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Information on EC 2.7.1.78 - polynucleotide 5'-hydroxyl-kinase and Organism(s) Homo sapiens
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2.7.1.78 polynucleotide 5'-hydroxyl-kinaseIUBMB Comments
Also acts on 5'-dephospho-RNA 3'-mononucleotides.
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Word Map
- 2.7.1.78
- termini
- strand
-
single-stranded
-
gamma-32patp
-
exonuclease
-
32p-postlabeling
-
5\'-hydroxyl
- bacteriophage
- phosphodiesterase
-
3'-phosphatase
- nick
-
32p-labeled
- duplex
- 3'-monophosphate
-
5'-phosphorylated
-
5'-terminal
-
postlabeling
- dsdna
-
anticodon
-
5\'-termini
-
klenow
- xrcc4
-
dinucleoside
-
micrococcal
- 3',5'-bisphosphate
- synthesis
- primase
-
carcinogen-dna
-
phosphotriester
-
t4-infected
- oligoribonucleotide
- analysis
- biotechnology
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pnk, polynucleotide kinase, t4 polynucleotide kinase, t4 pnk, hd-pnk, dna kinase, hpnkp, 5'-oh polynucleotide kinase, 5'-hydroxyl polynucleotide kinase, phoclp1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-hydroxyl polynucleotide kinase
-
-
-
-
5'-hydroxyl polyribonucleotide kinase
-
-
-
-
5'-hydroxyl RNA kinase
-
-
-
-
ATP:5'-dephosphopolynucleotide 5'-phosphatase
-
-
-
-
CLP1
DNA 5'-hydroxyl kinase
-
-
-
-
DNA kinase
-
-
-
-
kinase (phosphorylating), polynucleotide 5'-hydroxyl
-
-
-
-
PNK
PNKP
polynucleotide 5'-hydroxyl kinase (phosphorylating)
-
-
-
-
polynucleotide 5'-hydroxyl-kinase
-
-
-
-
polynucleotide kinase
polynucleotide kinase/phosphatase
additional information
PNK
-
-
-
-
polynucleotide kinase
-
-
-
-
polynucleotide kinase
-
bifunctional enzyme possessing a 5'-DNA kinase activity and a 3'-phosphatase activity
polynucleotide kinase
-
major cellular 3' DNA phosphatase which also possesses a 5' kinase activity
polynucleotide kinase
-
the phosphatase activity of the purified enzyme is significantly more active than its kinase activity
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA
mechanism involves a ternary complex of enzyme, ATP and DNA
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phopho group transfer
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:5'-dephosphopolynucleotide 5'-phosphotransferase
Also acts on 5'-dephospho-RNA 3'-mononucleotides.
CAS REGISTRY NUMBER
COMMENTARY
37211-65-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 5'-dephospho-RNA
CDP + 5'-phospho-RNA
-
less effective than ATP
-
?
[gamma-S]GTP + 5'-dephospho-RNA
[gamma-S]GDP + 5'-phospho-RNA
-
less effective than ATP
-
?
ATP + 5'-dephospho-DNA
ADP + 5'-phospho-DNA
-
-
-
-
?
ATP + 5'-dephospho-DNA
ADP + 5'-phospho-DNA
-
involved in repair of DNA single strand breaks
-
-
?
ATP + 5'-dephospho-RNA
ADP + 5'-phospho-RNA
-
much more efficient as substrate than DNA
-
?
ATP + synthetic oligonucleotide
ADP + oligonucleotide 5'-phosphate
-
5'-hydroxyl poly(A)
-
-
?
ATP + synthetic oligonucleotide
ADP + oligonucleotide 5'-phosphate
-
5'-hydroxyl poly(C)
-
-
?
ATP + synthetic oligonucleotide
ADP + oligonucleotide 5'-phosphate
-
low activity with 5'-hydroxyl poly(I)
-
-
?
ATP + synthetic oligonucleotide
ADP + oligonucleotide 5'-phosphate
-
5'-hydroxyl poly(dA), at 6% of 5'-hydroxyl poly(A)
-
-
?
CTP + 5'-dephospho-DNA
CDP + 5'-phospho-DNA
-
CTP gives 15% of the activity with ATP
-
?
GTP + 5'-dephospho-DNA
GDP + 5'-phospho-DNA
-
GTP gives 15% of the activity with ATP
-
?
additional information
?
