp=13; IntAct=EBI-847896, EBI-717592;
Q13426-2:XRCC4; NbExp=11; IntAct=EBI-847896, EBI-15891375;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Testis, thymus, prostate and heart.
-!- DISEASE: LIG4 syndrome (LIG4S) [MIM:606593]: Characterized by
immunodeficiency and developmental and growth delay. Patients
display unusual facial features, microcephaly, growth and/or
developmental delay, pancytopenia, and various skin abnormalities.
{ECO:0000269|PubMed:11779494}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Severe combined immunodeficiency autosomal recessive T-
cell-negative/B-cell-negative/NK-cell-positive with sensitivity to
ionizing radiation (RSSCID) [MIM:602450]: A form of severe
combined immunodeficiency, a genetically and clinically
heterogeneous group of rare congenital disorders characterized by
impairment of both humoral and cell-mediated immunity, leukopenia,
and low or absent antibody levels. Patients present in infancy
with recurrent, persistent infections by opportunistic organisms.
The common characteristic of all types of SCID is absence of T-
cell-mediated cellular immunity due to a defect in T-cell
development. Individuals affected by RS-SCID show defects in the
DNA repair machinery necessary for coding joint formation and the
completion of V(D)J recombination. A subset of cells from such
patients show increased radiosensitivity.
{ECO:0000269|PubMed:16357942}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL77435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA58467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=LIG4base; Note=LIG4 mutation db;
URL="http://structure.bmc.lu.se/idbase/LIG4base/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/lig4/";
-!- WEB RESOURCE: Name=Wikipedia; Note=DNA ligase entry;
URL="https://en.wikipedia.org/wiki/DNA_ligase";
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EMBL; X83441; CAA58467.1; ALT_INIT; mRNA.
EMBL; AF479264; AAL77435.1; ALT_INIT; Genomic_DNA.
EMBL; AL157762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037491; AAH37491.1; -; mRNA.
CCDS; CCDS9508.1; -.
PIR; I37079; I37079.
RefSeq; NP_001091738.1; NM_001098268.1.
RefSeq; NP_001317524.1; NM_001330595.1.
RefSeq; NP_002303.2; NM_002312.3.
RefSeq; NP_996820.1; NM_206937.1.
RefSeq; XP_005254113.1; XM_005254056.1.
RefSeq; XP_005254114.1; XM_005254057.4.
RefSeq; XP_005254115.1; XM_005254058.3.
RefSeq; XP_006720014.1; XM_006719951.3.
RefSeq; XP_006720015.1; XM_006719952.1.
RefSeq; XP_011519393.1; XM_011521091.2.
RefSeq; XP_011519394.1; XM_011521092.2.
RefSeq; XP_016876058.1; XM_017020569.1.
RefSeq; XP_016876059.1; XM_017020570.1.
RefSeq; XP_016876060.1; XM_017020571.1.
RefSeq; XP_016876062.1; XM_017020573.1.
UniGene; Hs.166091; -.
PDB; 1IK9; X-ray; 2.30 A; C=748-784.
PDB; 2E2W; NMR; -; A=654-759.
PDB; 3II6; X-ray; 2.40 A; X/Y=654-911.
PDB; 3VNN; X-ray; 2.90 A; A=268-406.
PDB; 3W1B; X-ray; 2.40 A; A=1-609.
PDB; 3W1G; X-ray; 2.55 A; A=1-609.
PDB; 3W5O; X-ray; 2.84 A; A/B=1-609.
PDB; 4HTO; X-ray; 2.81 A; A=1-240.
PDB; 4HTP; X-ray; 2.25 A; A/B=1-240.
PDBsum; 1IK9; -.
PDBsum; 2E2W; -.
PDBsum; 3II6; -.
PDBsum; 3VNN; -.
PDBsum; 3W1B; -.
PDBsum; 3W1G; -.
PDBsum; 3W5O; -.
PDBsum; 4HTO; -.
PDBsum; 4HTP; -.
ProteinModelPortal; P49917; -.
SMR; P49917; -.
BioGrid; 110169; 130.
CORUM; P49917; -.
DIP; DIP-37958N; -.
IntAct; P49917; 11.
MINT; MINT-3018022; -.
STRING; 9606.ENSP00000349393; -.
iPTMnet; P49917; -.
PhosphoSitePlus; P49917; -.
BioMuta; LIG4; -.
DMDM; 88911290; -.
EPD; P49917; -.
MaxQB; P49917; -.
PaxDb; P49917; -.
PeptideAtlas; P49917; -.
PRIDE; P49917; -.
