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Information on EC 3.1.3.32 - polynucleotide 3'-phosphatase and Organism(s) Mus musculus and UniProt Accession Q9JLV6
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3.1.3.32 polynucleotide 3'-phosphataseIUBMB Comments
Also hydrolyses nucleoside 2'-, 3'- and 5'-monophosphates, but only 2'- and 3'-phosphopolynucleotides.
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Word Map
- 3.1.3.32
- 3'-phosphate
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exonuclease
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5'-kinase
- ape1
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5\'-hydroxyl
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3'-blocking
- xrcc4
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end-healing
- apraxia
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apurinic
- aprataxin
- diesterase
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end-processing
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3'-phosphorylated
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strand-breaks
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3'-phosphoesterase
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3'-phosphoglycolate
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phosphoesterase
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tyrosyl-dna
- analysis
- ap-endonuclease
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
3'-phosphatase, polynucleotide kinase/phosphatase, dna 3'-phosphatase, 3' phosphatase, polynucleotide kinase phosphatase, polynucleotide kinase 3'-phosphatase, polynucleotide kinase-phosphatase, atzdp, t4 polynucleotide kinase/phosphatase, 3'-phosphatase/5'-oh kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'(3')-polynucleotidase
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3'-phosphatase/5'-OH kinase
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5' polynucleotidekinase 3' phosphatase
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chromatin 3'-phosphatase
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deoxyribonucleate 3'-phosphatase
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DNA 3'-phosphatase
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phosphatase, polynucleotide 3'-
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PNKP
polynucleotide kinase 3'-phosphatase
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SNQI-PNK
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PNKP
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Phosphorylation
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hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
polynucleotide 3'-phosphohydrolase
Also hydrolyses nucleoside 2'-, 3'- and 5'-monophosphates, but only 2'- and 3'-phosphopolynucleotides.
CAS REGISTRY NUMBER
COMMENTARY
37288-16-7
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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
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A12B4C3
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2-(1-hydroxyundecyl)-1-(4-nitrophenylamino)-6-phenyl-6,7a-dihydro-1H-pyrrolo[3,4-b]pyridine-5,7(2H,4aH)-dione
Mus musculus
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94% inhibition at 0.05 mM
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional polynucleotide phosphatase/kinase, cf. EC 2.7.1.78
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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polynucleotide kinase/phosphatase serves a crucial role in the repair of DNA strand breaks by catalyzing the restoration of 5'-phosphate and 3'-hydroxyl termini. It is involved in single-strand break repair and participates in several DNA repair pathways through interactions with other DNA repair proteins, notably XRCC1 and XRCC4, regulation and enzyme recruitment, overview. Physiological importance of PNKP in maintaining the genomic stability of normal tissues, particularly developing neural cells, as well as enhancing the resistance of cancer cells to genotoxic therapeutic agents. The enzyme also performs base excision and double-strand break repair, overview
additional information
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PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP FHA domain to phosphorylated motifs on XRCC1 and XRCC4, overview. The crystal structure of murine PNKP shows that the two catalytic active sites are positioned on the same side of the protein
physiological function
mice with PNKP inactivation in neural progenitors manifest neurodevelopmental abnormalities and postnatal death. The phenotype involves defective base excision repair and nonhomologous end-joining. Mice homozygous for the T424GfsX48 frame-shift allele are lethal embryonically, and attenuated PNKP levels akin to microcephaly with seizures syndrome show general neurodevelopmental defects. Directed postnatal neural inactivation of PNKP affects specific subpopulations including oligodendrocytes
physiological function
the phosphatase domain binds 3'-phosphorylated single-stranded DNAs in a manner that is highly dependent on the presence of the 3'-phosphate. Double-stranded substrate binding is not as dependent on the 3'-phosphate. The predicted loss of energy due to base pair disruption upon binding of the phosphatase active site is likely balanced by favorable interactions between the liberated complementary strand and PNKP. The surrounding surfaces of the active site cleft are important in binding to double-stranded substrates
physiological function
transgenic mice conditionally expressing the pathological form of human ataxin-3, a polyglutamine repeat-containing protein mutated in spinocerebellar ataxia type 3, also show decreased 3'-phosphatase activity of PNKP, mostly in the deep cerebellar nuclei
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). PNKP_MOUSE
522
0
57223
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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PNK phosphatase is a multidomain enzyme that consists of an N-terminal forkhead-associated domain and a C-terminal catalytic domain composed of fused phosphatase and kinase subdomains, structure of mammalian PNK phosphatase, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D170A
mutation of the first aspartate of the conserved phosphatase motif, catalytically inactive but structurally intact protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, full-length enzyme and catalytic domain, i.e. residues 141-522
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
fluorescence polarization methods can detect specific binding of single-stranded DNAs with the phosphatase domain, but not specific interactions between the PNKP phosphatase and double-stranded substrates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Homo sapiens, Mus musculus, Schizosaccharomyces pombe
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
Homo sapiens, Mus musculus
Havali-Shahriari, Z.; Weinfeld, M.; Glover, J.N.
Characterization of DNA substrate binding to the phosphatase domain of the DNA repair enzyme polynucleotide kinase/phosphatase
Biochemistry
56
1737-1745
2017
Mus musculus (Q9JLV6)
Shimada, M.; Dumitrache, L.C.; Russell, H.R.; McKinnon, P.J.
Polynucleotide kinase-phosphatase enables neurogenesis via multiple DNA repair pathways to maintain genome stability
EMBO J.
34
2465-2480
2015
Mus musculus (Q9JLV6), Mus musculus
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, Mus musculus (Q9JLV6), Mus musculus
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