-
-
PALF nuclease activity acts on single-stranded DNA or overhangs of duplex substrates. PALF does not open DNA hairpins. Reduction of PALF in vivo reduces the joining of incompatible DNA ends, PALF can function in concert with other nonhomologous DNA end joining proteins. PALF is able to resect 3 overhanging nucleotides and permit XRCC4-DNA ligase IV to complete the joining process in a manner that is as efficient as Artemis. Role for polynucleotide kinase and aprataxin-like forkhead-associated, PALF, in nonhomologous DNA end joining
-
-
?
additional information
?
-
-
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP forkhead-associated domain to phosphorylated motifs on XRCC1 and XRCC4, overview. Phosphorylation-independent interaction between PNKP and XRCC1 in human cells, since a non-phosphorylated XRCC1S518A/T519A/T523A triple mutant is also bound
-
-
?
additional information
?
-
-
recombinant Nol9 phosphorylates single-stranded and double-stranded RNA and DNA substrates with high efficiency, mainly pre-60S rRNP particles. Nol9 is able to transfer a phosphate to 5' ends of dsRNAs, but cannot phosphorylate 3' termini
-
-
?
additional information
?
-
-
the enzyme plays a role in tRNA splicing. The ATP-binding and/or hydrolysis capacity of CLP1 is required to enhance pre-tRNA cleavage
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 5'-dephospho-DNA
ADP + 5'-phospho-DNA
-
-
-
-
?
ATP + 5'-dephospho-DNA
ADP + 5'-phospho-DNA
-
involved in repair of DNA single strand breaks
-
-
?
additional information
?
-
-
PALF nuclease activity acts on single-stranded DNA or overhangs of duplex substrates. PALF does not open DNA hairpins. Reduction of PALF in vivo reduces the joining of incompatible DNA ends, PALF can function in concert with other nonhomologous DNA end joining proteins. PALF is able to resect 3 overhanging nucleotides and permit XRCC4-DNA ligase IV to complete the joining process in a manner that is as efficient as Artemis. Role for polynucleotide kinase and aprataxin-like forkhead-associated, PALF, in nonhomologous DNA end joining
-
-
?
additional information
?
-
-
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP forkhead-associated domain to phosphorylated motifs on XRCC1 and XRCC4, overview. Phosphorylation-independent interaction between PNKP and XRCC1 in human cells, since a non-phosphorylated XRCC1S518A/T519A/T523A triple mutant is also bound
-
-
?
additional information
?
-
-
the enzyme plays a role in tRNA splicing. The ATP-binding and/or hydrolysis capacity of CLP1 is required to enhance pre-tRNA cleavage
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
the ATP binding site is defined by the Walker A (P-loop) and B motifs conserved in various kinases, as well as an Asp396 that activates the 5'-OH for attack on the ATP gamma-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(1-hydroxyundecyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
2-(hydroxy(3,4,5-trimethoxyphenyl)methyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
-
A6B4C3
2-(hydroxy(phenyl)methyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
-
A1B4C3
2-(hydroxy(thiophen-2-yl)methyl)-6-methyl-1-(phenylamino)-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
-
A39B1C2
beta,gamma-imidoadenosine 5'-triphosphate
-
binds with high affinity, similar to ATP
tert-butyl 2-(1-hydroxy-2,2-diphenylethyl)-6-methyl-5,7-dioxo-2,4a,5,6,7,7a-hexahydro-1H-pyrrolo[3,4-b]pyridine-1yl-carbamate
-
A26B11C2
additional information
-
productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site
-
2-(1-hydroxyundecyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
-
A12B4C3
2-(1-hydroxyundecyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
A12B4C3, noncompetitive inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
XRCC1
-
mechanism underlying XRCC1-induced stimulation of PNKP, XRCC1 displaces PNKP from the reaction product, and addition of XRCC1 increases PNKP enzymatic turnover
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
effect of A12B4C3 binding on the W331F mutant, 95% inhibition
-
additional information
additional information
effect of A12B4C3 binding on the W402F mutant, 6% inhibition
-
additional information
additional information
effect of A12B4C3 binding on the WFX402 mutant, 90% inhibition
-
additional information
additional information
effect of A12B4C3 binding on the wild-type PNKP, 100% inhibition
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006
2-(1-hydroxyundecyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
