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Information on EC 6.5.1.1 - DNA ligase (ATP) and Organism(s) Homo sapiens and UniProt Accession P18858

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EC Tree
IUBMB Comments
The enzyme catalyses the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. RNA can also act as substrate, to some extent. cf. EC 6.5.1.2, DNA ligase (NAD+), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP).
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Homo sapiens
UNIPROT: P18858
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
dna ligase, dna repair enzyme, dna ligase i, t4 dna ligase, dna ligase iv, dna ligase iii, ligase 1, dna ligase ii, polynucleotide ligase, dna ligase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA ligase
-
DNA ligase I
-
DNA ligase III
-
DNA ligase IV
-
ATP-dependent DNA ligase
-
-
ATP-dependent DNA ligase I
-
-
Deoxyribonucleate ligase
-
-
-
-
Deoxyribonucleic acid joinase
-
-
-
-
Deoxyribonucleic acid ligase
-
-
-
-
Deoxyribonucleic acid repair enzyme
-
-
-
-
Deoxyribonucleic acid-joining enzyme
-
-
-
-
Deoxyribonucleic joinase
-
-
-
-
Deoxyribonucleic ligase
-
-
-
-
Deoxyribonucleic repair enzyme
-
-
-
-
Deoxyribonucleic-joining enzyme
-
-
-
-
DNA joinase
-
-
-
-
DNA ligase
-
-
-
-
DNA ligase 1
-
-
DNA ligase 4
-
DNA ligase I
DNA ligase II
-
-
-
-
DNA ligase III
DNA ligase IIIalpha
-
-
DNA ligase IV
DNA ligase IV homolog
-
-
-
-
DNA ligase IV-XRCC4 complex
-
-
DNA ligase IV/XRCC4 complex
-
plays a central role in DNA double-strand break repair by non-homologous end joining
DNA ligase IV/XRCC4/XLF complex
-
-
DNA ligase V
-
-
DNA repair enzyme
-
-
-
-
DNA-joining enzyme
-
-
-
-
L3BRCT
C-terminal ligase III-alpha BRCT domain
Lig I
-
-
Lig III
-
-
Lig(Tk)
-
-
-
-
Lig3
-
-
Lig3alpha
-
-
LigA
-
-
ligase III-alpha
-
Pfu DNA ligase
-
-
-
-
Polydeoxyribonucleotide synthase (ATP)
-
-
-
-
Polydeoxyribonucleotide synthase [ATP]
-
-
-
-
Polynucleotide ligase
-
-
-
-
Sealase
-
-
-
-
X4L4
-
-
XRCC4-DNA ligase IV complex
-
the X4L4 complex contains two subunits of XRCC4 and one subunit of ligase IV
SYSTEMATIC NAME
IUBMB Comments
poly(deoxyribonucleotide)-3'-hydroxyl:5'-phospho-poly(deoxyribonucleotide) ligase (ATP)
The enzyme catalyses the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. RNA can also act as substrate, to some extent. cf. EC 6.5.1.2, DNA ligase (NAD+), EC 6.5.1.6, DNA ligase (ATP or NAD+), and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP).
CAS REGISTRY NUMBER
COMMENTARY hide
9015-85-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)m+n
show the reaction diagram
-
-
-
?
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)n+m
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)m+n
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)n+m
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)n+m
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)m+n
show the reaction diagram
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + diphosphate + (deoxyribonucleotide)n+m
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
3fold stimulation at 70 mM KCl, 4fold stimulation at 150 mM KCl
Mn2+
-
Mn2+ cannot replace Mg2+ in activation
Zn2+
-
the enzyme contains a PARP-like zinc finger
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-hydroxyphenyl)(4-hydroxyphenyl)methanone
50.7% inhibition at 0.1 mM
2,3-dioxo-2,3-dihydro-1H-indole-7-carboxylic acid
59.3% inhibition at 0.1 mM
2-[(3,5-dibromo-4-methylphenyl)amino]-N'-[(1Z)-(2-hydroxy-5-nitrophenyl)methylidene]acetohydrazide
78.3% inhibition at 0.1 mM
3-amino-2-[[(1E)-phenylmethylidene]amino]-5-sulfanylphenol
68.8% inhibition at 0.1 mM
3-[(4-bromophenyl)sulfonyl]-N-[2-(4-sulfamoylphenyl)ethyl]propanamide
53.4% inhibition at 0.1 mM
4-([[(4-carboxy-5-methylfuran-2-yl)methyl]sulfanyl]methyl)-5-methylfuran-2-carboxylic acid
91% inhibition at 0.1 mM
4-chloro-5-[(2Z)-2-[(4-hydroxy-3-nitrophenyl)methylidene]hydrazino]pyridazin-3(2H)-one
59.8% inhibition at 0.1 mM
5-(methylsulfanyl)thiophene-2-carboxylic acid
60.5% inhibition at 0.1 mM
7-(4-methoxyphenyl)pteridine-2,4-diol
52.5% inhibition at 0.1 mM
[(7-chloro-4-nitro-2,1,3-benzoxadiazol-5-yl)sulfanyl]acetic acid
60.6% inhibition at 0.1 mM
(1S,3S)-3-acetyl-3,5,10-trihydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-alpha-L-lyxo-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl 3-(2-cyanopiperidin-1-yl)-2,3,6-trideoxy-alpha-D-glycero-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-2,6-dideoxy-beta-L-threo-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-beta-L-threo-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-4-amino-2,4,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-2,6-dideoxy-beta-L-threo-hexopyranoside