DNASU; 3981; -.
Ensembl; ENST00000356922; ENSP00000349393; ENSG00000174405.
Ensembl; ENST00000405925; ENSP00000385955; ENSG00000174405.
Ensembl; ENST00000442234; ENSP00000402030; ENSG00000174405.
Ensembl; ENST00000611712; ENSP00000484288; ENSG00000174405.
GeneID; 3981; -.
KEGG; hsa:3981; -.
UCSC; uc001vqn.4; human.
CTD; 3981; -.
DisGeNET; 3981; -.
EuPathDB; HostDB:ENSG00000174405.13; -.
GeneCards; LIG4; -.
HGNC; HGNC:6601; LIG4.
HPA; HPA001334; -.
MalaCards; LIG4; -.
MIM; 601837; gene.
MIM; 602450; phenotype.
MIM; 606593; phenotype.
neXtProt; NX_P49917; -.
OpenTargets; ENSG00000174405; -.
Orphanet; 235; Dubowitz syndrome.
Orphanet; 99812; LIG4 syndrome.
Orphanet; 39041; Omenn syndrome.
PharmGKB; PA30375; -.
eggNOG; KOG0966; Eukaryota.
eggNOG; COG1793; LUCA.
GeneTree; ENSGT00860000133881; -.
HOGENOM; HOG000007831; -.
HOVERGEN; HBG005516; -.
InParanoid; P49917; -.
KO; K10777; -.
OMA; HMCPSTK; -.
OrthoDB; EOG091G03K0; -.
PhylomeDB; P49917; -.
TreeFam; TF312980; -.
BRENDA; 6.5.1.1; 2681.
Reactome; R-HSA-164843; 2-LTR circle formation.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
SignaLink; P49917; -.
SIGNOR; P49917; -.
ChiTaRS; LIG4; human.
EvolutionaryTrace; P49917; -.
GeneWiki; LIG4; -.
GenomeRNAi; 3981; -.
PRO; PR:P49917; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000174405; -.
CleanEx; HS_LIG4; -.
ExpressionAtlas; P49917; baseline and differential.
Genevisible; P49917; HS.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0032807; C:DNA ligase IV complex; IMP:UniProtKB.
GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IC:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003910; F:DNA ligase (ATP) activity; IDA:UniProtKB.
GO; GO:0003909; F:DNA ligase activity; IDA:UniProtKB.
GO; GO:0016874; F:ligase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
GO; GO:0071285; P:cellular response to lithium ion; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
GO; GO:0006266; P:DNA ligation; IDA:UniProtKB.
GO; GO:0051102; P:DNA ligation involved in DNA recombination; ISS:UniProtKB.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; IMP:BHF-UCL.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0033152; P:immunoglobulin V(D)J recombination; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IDA:UniProtKB.
GO; GO:2001252; P:positive regulation of chromosome organization; IMP:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0002328; P:pro-B cell differentiation; ISS:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0010165; P:response to X-ray; IMP:UniProtKB.
GO; GO:0000012; P:single strand break repair; IDA:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0033153; P:T cell receptor V(D)J recombination; ISS:UniProtKB.
GO; GO:0033151; P:V(D)J recombination; IDA:UniProtKB.
CDD; cd00027; BRCT; 2.
Gene3D; 1.10.3260.10; -; 1.
Gene3D; 3.40.50.10190; -; 2.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR000977; DNA_ligase_ATP-dep.
InterPro; IPR012309; DNA_ligase_ATP-dep_C.
InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
InterPro; IPR012308; DNA_ligase_ATP-dep_N.
InterPro; IPR021536; DNA_ligase_IV_dom.
InterPro; IPR036599; DNA_ligase_N_sf.
InterPro; IPR029710; LIG4.
InterPro; IPR012340; NA-bd_OB-fold.
PANTHER; PTHR10459:SF7; PTHR10459:SF7; 2.
Pfam; PF00533; BRCT; 2.
Pfam; PF04679; DNA_ligase_A_C; 1.
Pfam; PF01068; DNA_ligase_A_M; 1.
Pfam; PF04675; DNA_ligase_A_N; 1.
Pfam; PF11411; DNA_ligase_IV; 1.
SMART; SM00292; BRCT; 2.
SUPFAM; SSF117018; SSF117018; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52113; SSF52113; 2.
TIGRFAMs; TIGR00574; dnl1; 1.
PROSITE; PS50172; BRCT; 2.
PROSITE; PS00697; DNA_LIGASE_A1; 1.
PROSITE; PS00333; DNA_LIGASE_A2; 1.