7.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.9
-
pH 6.5: about 50% of activity maximum, pH 7.9-8.9: activity maximum, substrate RNA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
polynucleotide 5-kinase Nol9 is involved in ribosomal RNA processing
physiological function
additional information
malfunction
-
depletion of Nol9 leads to a severe impairment of ribosome biogenesis. Upon Nol9 knockdown, specific maturation defect at the 5' end of the predominant 5.8S short-form rRNA (5.8SS) occur, possibly due to the Nol9 requirement for 5'>3' exonucleolytic trimming
malfunction
-
knockdown of polynucleotide kinase and aprataxin-like forkhead-associated using siRNA reduces rejoining of two incompatible I-SceI-generated DNA ends by 50%
malfunction
-
PNKP depletion in human cells renders cells sensitive to camptothecin. A small molecule inhibitor of PNKP phosphatase activity enhances the sensitivity of cells to IR and camptothecin. Enzyme mutational defects can cause neurological disorders with various symptoms, e.g. a severe neurological autosomal recessive disease characterized by microcephaly, intractable seizures and developmental delay
malfunction
-
mutations lead to a loss of enzyme interaction with the tRNA splicing endonuclease complex, largely reduced pretRNA cleavage activity, and accumulation of linear tRNA introns. The affected individuals develop severe motor-sensory defects, cortical dysgenesis, and microcephaly
malfunction
-
the lack of CLP1 kinase activity leads to progressive motor neuron loss and accumulation of novel 5' leader-5' exon tRNA fragments
physiological function
-
bifunctional polynucleotide kinase/phosphatase contains both DNA 5'-kinase and 3'-phosphatase activities required for restoration of 3'-hydroxyls and 5'-phosphates needed to seal the broken DNA. Cellular DNA is constantly assaulted by ionizing radiation and reactive oxygen species. This damage, along with the products of some DNA repair enzymes, may contain 5' hydroxyls or 3' phosphates. These are converted by PNK to 5' phosphates and 3' hydroxyls, which are required for DNA polymerases and DNA ligases to complete repair of the damaged DNA. Productive engagement of a 3'-phosphate terminus may block access of a 5'-hydroxyl to the kinase active site
physiological function
-
polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3 exonuclease and can participate in DNA end joining in a biochemical system, they use the forkhead-associated domain to bind to x-ray repair complementing defective repair in Chinese hamster cells 4, XRCC4, overview
physiological function
-
polynucleotide kinase/phosphatase is an essential enzyme for the repair of damaged DNA termini. PNKP possesses both 5'-kinase and 3'-phosphatase activities that are frequently required for processing of single- and double-strand break termini
physiological function
-
the nonribosomal protein Nol9 is a polynucleotide 5'-kinase that sediments primarily with the pre-60S and pre-40S ribosomal particles in HeLa nuclear extracts. The polynucleotide kinase activity of Nol9 is required for processing of large subunit rRNA and efficient generation of the 5.8S and 28S rRNAs from the 32S precursor
physiological function
-
PNKP stably associates with ataxin-3. Purified wild-type ataxin-3 stimulates, and the mutant form specifically inhibits, PNKP's 3'-phosphatase activity in vitro. ATXN3-deficient cells also show decreased PNKP activity
physiological function
-
polynucleotide kinase phosphatase is a DNA repair factor with dual enzymatic functions, i.e., phosphorylation of 5'-end and dephosphorylation of 3'-end, which are prerequisites for DNA ligation and, thus, is involved in multiple DNA repair pathways, i.e., base excision repair, single-strand break repair and double-strand break repair through nonhomologous end joining
additional information
-
molecular architecture of the enzyme, overview. The mammalian enzyme preferentially phosphorylates 5'-hydroxyl termini within nicked, gapped or double-strand breaks with single-stranded 3'-overhanging ends, whereas single-stranded 5'-termini or blunt double-stranded ends are phosphorylated less efficiently. The selective recognition of the larger, double-stranded DNA substrates is effected by a broad DNA recognition groove composed of two distinct positively charged surfaces. Mechanisms of single-strand break and double-strand break repairs, and of base excision repair, overview
additional information
-