-
-
(3S)-3,5,12-trihydroxy-3-(hydroxyacetyl)-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3-acetyl-3,5,10-trihydroxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3,4-diamino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-4-amino-2,4,6-trideoxy-alpha-D-threo-hexopyranoside
-
-
(3S)-3-acetyl-3,5,12-trihydroxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-2,6-dideoxy-beta-L-threo-hexopyranoside
-
-
(3S)-3-acetyl-3,5,12-trihydroxy-6,11-dioxo-1,2,3,4,5a,6,11,11a-octahydrotetracen-1-yl-3-amino-2,3,6-trideoxy-alpha-D-erythro-hexopyranoside
-
-
(8S)-10-[[(2R,4R)-4-amino-6-methyltetrahydro-2H-pyran-2-yl]oxy]-6,8,11-trihydroxy-8-(hydroxyacetyl)-1-methoxy-5a,7,8,9,10,11a-hexahydrotetracene-5,12-dione
-
-
(8S)-10-[[(2S,4S,5S)-4-amino-5-iodo-6-methyltetrahydro-2H-pyran-2-yl]oxy]-6,8,11-trihydroxy-8-(hydroxyacetyl)-1-methoxy-5a,7,8,9,10,11a-hexahydrotetracene-5,12-dione
-
-
(8S)-8-acetyl-10-[[(2R,4R)-4-amino-6-methyltetrahydro-2H-pyran-2-yl]oxy]-6,8,11-trihydroxy-1-methoxy-5a,7,8,9,10,11a-hexahydrotetracene-5,12-dione
-
-
(9S)-7-[[(2R,4R)-4-amino-6-methyltetrahydro-2H-pyran-2-yl]oxy]-6,9,11-trihydroxy-9-(hydroxyacetyl)-5a,7,8,9,10,11a-hexahydrotetracene-5,12-dione
-
-
(9S)-9-acetyl-7-[[(2S,5R)-5-amino-6-methyltetrahydro-2H-pyran-2-yl]oxy]-6,9,11-trihydroxy-5a,7,8,9,10,11a-hexahydrotetracene-5,12-dione
-
-
(E)-2-(3,5-dibromo-4-methylphenylamino)-N'-(2-hydroxy-5-nitrobenzylidene)acetohydrazide
-
inhibits Lig1 and Lig3
12-(6-piperidin-1-ylhexyl)-7,12-dihydro-6H-[1]benzothiepino[5,4-b]indole
-
-
2-[(3,5-dibromo-4-methylphenyl)amino]-N'-[(1E)-(2-hydroxy-5-nitrophenyl)methylidene]acetohydrazide
-
-
4-chloro-5-[(2E)-2-(4-hydroxy-3-nitrobenzylidene)hydrazinyl]pyridazin-3(2H)-one
-
specific for Lig1
4-chloro-5-[(2E)-2-[(4-hydroxy-3-nitrophenyl)methylidene]hydrazino]pyridazin-3(2H)-one
-
-
4-demethyl-6-deoxydaunorubicin
-
-
6-amino-5-[[(1E)-phenylmethylidene]amino]-2-sulfanylpyrimidin-4-ol
-
-
9-beta-D-Arabinofuranosyl-2-fluoroadenine triphosphate
-
0.08 mM, 90% inhibition
actinomycin
-
-
aleuritolic acid
-
-
Anthracycline derivatives
apurine/apyrimidinic endonuclease I
-
inhibition if the DNA ligase I substrate has a tetrahydrofuran residue on the 5'-downstream primer of a nick, simulating a reduced abasic site
-
Ca2+
-
CaCl2 inhibits Mg2+-catalyzed reaction
CdCl2
-
0.04 mM, complete inhibition
chelerythrine chloride
diphosphate
-
-
Distamycin
-
and derivatives, inhibit human DNA ligase I and rat DNA ligase I and III in the poly[d(A-T)] joining assay
doxorubicin
EDTA
-
EDTA rapidly inactivates all LIG1-catalyzed reactions
Ethidium bromide
-
-
Fagaronine chloride
Fulvoplumierin
-
-
Mn2+
-
MnCl2 inhibits Mg2+-catalyzed reaction
morin
-
-
myricetin
-
-
N-[5-([5-[(3-amino-3-iminopropyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]-4-(formylamino)-1-methyl-1H-pyrrole-2-carboxamide hydrochloride
-
distamycin A
N-[5-([5-[(3-amino-3-iminopropyl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]-4-[([4-[bis(2-chloroethyl)amino]phenyl]carbonyl)amino]-1-methyl-1H-pyrrole-2-carboxamide hydrochloride
-
FCE-24517
Nitidine chloride
oleanolic acid
-
-
Protein inhibitor
-
Protolichesterinic acid
-
-
Replication factor C
-
LigI interacts with and is inhibited by replication factor C
-
sanguinarine
-
low active inhibitor
Sanguinarine nitrate
-
-
Swertifrancheside
ursolic acid
-
-
ZnCl2
-
0.8 mM, complete inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apurine/apyrimidinic endonuclease I
-
stimulation of DNA ligase activity, inhibition if the DNA ligase I substrate has a tetrahydrofuran residue on the 5'-downstream primer of a nick, simulating a reduced abasic site
-
dithiothreitol
-
required for optimal activity
proliferating cell nuclear antigen
-
replication protein
-
-
-
replication protein A
-
approx. 15fold stimulation of DNA ligase I
-
XLF-Cernunnos
-
a component of the DNA ligase IV-XRCC4 complex, which functions during DNA non-homologous end joining and stimulates ligase IV re-adenylation following ligation
-
XRCC4
-
stimulates DNA ligase activity primarily through direct structure interaction with DNA ligase
-
additional information
-
LigI activity is strongly linked to proliferating cell nuclear antigen, the interaction between both factors is essential for the recruitment of LigI to replication foci and sites of DNA damage, replication efficiency is reduced on CTG/CAG templates with a defective LigI
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000034 - 0.012
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026 - 0.74
ATP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
(2-hydroxyphenyl)(4-hydroxyphenyl)methanone
Homo sapiens
-
0.004
2,3-dioxo-2,3-dihydro-1H-indole-7-carboxylic acid
