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Information on EC 3.9.1.3 - phosphohistidine phosphatase
for references in articles please use BRENDA:EC3.9.1.3
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EC Tree 3 Hydrolases
3.9 Acting on phosphorus-nitrogen bonds
3.9.1 Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date)
3.9.1.3 phosphohistidine phosphatase
IUBMB Comments
This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most) . The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate [1,4] and peptide-bound phospholysine .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showSynonyms
phpt1, php14, protein histidine phosphatase, phosphohistidine phosphatase, protein histidine phosphatase 1, 14-kda phosphohistidine phosphatase, phosphohistidine phosphatase 1, phpti, phpt-1, phospho-histidine phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
14 kDa phosphohistidine phosphatase
14-kDa phosphohistidine phosphatase
LHPP
pHis phosphatase
phosphohistidine phosphatase 1
PHP
PHP14
PHPT-1
PHPT1
PP1
PP2A
protein histidine phosphatase
protein histidine phosphatase 1
SixA
PHP
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PHPT1
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-
-
-
protein histidine phosphatase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [protein]-N-phospho-L-histidine + H2O = a [protein]-L-histidine + phosphate
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SYSTEMATIC NAME
IUBMB Comments
[protein]-N-phospho-L-histidine phosphohydrolase
This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most) [4]. The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate [1,4] and peptide-bound phospholysine [5].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
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4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
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6,8-difluoromethylumbelliferyl phosphate + H2O
6,8-difluoromethylumbelliferone + phosphate
Substrates: -
Products: -
Products: -
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succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
VIFIE-N-phospho-HAKRKG + H2O
VIFIEHAKRKG + phosphate
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Substrates: -
Products: -
Products: -
?
[ACLY protein]-N-phospho-L-histidine + H2O
[ACLY protein]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
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[ArcB]-N-phospho-L-histidine + H2O
[ArcB]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
[ATP-citrate lyase]-N-phospho-L-histidine760 + H2O
[ATP-citrate lyase]-L-histidine760 + phosphate
Substrates: -
Products: -
Products: -
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[beta-subunit of heterotrimeric G-protein]-N-phospho-L-histidine + H2O
[beta-subunit of heterotrimeric G-protein]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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[cation channel SK4]-N-phospho-L-histidine + H2O
[cation channel SK4]-L-histidine + phosphate
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Substrates: -
Products: -
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[CheA]-N-phospho-L-histidine + H2O
[CheA]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
[G protein beta subunit]-N-phospho-L-histidine266 + H2O
[G protein beta subunit]-L-histidine266 + phosphate
Substrates: -
Products: -
Products: -
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[Gbeta1 protein]-N-phospho-L-histidine + H2O
[Gbeta1 protein]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
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[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
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Substrates: -
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[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
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Substrates: the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
Products: -
Products: -
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[KCa3.1]-N-phospho-L-histidine + H2O
[KCa3.1]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
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[KCa3.1]-N-phospho-L-histidine358 + H2O
[KCa3.1]-L-histidine358 + phosphate
Substrates: -
Products: -
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[NPr]-N-phospho-L-histidine + H2O
[NPr]-L-histidine + phosphate
Substrates: -
Products: -
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[nucleoside diphosphate kinase B]-N-phospho-L-histidine + H2O
[nucleoside diphosphate kinase B]-L-histidine + phosphate
Substrates: the enzyme (PGAM5) specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
Products: -
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[peptide]-N-phospho-L-histidine + H2O
[peptide]-L-histidine + phosphate
Substrates: H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
Products: -
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[phosphocarrier protein NPr]-N-phospho-L-histidine16 + H2O
[phosphocarrier protein NPr]-L-histidine16 + phosphate
Substrates: -
Products: -
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[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
-
Substrates: -
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[TRP channel protein TRPV5]-N-phospho-L-histidine + H2O
[TRP channel protein TRPV5]-L-histidine + phosphate
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Substrates: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
Substrates: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
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succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
Substrates: -
Products: -
Products: -
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succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
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Substrates: -
Products: -
Products: -
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succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
-
Substrates: -
Products: -
Products: -
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succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
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Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
Substrates: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
Substrates: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
Substrates: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
Substrates: -
Products: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
Substrates: -
Products: -
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r
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
Substrates: -
Products: -
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[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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[TRPV5]-N-phospho-L-histidine + H2O
[TRPV5]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[TRPV5]-N-phospho-L-histidine + H2O
[TRPV5]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also dephosphorylates phospholysine of chemically phosphorylated histone H1.2 and polylysine
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme does not dephosphorylate free phosphoarginine
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme is unable to catalyse the dephosphorylation of histone H4 that has been phosphorylated with a histone H4 histidine kinase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme may also act on phospholysine (e.g. chemically phosphorylated 30 kDa and 90 kDa polylysine or phospholysine in histone H1.2)
Products: -
Products: -
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additional information
?
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Substrates: histidine phosphoproteins of 40000 and 20000 Da are not dephosphorylated by the enzyme
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[ACLY protein]-N-phospho-L-histidine + H2O
[ACLY protein]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
?