PROSITE; PS50160; DNA_LIGASE_A3; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell cycle; Cell division;
Complete proteome; Direct protein sequencing; Disease mutation;
DNA damage; DNA recombination; DNA repair; DNA replication; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Polymorphism;
Reference proteome; Repeat; SCID.
CHAIN 1 911 DNA ligase 4.
/FTId=PRO_0000059576.
DOMAIN 654 743 BRCT 1. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 808 911 BRCT 2. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
ACT_SITE 273 273 N6-AMP-lysine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10135}.
METAL 331 331 Magnesium 1. {ECO:0000255}.
METAL 427 427 Magnesium 2. {ECO:0000255}.
BINDING 271 271 ATP. {ECO:0000250}.
BINDING 278 278 ATP. {ECO:0000250}.
BINDING 293 293 ATP. {ECO:0000250}.
BINDING 432 432 ATP. {ECO:0000250}.
BINDING 443 443 ATP. {ECO:0000250}.
BINDING 449 449 ATP. {ECO:0000250}.
VARIANT 3 3 A -> V (associated with resistance to
multiple myeloma; dbSNP:rs1805389).
{ECO:0000269|PubMed:12471202}.
/FTId=VAR_029352.
VARIANT 9 9 T -> I (associated with resistance to
multiple myeloma; dbSNP:rs1805388).
{ECO:0000269|PubMed:12471202}.
/FTId=VAR_033884.
VARIANT 62 62 D -> H (in dbSNP:rs3093763).
/FTId=VAR_029353.
VARIANT 231 231 P -> S (in dbSNP:rs3093765).
{ECO:0000269|Ref.2}.
/FTId=VAR_018808.
VARIANT 278 278 R -> H (in LIG4S and leukemia; impairs
activity; dbSNP:rs104894421).
{ECO:0000269|PubMed:10395545,
ECO:0000269|PubMed:11349135,
ECO:0000269|PubMed:11779494}.
/FTId=VAR_012774.
VARIANT 433 433 Missing (in RSSCID).
{ECO:0000269|PubMed:16357942}.
/FTId=VAR_044123.
VARIANT 461 461 E -> G (in dbSNP:rs2232640).
/FTId=VAR_044124.
VARIANT 469 469 G -> E (in LIG4S; dbSNP:rs104894420).
{ECO:0000269|PubMed:11779494}.
/FTId=VAR_012775.
VARIANT 539 539 L -> F (in dbSNP:rs3742212).
/FTId=VAR_016771.
VARIANT 658 658 I -> V (in dbSNP:rs2232641).
/FTId=VAR_016772.
VARIANT 774 774 L -> P (found in a patient with
microcephalic primordial dwarfism;
unknown pathological significance).
{ECO:0000269|PubMed:25728776}.
/FTId=VAR_075826.
VARIANT 857 857 A -> T (in dbSNP:rs2232642).
{ECO:0000269|Ref.2}.
/FTId=VAR_016773.
CONFLICT 246 246 F -> S (in Ref. 1; CAA58467).
{ECO:0000305}.
HELIX 10 12 {ECO:0000244|PDB:4HTP}.
HELIX 16 28 {ECO:0000244|PDB:4HTP}.
HELIX 32 53 {ECO:0000244|PDB:4HTP}.
TURN 54 56 {ECO:0000244|PDB:4HTP}.
HELIX 65 71 {ECO:0000244|PDB:4HTP}.
HELIX 73 75 {ECO:0000244|PDB:4HTP}.
HELIX 86 96 {ECO:0000244|PDB:4HTP}.
HELIX 104 110 {ECO:0000244|PDB:4HTP}.
HELIX 125 133 {ECO:0000244|PDB:4HTP}.
TURN 134 136 {ECO:0000244|PDB:3W1B}.
HELIX 145 160 {ECO:0000244|PDB:4HTP}.
HELIX 164 176 {ECO:0000244|PDB:4HTP}.
HELIX 180 191 {ECO:0000244|PDB:4HTP}.
HELIX 200 207 {ECO:0000244|PDB:4HTP}.
HELIX 211 218 {ECO:0000244|PDB:4HTP}.
HELIX 221 227 {ECO:0000244|PDB:4HTP}.
STRAND 250 253 {ECO:0000244|PDB:3W1B}.
HELIX 256 258 {ECO:0000244|PDB:3W1B}.
HELIX 259 262 {ECO:0000244|PDB:3W1B}.
TURN 263 265 {ECO:0000244|PDB:3W1B}.
STRAND 268 272 {ECO:0000244|PDB:3W1B}.