the nuclease activity of polynucleotide kinase and aprataxin-like forkhead-associated is not affected by Ku or XRCC4-DNA ligase IV
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CLP1_HUMAN
425
0
47646
Swiss-Prot
other Location (Reliability: 1)
PNKP_HUMAN
521
0
57076
Swiss-Prot
other Location (Reliability: 1)
E9PL17_HUMAN
436
0
48940
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
PNKP is a multi-domain enzyme that consists of an N-terminal forkhead-associated domain and a C-terminal catalytic domain composed of fused phosphatase and kinase subdomains
additional information
-
separate kinase and phosphatase catalytic activities are located in two halves of an interconnected bilobed catalytic domain that is flexibly linked to an aminoterminal phosphoprotein-binding forkhead-associated domain
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K138A/R35A
-
the mutant shows impaired nuclear localization as compared to the wild type enzyme
R140H
WFX402
mutant, all tryptophans except 402 are replaced by phenylalanine, 85% phosphatase activity
R140H
the mutation does not destabilize the protein but substantially impairs kinase activity (less than 40% compared to the wild type). The mutation is associated with degeneration/hypoplasia of the central nervous system
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin and dithiothreitol stabilize the enzyme during activity assay
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged human Nol9 from Sf9 insect cells by glutathione affinity chromatography
-
recombinant His-tagged full length enzyme and recombinant truncated enzyme from Escherichia coli
-
recombinant N-terminally His-tagged polynucleotide kinase and aprataxin-like forkhead-associated from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a vector encoding N-terminally Strep II epitope-tagged polynucleotide kinase is prepared, the protein is expressed in Escherichia coli Rosetta 2 DE3 pLysS cells
-
expression of N-terminally His-tagged polynucleotide kinase and aprataxin-like forkhead-associated in Escherichia coli strain BL21(DE3)
-
expression of truncated enzyme, residue Met140 to C-terminus, in Escherichia coli
-
the PNKP mutants are subcloned into the vector pET16b for expression in Escherichia coli BL21DE3 pLysS cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
A12B4C3 enhances the radiosensitivity of human A549 lung carcinoma and MDA-MB-231 breast adenocarcinoma cells by a factor of two
medicine
-
human Machado-Joseph disease patients' brain samples show a significant accumulation of DNA strand breaks. PNKP stably associates with ataxin-3, a polyglutamine repeat-containing protein mutated in spinocerebellar ataxia type 3, i.e. Machado-Joseph disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maunders, M.J.
Polynucleotide kinase (EC 2.7.1.78)
Methods Mol. Biol.
16
343-357
1993
Escherichia phage T2, Tequatrovirus T4, Enterobacteria phage T6, Bos taurus, Homo sapiens, Mesocricetus auratus, no activity in Escherichia coli, Rattus norvegicus
Shuman, S.; Hurwitz, J.
5-Hydroxyl polyribonucleotide kinase from HeLa cell nuclei. Purification and properties
J. Biol. Chem.
254
10396-10404
1979
Homo sapiens
Fanta, M.; Zhang, H.; Bernstein, N.; Glover, M.; Karimi-Busheri, F.; Weinfeld, M.
Production, characterization, and epitope mapping of monoclonal antibodies against human polydeoxyribonucleotide kinase
Hybridoma
20
237-242
2001
Homo sapiens
Mani, R.S.; Karimi-Busheri, F.; Fanta, M.; Cass, C.E.; Weinfeld, M.
Spectroscopic studies of DNA and ATP binding to human polynucleotide kinase: evidence for a ternary complex
Biochemistry
42
12077-12084
2003
Homo sapiens
Karimi-Busheri, F.; Rasouli-Nia, A.; Allalunis-Turner, J.; Weinfeld, M.
Human polynucleotide kinase participates in repair of DNA double-strand breaks by nonhomologous end joining but not homologous recombination
Cancer Res.
67
6619-6625
2007
Homo sapiens
Audebert, M.; Salles, B.; Weinfeld, M.; Calsou, P.
Involvement of polynucleotide kinase in a poly(ADP-ribose) polymerase-1-dependent DNA double-strand breaks rejoining pathway
J. Mol. Biol.
356
257-265
2006
Homo sapiens
Dobson, C.J.; Allinson, S.L.
The phosphatase activity of mammalian polynucleotide kinase takes precedence over its kinase activity in repair of single strand breaks
Nucleic Acids Res.
34
2230-2237
2006
Homo sapiens
Freschauf, G.K.; Karimi-Busheri, F.; Ulaczyk-Lesanko, A.; Mereniuk, T.R.; Ahrens, A.; Koshy, J.M.; Rasouli-Nia, A.; Pasarj, P.; Holmes, C.F.; Rininsland, F.; Hall, D.G.; Weinfeld, M.