Homo sapiens
-
0.018
3-[(4-bromophenyl)sulfonyl]-N-[2-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens
-
0.0006
4-([[(4-carboxy-5-methylfuran-2-yl)methyl]sulfanyl]methyl)-5-methylfuran-2-carboxylic acid
Homo sapiens
-
0.01
5-(methylsulfanyl)thiophene-2-carboxylic acid
Homo sapiens
-
0.025
7-(4-methoxyphenyl)pteridine-2,4-diol
Homo sapiens
-
0.013
[(7-chloro-4-nitro-2,1,3-benzoxadiazol-5-yl)sulfanyl]acetic acid
Homo sapiens
-
0.205
aleuritolic acid
Homo sapiens
-
-
0.226
chelerythrine chloride
Homo sapiens
-
-
0.027
Fagaronine chloride
Homo sapiens
-
-
0.357
Fulvoplumierin
Homo sapiens
-
-
0.236
morin
Homo sapiens
-
-
0.091
myricetin
Homo sapiens
-
-
0.069
Nitidine chloride
Homo sapiens
-
-
0.216
oleanolic acid
Homo sapiens
-
-
0.387
Protolichesterinic acid
Homo sapiens
-
-
0.322
sanguinarine
Homo sapiens
-
-
0.105
Swertifrancheside
Homo sapiens
-
-
0.216
ursolic acid
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
-
approximately 70% of maximal activity at pH 7.0 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
20°C: 55% of maximal activity, 37°C: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
studies carried out in thymidine kinase 1-deficient human osteosarcoma cell line (143B [TK-])
Manually annotated by BRENDA team
-
heteroploid
Manually annotated by BRENDA team
-
adenovirus type 2-infected
Manually annotated by BRENDA team
-
activity is much lower in resting lymphocytes than in actively growing cells
Manually annotated by BRENDA team
-
cell lines NGP and SK-N-Be
Manually annotated by BRENDA team
-
MiaPaCa cell line
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DNLI1_HUMAN
919
0
101736
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
glycerol density gradient sedimentation
190000
-
and a lower MW form of MW 95000, gel filtration
44000
-
x * 44000, DNA ligase V, SDS-PAGE
95000
-
DNA ligase II, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphorylation of human DNA ligase I regulates its interaction with replication factor C and its participation in DNA replication and DNA repair
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of human DNA ligase I bound to nicked, 5'-adenylated DNA. The crystal structure of human DNA ligase I complexed to DNA demonstrates that the enzyme encircles its DNA substrate
in complex with the AMP-DNA reaction intermediate
-
LigIII in complex with 22-mer nicked DNA, hanging drop vapor diffusion method, using 1.8 M ammonium sulfate and 0.1 M sodium acetate (pH 5.6)
-
LigIV in complex with XRCC4
-
X1BRCTb complexed with L3BRCT
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F717L
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
G468A
-
mutant enzyme shows residual adenylate complex formation at high protein concentrations, mutant complex has a lower affinity for ATP compared to wild-type complex
G468E
-
mutant DNA ligase IV/Xrrc4 complex is poorly expressed, mutation completely abolishes adenylate complex formation, mutant complex has no ligation activity
G469A
-
mutant enzyme shows residual adenylate complex formation
G469E
-
mutant DNA ligase IV/Xrrc4 complex is poorly expressed, mutation completely abolishes adenylate complex formation, mutant complex has no ligation activity
G712A
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, complements Escherichia coli lig mutant
K323E
-
the mutant has significantly reduced blunt end DNA ligation activity (87% decrease in the initial velocity of blunt end DNA ligation compared to wild type enzyme), but has very little effect on DNA nick joining activity, the mutation selectively blocks zinc finger function
K323E/E265K
-
the mutations do not restore efficient blunt end DNA joining activity
K724E
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
K727G
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
K727R
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
P718A
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, complements Escherichia coli lig mutant
P718T
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, complements Escherichia coli lig mutant
p719G
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant, thermolabile mutant
R278H
-
the mutant form of ligase IV is severely impaired for formation of the ligase IV-adenylate and assesses DNA binding by XRCC4
R327E
-
the mutant is nearly devoid of blunt end joining activity, mimicking a deletion of the zinc finger
R327E/D262R
-
the mutations do not restore efficient blunt end DNA joining activity
R716G
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
R722Q
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, complements Escherichia coli lig mutant
R722V