STRAND 276 284 {ECO:0000244|PDB:3W1B}.
STRAND 287 292 {ECO:0000244|PDB:3W1B}.
HELIX 299 302 {ECO:0000244|PDB:3W1B}.
STRAND 308 311 {ECO:0000244|PDB:3W1B}.
HELIX 312 315 {ECO:0000244|PDB:3W1B}.
HELIX 316 318 {ECO:0000244|PDB:3W1B}.
STRAND 324 336 {ECO:0000244|PDB:3W1B}.
TURN 337 340 {ECO:0000244|PDB:3W1B}.
STRAND 341 343 {ECO:0000244|PDB:3W1B}.
HELIX 351 356 {ECO:0000244|PDB:3W1B}.
STRAND 359 372 {ECO:0000244|PDB:3W1B}.
STRAND 378 380 {ECO:0000244|PDB:3VNN}.
HELIX 382 392 {ECO:0000244|PDB:3W1B}.
TURN 397 399 {ECO:0000244|PDB:3W1B}.
STRAND 400 402 {ECO:0000244|PDB:3W1B}.
STRAND 405 408 {ECO:0000244|PDB:3W1B}.
HELIX 411 423 {ECO:0000244|PDB:3W1B}.
STRAND 429 432 {ECO:0000244|PDB:3W1B}.
STRAND 443 450 {ECO:0000244|PDB:3W1B}.
HELIX 458 460 {ECO:0000244|PDB:3W1B}.
STRAND 462 471 {ECO:0000244|PDB:3W1B}.
HELIX 474 478 {ECO:0000244|PDB:3W1B}.
STRAND 479 488 {ECO:0000244|PDB:3W1B}.
STRAND 500 507 {ECO:0000244|PDB:3W1B}.
HELIX 513 522 {ECO:0000244|PDB:3W1B}.
HELIX 523 525 {ECO:0000244|PDB:3W1B}.
STRAND 536 539 {ECO:0000244|PDB:3W1G}.
STRAND 546 548 {ECO:0000244|PDB:3W1B}.
HELIX 551 553 {ECO:0000244|PDB:3W1B}.
STRAND 556 560 {ECO:0000244|PDB:3W1B}.
STRAND 562 566 {ECO:0000244|PDB:3W1B}.
STRAND 568 570 {ECO:0000244|PDB:3W1B}.
STRAND 573 578 {ECO:0000244|PDB:3W1B}.
STRAND 580 584 {ECO:0000244|PDB:3W1B}.
HELIX 590 592 {ECO:0000244|PDB:3W1B}.
HELIX 596 603 {ECO:0000244|PDB:3W1B}.
TURN 658 661 {ECO:0000244|PDB:3II6}.
STRAND 663 666 {ECO:0000244|PDB:3II6}.
STRAND 671 673 {ECO:0000244|PDB:2E2W}.
HELIX 675 684 {ECO:0000244|PDB:3II6}.
STRAND 687 692 {ECO:0000244|PDB:2E2W}.
STRAND 697 701 {ECO:0000244|PDB:3II6}.
HELIX 707 714 {ECO:0000244|PDB:3II6}.
HELIX 723 732 {ECO:0000244|PDB:3II6}.
HELIX 740 742 {ECO:0000244|PDB:3II6}.
STRAND 743 745 {ECO:0000244|PDB:3II6}.
HELIX 748 753 {ECO:0000244|PDB:3II6}.
TURN 754 757 {ECO:0000244|PDB:3II6}.
STRAND 764 767 {ECO:0000244|PDB:1IK9}.
HELIX 771 779 {ECO:0000244|PDB:1IK9}.
HELIX 789 802 {ECO:0000244|PDB:3II6}.
HELIX 809 811 {ECO:0000244|PDB:3II6}.
TURN 812 815 {ECO:0000244|PDB:3II6}.
STRAND 817 820 {ECO:0000244|PDB:3II6}.
STRAND 823 825 {ECO:0000244|PDB:3II6}.
HELIX 829 831 {ECO:0000244|PDB:3II6}.
HELIX 837 847 {ECO:0000244|PDB:3II6}.
STRAND 851 855 {ECO:0000244|PDB:3II6}.
STRAND 862 865 {ECO:0000244|PDB:3II6}.
HELIX 872 880 {ECO:0000244|PDB:3II6}.
STRAND 887 890 {ECO:0000244|PDB:3II6}.
HELIX 892 899 {ECO:0000244|PDB:3II6}.
HELIX 906 908 {ECO:0000244|PDB:3II6}.
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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