Identification of a small molecule inhibitor of the human DNA repair enzyme polynucleotide kinase/phosphatase
Cancer Res.
69
7739-7746
2009
Tequatrovirus T4, Homo sapiens, Schizosaccharomyces pombe, Mus musculus (Q9JLV6)
Whiteside, J.R.; Box, C.L.; McMillan, T.J.; Allinson, S.L.
Cadmium and copper inhibit both DNA repair activities of polynucleotide kinase
DNA Repair
9
83-89
2010
Homo sapiens
Freschauf, G.K.; Mani, R.S.; Mereniuk, T.R.; Fanta, M.; Virgen, C.A.; Dianov, G.L.; Grassot, J.M.; Hall, D.G.; Weinfeld, M.
Mechanism of action of an imido-piperidine inhibitor of human polynucleotide kinase/phosphatase
J. Biol. Chem.
285
2351-2360
2010
Homo sapiens (Q96T60)
Weinfeld, M.; Mani, R.S.; Abdou, I.; Aceytuno, R.D.; Glover, J.N.
Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair
Trends Biochem. Sci.
36
262-271
2011
Tequatrovirus T4, Homo sapiens, Mus musculus, Schizosaccharomyces pombe
Heindl, K.; Martinez, J.
Nol9 is a novel polynucleotide 5-kinase involved in ribosomal RNA processing
EMBO J.
29
4161-4171
2010
Homo sapiens
Li, S.; Kanno, S.; Watanabe, R.; Ogiwara, H.; Kohno, T.; Watanabe, G.; Yasui, A.; Lieber, M.R.
Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3 exonuclease and can participate in DNA end joining in a biochemical system
J. Biol. Chem.
286
36368-36377
2011
Homo sapiens
Schellenberg, M.; Williams, R.
DNA end processing by polynucleotide kinase/phosphatase
Proc. Natl. Acad. Sci. USA
108
20855-20856
2011
Homo sapiens, Mus musculus
Mair, B.; Popow, J.; Mechtler, K.; Weitzer, S.; Martinez, J.
Intron excision from precursor tRNA molecules in mammalian cells requires ATP hydrolysis and phosphorylation of tRNA-splicing endonuclease components
Biochem. Soc. Trans.
41
831-837
2013
Homo sapiens
Karaca, E.; Weitzer, S.; Pehlivan, D.; Shiraishi, H.; Gogakos, T.; Hanada, T.; Jhangiani, S.N.; Wiszniewski, W.; Withers, M.; Campbell, I.M.; Erdin, S.; Isikay, S.; Franco, L.M.; Gonzaga-Jauregui, C.; Gambin, T.; Gelowani, V.; Hunter, J.V.; Yesil, G.; Koparir, E.; Yilmaz, S.; Brown, M.; Briskin, D.; H, H.a.
Human CLP1 mutations alter tRNA biogenesis, affecting both peripheral and central nervous system function
Cell
157
636-650
2014
Homo sapiens
Schaffer, A.E.; Eggens, V.R.; Caglayan, A.O.; Reuter, M.S.; Scott, E.; Coufal, N.G.; Silhavy, J.L.; Xue, Y.; Kayserili, H.; Yasuno, K.; Rosti, R.O.; Abdellateef, M.; Caglar, C.; Kasher, P.R.; Cazemier, J.L.; Weterman, M.A.; Cantagrel, V.; Cai, N.; Zweier, C.; Altunoglu, U.; Satkin, N.B.; Aktar, F.; Tuysuz, B.
CLP1 founder mutation links tRNA splicing and maturation to cerebellar development and neurodegeneration
Cell
157
651-663
2014
Homo sapiens (Q92989), Homo sapiens
Chatterjee, A.; Saha, S.; Chakraborty, A.; Silva-Fernandes, A.; Mandal, S.M.; Neves-Carvalho, A.; Liu, Y.; Pandita, R.K.; Hegde, M.L.; Hegde, P.M.; Boldogh, I.; Ashizawa, T.; Koeppen, A.H.; Pandita, T.K.; Maciel, P.; Sarkar, P.S.; Hazra, T.K.
The role of the mammalian DNA end-processing enzyme polynucleotide kinase 3-phosphatase in spinocerebellar ataxia type 3 pathogenesis
PLoS Genet.
11
e1004749
2015
Homo sapiens
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