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, complements Escherichia coli lig mutant
R724G
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
R771W
S714I
-
amino acid substitution within the conserved peptide of DNA ligase IIIbeta, does not complement Escherichia coli lig mutant
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DNA ligase IV depends on the partner protein XRCC4 for stability and activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol w/w, 3 mg/ml bovine serum albumin, stable for up to 7 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA ligase V
-
HiTrap nickel chelating column chromatography and Sephadex S200 gel filtration
-
immobilized metal affinity column chromatography and Superdex S75 gel filtration
multienzyme complex consisting of DNA polymerase alpha-primase, a 3',5'-exonuclease, DNA ligase I, RNase H, and topoisomerase I
-
Ni-NTA column chromatography and Q-Sepharose column chromatography
-
nickel-agarose bead chromatography, ion exchange chromatography, and gel filtration
-
recombinant DNA ligase I
-
recombinant DNA ligase III
-
recombinant DNA ligase IV-XRCC4 complex, metal-chelate Talon affinity resin, Mono Q
-
Sepharose column chromatography and hydroxyapatite column chromatography
-
Sepharose column chromatography, Source Q column chromatography, and Superdex 200 gel filtration
-
wild-type and mutant DNA ligase IV/Xrrc4 complexes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amino acid sequence of human DNA ligase I and enzyme from Schizosaccharomyces pombe are virtually identical in the region of the active site, although the two enzymes show only 44% overall identity. The sequence of DNA ligase II appears to be quite different from that of DNA ligase I
-
coexpression of DNA ligase IV-XRCC4 complex in Sf9 insect cells
-
DNA ligase I, III-alpha, III-beta, IV
-
DNA ligase II and IV. DNA ligase III and IV are encoded by distinct genes located on human chromosome 17q11.2-12 and 13q33-34
-
Escherichia coli-based coexpression system provides relatively high yields of the ligase IV/XRCC4 complex
expressed as His6-tagged protein in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli and in Sf9 insect cells
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21-DE3-RIL cells
expression in Saccharomyces cerevisiae
-
expression in Sf9 insect cells
-
expression of wild-type and mutant Xrcc4/DNA ligase IV complexes in insect cells
-
overexpression in Spodoptera frugiperda Sf9 insect cells infected with the recombinant baculovirus
-
the catalytic domain of human LIG1 (residues 232-919) is expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ectopic overexpression of competing LigIV fragments downregulates endogenous LigIV protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
a procedure for fast, sensitive and quantitative measurement of DNA ligase activity in crude cell extract
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindahl, T.; Barnes, D.E.
Mammalian DNA ligases
Annu. Rev. Biochem.
61
251-281
1992
Ambystoma mexicanum, Tequatrovirus T4, Bos taurus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mammalia, Pleurodeles sp., Rattus norvegicus, Schizosaccharomyces pombe, Vaccinia virus, Xenopus laevis
Manually annotated by BRENDA team
Tomkinson, A.E.; Levin, D.S.
Mammalian DNA ligases
BioEssays
19
893-901
1997
Bos taurus, Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens, Mammalia, Schizosaccharomyces pombe, Vaccinia virus, Xenopus laevis
Manually annotated by BRENDA team
Tsuruo, T.; Arens, M.; Padmanabhan, R.; Green, M.
Purification and properties of a DNA ligase from a soluble DNA replication complex
Biochim. Biophys. Acta
606
202-213
1980
Homo sapiens
Manually annotated by BRENDA team
Pedrali Noy, G.C.F.; Spadari, S; Ciarrocchi, G.; Pedrini, A.M.; Falaschi, A.
Two forms of the DNA ligase of human cells
Eur. J. Biochem.
39
343-351
1973
Homo sapiens
Manually annotated by BRENDA team
Saucier, J.M.; Laval, F.
DNA ligase activity in crude extracts of fibroblasts and lymphocytes
Biochem. Biophys. Res. Commun.
116
657-662
1983
Homo sapiens
Manually annotated by BRENDA team
Yang, S.; Becker, F.F.; Chan, J.Y.H.
Biochemical characterization of a protein inhibitor for DNA ligase I from human cells
Biochem. Biophys. Res. Commun.
191
1004-1013
1993
Tequatrovirus T4, Homo sapiens
Manually annotated by BRENDA team
Johnson, A.P.; Fairman, M.P.
The identification and purification of a novel mammalian DNA ligase
Mutat. Res.
383
205-212
1997
Homo sapiens
Manually annotated by BRENDA team
Montecucco, A.; Lestingi, M.; Rossignol, J.M.; Elder, R.H.; Ciarrocchi, G.
Lack of discrimination between DNA ligase I and III by two classes of inhibitors, anthracyclines and distamycin
Biochem. Pharmacol.
45
1536-1539
1993
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Gallina, A.; Rossi, F.; Milanesi, G.; Rossi, R.; Montecucco, A.; Ciarrocchi, G.
Characterization of human DNA ligase I expressed in a baculovirus-insect cell system
Biochem. J.
312
593-597
1995
Homo sapiens
Manually annotated by BRENDA team
Tan, G.T.; Lee, S.; Lee, I.S.; Chen, J.; Leitner, P.; Besterman, J.; Kinghorn, A.D.; Pezzuto, J.M.
Natural-product inhibitors of human DNA ligase I
Biochem. J.
314
993-1000
1996
Homo sapiens
Manually annotated by BRENDA team
Yang, S.W.; Becker, F.F.; Chan, J.Y.H.
Inhibition of human DNA ligase I activity by zinc and cadmium and the fidelity of ligation
Environ. Mol. Mutagen.
28
19-25
1996
Homo sapiens
Manually annotated by BRENDA team
Grawunder, U.; Wilm, M.; Wu, X.; Kuleza, P.; Wilson, T.E.; Mann, M.; Lieber, M.R.
Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
Nature
388
492-495
1997
Homo sapiens
Manually annotated by BRENDA team
Robin, P.; Lindahl, T.
DNA ligase IV from HeLa cell nuclei
J. Biol. Chem.
271
24257-24261
1996
Tequatrovirus T4, Homo sapiens
Manually annotated by BRENDA team
Ciarrocchi, G.; Lestingi, M.; Fontana, M.; Spadari, S.; Montecuccho, A.
Correlation between anthracycline structure and human DNA ligase inhibition
Biochem. J.
279
141-146
1991
Homo sapiens
Manually annotated by BRENDA team
Chen, J.; Tomkinson, A.E.; Ramos, W.; Mackey, Z.B.; Danehower, S.; Walter, C.A.; Schultz, R.A.; Besterman, J.M.; Husain, I.
Mammalian DNA ligase III: molecular cloning, chromosomal localization, and expression in spermatocytes undergoing meiotic recombination
Mol. Cell. Biol.
15
5412-5422
1995
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.C.; Burkhart, W.A.; Mackey, Z.B.; Moyer, M.B.; Ramos, W.; Husain, I.; Chen, J.; Besterman, J.M.; Tomkinson, A.E.
Mammalian DNA ligase II is highly homologous with vaccinia DNA ligase. Identification of the DNA ligase II active site for enzyme-adenylate formation
J. Biol. Chem.
269
31923-31928
1994
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Wei, Y.F.; Robins, P.; Carter, K.; Caldecott, K.; Pappin, D.J.; Yu, G.L.; Wang, R.P.; Shell, B.K.; Nash, R.A.; Schar, P.
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
Homo sapiens
Manually annotated by BRENDA team
Li, C.; Cao, L.G.; Wang, Y.L.; Baril, E.F.
Further purification and characterization of a multienzyme complex for DNA synthesis in human cells
J. Cell. Biochem.
53
405-419
1993
Homo sapiens
Manually annotated by BRENDA team
Barnes, D.E.; Johnston, L.H.; Kodama, K.; Tomkinson, A.E.; Lasko, D.D.; Lindahl, T.
Human DNA ligase I cDNA: cloning and functional expression in Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
87
6679-6683
1990
Homo sapiens
Manually annotated by BRENDA team
Yang, S.W.; Becker, F.F.; Chan, J.Y.
Identification of a specific inhibitor for DNA ligase I in human cells
Proc. Natl. Acad. Sci. USA
89
2227-2231
1992
Homo sapiens
Manually annotated by BRENDA team
Yang, S.W.; Huang, P.; Plunkett, W.; Becker, F.F.; Chan, J.Y.
Dual mode of inhibition of purified DNA ligase I from human cells by 9-beta-D-arabinofuranosyl-2-fluoroadenine triphosphate
J. Biol. Chem.
267
2345-2349
1992
Homo sapiens
Manually annotated by BRENDA team
Sun, D.; Urrabaz, R.; Kelly, S.; Nguyen, M.; Weitman, S.
Enhancement of DNA ligase I level by gemcitabine in human cancer cells
Clin. Cancer Res.
8
1189-1195
2002
Homo sapiens
Manually annotated by BRENDA team
Sun, D.; Urrabaz, R.; Buzello, C.; Nguyen, M.
Induction of DNA ligase I by 1-beta-D-arabinosylcytosine and aphidicolin in MiaPaCa human pancreatic cancer cells
Exp. Cell Res.
280
90-96
2002
Homo sapiens
Manually annotated by BRENDA team
Mossi, R.; Ferrari, E.; Hubscher, U.
DNA ligase I selectively affects DNA synthesis by DNA polymerases delta and epsilon suggesting differential functions in DNA replication and repair
J. Biol. Chem.
273
14322-14330
1998
Homo sapiens
Manually annotated by BRENDA team
Mackey, Z.B.; Niedergang, C.; Murcia, J.M.D.; Leppard, J.; Au, K.; Chen, J.; De Murcia, G.; Tomkinson, A.E.
DNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III
J. Biol. Chem.
274
21679-21687
1999
Homo sapiens
Manually annotated by BRENDA team
Tom, S.; Henricksen, L.A.; Park, M.S.; Bambara, R.A.
DNA ligase I and proliferating cell nuclear antigen form a functional complex
J. Biol. Chem.
276
24817-24825
2001
Homo sapiens
Manually annotated by BRENDA team
Ranalli, T.A.; DeMott, M.S.; Bambara, R.A.
Mechanism underlying replication protein A stimulation of DNA ligase I
J. Biol. Chem.
277
1719-1727
2002
Homo sapiens
Manually annotated by BRENDA team
Ranalli, T.A.; Tom, S.; Bambara, R.A.
AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair
J. Biol. Chem.
277
41715-41724
2002
Homo sapiens
Manually annotated by BRENDA team
Kysela, B.; Doherty, A.J.; Chovanec, M.; Stiff, T.; Ameer-Beg, S.M.; Vojnovic, B.; Girard, P.M.; Jeggo, P.A.
Ku stimulation of DNA ligase IV-dependent ligation requires inward movement along the DNA molecule
J. Biol. Chem.
278
22466-22474
2003
Homo sapiens
Manually annotated by BRENDA team
Tomkinson, A.E.; Mackey, Z.B.
Structure and function of mammalian DNA ligases
Mutat. Res.
407
1-9
1998
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Karimi-Busheri, F.; Lee, J.; Tomikson, A.E.; Weinfeld, M.
Repair of DNA strand gaps and nicks containing 3'-phosphate and 5'-hydroxyl termini by purified mammalian enzymes
Nucleic Acids Res.
26
4395-4400
1998
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Zeng, Z.C.; Perrault, A.R.; Cheng, X.; Qin, W.; Iliakis, G.
Genetic evidence for the involvement of DNA ligase IV in the DNA-PK-dependent pathway of non-homologous end joining in mammalian cells
Nucleic Acids Res.
29
1653-1660
2001
Homo sapiens
Manually annotated by BRENDA team
Wang, H.; Rosidi, B.; Perrault, R.; Wang, M.; Zhang, L.; Windhofer, F.; Iliakis, G.
DNA ligase III as a candidate component of backup pathways of nonhomologous end joining
Cancer Res.
65
4020-4030
2005
Homo sapiens
Manually annotated by BRENDA team
Goetz, J.D.; Motycka, T.A.; Han, M.; Jasin, M.; Tomkinson, A.E.
Reduced repair of DNA double-strand breaks by homologous recombination in a DNA ligase I-deficient human cell line
DNA Repair
4
649-654
2005
Homo sapiens
Manually annotated by BRENDA team
De, A.; Campbell, C.
A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability
Biochem. J.
402
175-186
2007
Homo sapiens (P49916)
Manually annotated by BRENDA team
Wang, Y.; Lamarche, B.J.; Tsai, M.D.
Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity
Biochemistry
46
4962-4976
2007
Homo sapiens (P49917), Homo sapiens
Manually annotated by BRENDA team
Tomkinson, A.E.; Vijayakumar, S.; Pascal, J.M.; Ellenberger, T.
DNA ligases: Structure, reaction mechanism, and function
Chem. Rev.
106
687-699
2006
Escherichia phage T7 (P00969), Homo sapiens (P18858)
Manually annotated by BRENDA team
Petermann, E.; Keil, C.; Oei, S.L.
Roles of DNA ligase III and XRCC1 in regulating the switch between short patch and long patch BER
DNA Repair
5
544-555
2006
Homo sapiens
Manually annotated by BRENDA team
Marchetti, C.; Walker, S.A.; Odreman, F.; Vindigni, A.; Doherty, A.J.; Jeggo, P.
Identification of a novel motif in DNA ligases exemplified by DNA ligase IV
DNA Repair
5
788-798
2006
Homo sapiens
Manually annotated by BRENDA team
Costantini, S.; Woodbine, L.; Andreoli, L.; Jeggo, P.A.; Vindigni, A.
Interaction of the Ku heterodimer with the DNA ligase IV/Xrcc4 complex and its regulation by DNA-PK
DNA Repair
6
712-722
2007
Homo sapiens
Manually annotated by BRENDA team
Gu, J.; Lu, H.; Tippin, B.; Shimazaki, N.; Goodman, M.F.; Lieber, M.R.
XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps
EMBO J.
26
1010-1023
2007
Homo sapiens
Manually annotated by BRENDA team
Mortusewicz, O.; Rothbauer, U.; Cardoso, M.C.; Leonhardt, H.
Differential recruitment of DNA ligase I and III to DNA repair sites
Nucleic Acids Res.
34
3523-3532
2006
Homo sapiens
Manually annotated by BRENDA team
Kusumoto, R.; Dawut, L.; Marchetti, C.; Wan Lee, J.; Vindigni, A.; Ramsden, D.; Bohr, V.A.
Werner protein cooperates with the XRCC4-DNA ligase IV complex in end-processing
Biochemistry
47
7548-7556
2008
Homo sapiens
Manually annotated by BRENDA team
Chen, X.; Zhong, S.; Zhu, X.; Dziegielewska, B.; Ellenberger, T.; Wilson, G.M.; MacKerell, A.D.; Tomkinson, A.E.
Rational design of human DNA ligase inhibitors that target cellular DNA replication and repair
Cancer Res.
68
3169-3177
2008
Homo sapiens
Manually annotated by BRENDA team
Pascal, J.M.
DNA and RNA ligases: structural variations and shared mechanisms
Curr. Opin. Struct. Biol.
18
96-105
2008
Homo sapiens, Pyrococcus furiosus, Saccharolobus solfataricus
Manually annotated by BRENDA team
Meier, T.I.; Yan, D.; Peery, R.B.; McAllister, K.A.; Zook, C.; Peng, S.B.; Zhao, G.
Identification and characterization of an inhibitor specific to bacterial NAD+-dependent DNA ligases
FEBS J.
275
5258-5271
2008
Tequatrovirus T4, Homo sapiens
Manually annotated by BRENDA team
Cotner-Gohara, E.; Kim, I.K.; Tomkinson, A.E.; Ellenberger, T.
Two DNA-binding and nick recognition modules in human DNA ligase III
J. Biol. Chem.
283
10764-10772
2008
Homo sapiens
Manually annotated by BRENDA team
Zhong, S.; Chen, X.; Zhu, X.; Dziegielewska, B.; Bachman, K.E.; Ellenberger, T.; Ballin, J.D.; Wilson, G.M.; Tomkinson, A.E.; MacKerell, A.D.
Identification and validation of human DNA ligase inhibitors using computer-aided drug design
J. Med. Chem.
51
4553-4562
2008
Homo sapiens (P18858), Homo sapiens
Manually annotated by BRENDA team
Dwivedi, N.; Dube, D.; Pandey, J.; Singh, B.; Kukshal, V.; Ramachandran, R.; Tripathi, R.P.
NAD+-dependent DNA ligase: a novel target waiting for the right inhibitor
Med. Res. Rev.
28
545-568
2008
Homo sapiens
Manually annotated by BRENDA team
Friesen, C.; Uhl, M.; Pannicke, U.; Schwarz, K.; Miltner, E.; Debatin, K.M.
DNA-ligase IV and DNA-protein kinase play a critical role in deficient caspases activation in apoptosis-resistant cancer cells by using doxorubicin
Mol. Biol. Cell
19
3283-3289
2008
Homo sapiens
Manually annotated by BRENDA team
Liang, L.; Deng, L.; Nguyen, S.C.; Zhao, X.; Maulion, C.D.; Shao, C.; Tischfield, J.A.
Human DNA ligases I and III, but not ligase IV, are required for microhomology-mediated end joining of DNA double-strand breaks
Nucleic Acids Res.
36
3297-3310
2008
Homo sapiens
Manually annotated by BRENDA team
Jayaram, S.; Ketner, G.; Adachi, N.; Hanakahi, L.A.
Loss of DNA ligase IV prevents recognition of DNA by double-strand break repair proteins XRCC4 and XLF
Nucleic Acids Res.
36
5773-5786
2008
Homo sapiens
Manually annotated by BRENDA team
Riballo, E.; Woodbine, L.; Stiff, T.; Walker, S.A.; Goodarzi, A.A.; Jeggo, P.A.
XLF-Cernunnos promotes DNA ligase IV-XRCC4 re-adenylation following ligation
Nucleic Acids Res.
37
482-492
2008
Homo sapiens
Manually annotated by BRENDA team
Jayaram, S.; Gilson, T.; Ehrlich, E.S.; Yu, X.F.; Ketner, G.; Hanakahi, L.
E1B 55k-independent dissociation of the DNA ligase IV/XRCC4 complex by E4 34k during adenovirus infection
Virology
382
163-170
2008
Homo sapiens
Manually annotated by BRENDA team
Yutin, N.; Koonin, E.V.
Evolution of DNA ligases of nucleo-cytoplasmic large DNA viruses of eukaryotes: a case of hidden complexity
Biol. Direct
4
51
2009
Acanthocystis turfacea chlorella virus 1, Acidobacterium capsulatum ATCC 51196, African swine fever virus, Agrotis segetum granulovirus, Aquifex aeolicus VF5, Arabidopsis thaliana, Archaeoglobus fulgidus DSM 4304, Chthoniobacter flavus, Chthoniobacter flavus Ellin428, Cinqassovirus aeh1, deerpox virus W-848-83, Dictyostelium discoideum, Drosophila melanogaster, Emiliania huxleyi virus 86, Entamoeba histolytica HM-1:IMSS, Enterobacteria phage, Erwinia phage, Escherichia phage V5, Fowlpox virus, Gemmata obscuriglobus UQM 2246, goatpox virus Pellor, Heliothis zea nudivirus, Homo sapiens, Lessievirus bcepil02, Lymantria dispar multiple nucleopolyhedrovirus, Marseillevirus, Methanosarcina acetivorans C2A, Methylibium petroleiphilum PM1, Monosiga brevicollis MX1, myxoma virus, Nanoarchaeum equitans Kin4-M, Nitrosopumilus maritimus SCM1, Okubovirus SPO1, Opitutus terrae PB90-1, Orgyia leucostigma nucleopolyhedrovirus, Ostreococcus virus OsV5, Paramecium bursaria Chlorella virus 1, Planctopirus limnophila DSM 3776, Plutella xylostella granulovirus, Prochlorococcus marinus, Pseudarthrobacter chlorophenolicus A6, Pseudomonas phage F8, Ralstonia phage RSB1, Saccharomyces cerevisiae, Sphingobacterium spiritivorum ATCC 33300, Spodoptera litura granulovirus, Staphylococcus epidermidis RP62A, Staphylothermus marinus F1, Stigmatella aurantiaca DW4/3-1, swinepox virus, Tetrahymena thermophila, Thermobaculum terrenum ATCC BAA-798, Thermofilum pendens Hrk 5, Vaccinia virus, Vibrio phage, Xanthomonas phage, Xylanimonas cellulosilytica DSM 15894
Manually annotated by BRENDA team
Chiang, S.C.; Carroll, J.; El-Khamisy, S.F.
TDP1 serine 81 promotes interaction with DNA ligase IIIalpha and facilitates cell survival following DNA damage
Cell Cycle
9
588-595
2010
Homo sapiens
Manually annotated by BRENDA team
Paran, N.; De Silva, F.S.; Senkevich, T.G.; Moss, B.
Cellular DNA ligase I is recruited to cytoplasmic vaccinia virus factories and masks the role of the vaccinia ligase in viral DNA replication
Cell Host Microbe
6
563-569
2009
Homo sapiens
Manually annotated by BRENDA team
Song, W.; Pascal, J.M.; Ellenberger, T.; Tomkinson, A.E.
The DNA binding domain of human DNA ligase I interacts with both nicked DNA and the DNA sliding clamps, PCNA and hRad9-hRad1-hHus1
DNA Repair
8
912-919
2009
Homo sapiens
Manually annotated by BRENDA team
Lopez Castel, A.; Tomkinson, A.E.; Pearson, C.E.
CTG/CAG repeat instability is modulated by the levels of human DNA ligase I and its interaction with proliferating cell nuclear antigen: a distinction between replication and slipped-DNA repair
J. Biol. Chem.
284
26631-26645
2009
Homo sapiens
Manually annotated by BRENDA team
Soza, S.; Leva, V.; Vago, R.; Ferrari, G.; Mazzini, G.; Biamonti, G.; Montecucco, A.
DNA ligase I deficiency leads to replication-dependent DNA damage and impacts cell morphology without blocking cell cycle progression
Mol. Cell. Biol.
29
2032-2041
2009
Homo sapiens
Manually annotated by BRENDA team
Vijayakumar, S.; Dziegielewska, B.; Levin, D.S.; Song, W.; Yin, J.; Yang, A.; Matsumoto, Y.; Bermudez, V.P.; Hurwitz, J.; Tomkinson, A.E.
Phosphorylation of human DNA ligase I regulates its interaction with replication factor C and its participation in DNA replication and DNA repair
Mol. Cell. Biol.
29
2042-2052
2009
Homo sapiens
Manually annotated by BRENDA team
Wu, P.Y.; Frit, P.; Meesala, S.; Dauvillier, S.; Modesti, M.; Andres, S.N.; Huang, Y.; Sekiguchi, J.; Calsou, P.; Salles, B.; Junop, M.S.
Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4
Mol. Cell. Biol.
29
3163-3172
2009
Homo sapiens
Manually annotated by BRENDA team
Unal, S.; Cerosaletti, K.; Uckan-Cetinkaya, D.; Cetin, M.; Gumruk, F.
A novel mutation in a family with DNA ligase IV deficiency syndrome
Pediatr. Blood Cancer
53
482-484
2009
Homo sapiens
Manually annotated by BRENDA team
Cotner-Gohara, E.; Kim, I.K.; Hammel, M.; Tainer, J.A.; Tomkinson, A.E.; Ellenberger, T.
Human DNA ligase III recognizes DNA ends bydynamic switching between two DNA-bound states
Biochemistry
49
6165-6176
2010
Homo sapiens
Manually annotated by BRENDA team
Ruhanen, H.; Ushakov, K.; Yasukawa, T.
Involvement of DNA ligase III and ribonuclease H1 in mitochondrial DNA replication in cultured human cells
Biochim. Biophys. Acta
1813
2000-2007
2011
Homo sapiens
Manually annotated by BRENDA team
Taylor, M.R.; Conrad, J.A.; Wahl, D.; OBrien, P.J.
Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency
J. Biol. Chem.
286
23054-23062
2011
Homo sapiens
Manually annotated by BRENDA team
Cuneo, M.J.; Gabel, S.A.; Krahn, J.M.; Ricker, M.A.; London, R.E.
The structural basis for partitioning of the XRCC1/DNA ligase III-alpha BRCT-mediated dimer complexes
Nucleic Acids Res.
39
7816-7827
2011
Homo sapiens (P49916)
Manually annotated by BRENDA team
Tome, S.; Panigrahi, G.B.; Lopez Castel, A.; Foiry, L.; Melton, D.W.; Gourdon, G.; Pearson, C.E.
Maternal germline-specific effect of DNA ligase I on CTG/CAG instability
Hum. Mol. Genet.
20
2131-2143
2011
Homo sapiens
Manually annotated by BRENDA team