[ArcB]-N-phospho-L-histidine + H2O
[ArcB]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
[ATP-citrate lyase]-N-phospho-L-histidine760 + H2O
[ATP-citrate lyase]-L-histidine760 + phosphate
Substrates: -
Products: -
Products: -
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[beta-subunit of heterotrimeric G-protein]-N-phospho-L-histidine + H2O
[beta-subunit of heterotrimeric G-protein]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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[cation channel SK4]-N-phospho-L-histidine + H2O
[cation channel SK4]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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[CheA]-N-phospho-L-histidine + H2O
[CheA]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
[G protein beta subunit]-N-phospho-L-histidine266 + H2O
[G protein beta subunit]-L-histidine266 + phosphate
Substrates: -
Products: -
Products: -
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[Gbeta1 protein]-N-phospho-L-histidine + H2O
[Gbeta1 protein]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
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[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
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Substrates: -
Products: -
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[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
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Substrates: the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
Products: -
Products: -
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[KCa3.1]-N-phospho-L-histidine + H2O
[KCa3.1]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
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[KCa3.1]-N-phospho-L-histidine358 + H2O
[KCa3.1]-L-histidine358 + phosphate
Substrates: -
Products: -
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[NPr]-N-phospho-L-histidine + H2O
[NPr]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[nucleoside diphosphate kinase B]-N-phospho-L-histidine + H2O
[nucleoside diphosphate kinase B]-L-histidine + phosphate
Substrates: the enzyme (PGAM5) specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
Products: -
Products: -
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[phosphocarrier protein NPr]-N-phospho-L-histidine16 + H2O
[phosphocarrier protein NPr]-L-histidine16 + phosphate
Substrates: -
Products: -
Products: -
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[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
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Substrates: -
Products: -
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[TRP channel protein TRPV5]-N-phospho-L-histidine + H2O
[TRP channel protein TRPV5]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
Products: -
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a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
?
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
Products: -
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a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
-
Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
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Substrates: -
Products: -
Products: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[Escherichia coli histidine kinase ArcB]-N-phospho-L-histidine + H2O
[Escherichia coli histidine kinase ArcB]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
r
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
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Substrates: -
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[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
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Substrates: -
Products: -
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[TRPV5]-N-phospho-L-histidine + H2O
[TRPV5]-L-histidine + phosphate
Substrates: -
Products: -
Products: -
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[TRPV5]-N-phospho-L-histidine + H2O
[TRPV5]-L-histidine + phosphate
Substrates: substrate for PHPT1
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme also dephosphorylates phospholysine of chemically phosphorylated histone H1.2 and polylysine
Products: -
Products: -
?
additional information
?
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-
Substrates: the enzyme does not dephosphorylate free phosphoarginine
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
overnight incubation with 1 mM ATP reduces the enzyme activity by 34%
bovine serum albumin
minimal effects on activity with the exception of a 35% activity decrease in Tris/HCl
-
CaCl2
1 mM, 40% decrease of activity in HEPES and a 15% decrease in Tris/HCl buffer
NaCl
100 mM, 30-60% decrease in activity. 50 mM, reductions of 10-25% of activity. 10 mM, 5-15% reduction of activity
ZnCl2
1 mM, almost completely inhibits enzyme activity. Biphasic curve with IC50 values of 0.025 and 0.49 mM, indicating that there may be two zinc binding sites in the enzyme
okadaic acid
-
isoform PP1 is inhibited by 0.001 mM okadaic acid and isoform PP2A by 3 nM okadaic acid
okadaic acid
-
isoform PP1 is inhibited by 0.001 mM okadaic acid and isoform PP2A by 3 nM okadaic acid
additional information
removal of dithiothreitol from reaction results in a substantial loss of activity in both Tris/HCl and HEPES, a 40% reduction in bicine, and a 65% reduction in bis-Tris propane
-
additional information
not inhibited by iodoacetamide, 2-iodo-N-phenylacetamide, methyl-4-toluenesulfonate, and GSSG
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
slightly increased activity in the presence of 5,5'-dithiobis-2-nitrobenzoic acid and GSH
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Atherosclerosis
Nucleoside diphosphate kinase B-activated intermediate conductance potassium channels are critical for neointima formation in mouse carotid arteries.
Carcinogenesis
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Carcinoma
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Carcinoma, Hepatocellular
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Carcinoma, Hepatocellular
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Carcinoma, Renal Cell
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Colorectal Neoplasms
Differential expression of alternatively spliced transcripts related to energy metabolism in colorectal cancer.
Infections
Primary hyperparathyroidism characterized by diffuse homogeneous metastatic pulmonary calcification: A case report.
Liver Cirrhosis
14-kDa phosphohistidine phosphatase is a potential therapeutic target for liver fibrosis.
Liver Cirrhosis
PHP14 regulates hepatic stellate cells migration in liver fibrosis via mediating TGF-?1 signaling to PI3K?/AKT/Rac1 pathway.
Lung Neoplasms
14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion.
Lung Neoplasms
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Lung Neoplasms
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Neoplasm Metastasis
14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion.
Neoplasms
14-kDa Phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation.
Neoplasms
Down-regulation of LHPP in cervical cancer influences cell proliferation, metastasis and apoptosis by modulating AKT.
Neoplasms
Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections.
Neoplasms
Knockdown of 14-kDa phosphohistidine phosphatase expression suppresses lung cancer cell growth in vivo possibly through inhibition of NF-?B signaling pathway.
Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Neoplasms
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma.
Respiratory Tract Infections
Primary hyperparathyroidism characterized by diffuse homogeneous metastatic pulmonary calcification: A case report.
Urinary Bladder Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
Uterine Cervical Neoplasms
LHPP suppresses proliferation, migration, and invasion and promotes apoptosis in pancreatic cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.4
4-nitrophenylphosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
0.22
6,8-difluoromethylumbelliferyl phosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
4-nitrophenylphosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
0.39
6,8-difluoromethylumbelliferyl phosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.047
4-nitrophenylphosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
1.8
6,8-difluoromethylumbelliferyl phosphate
pH 8.0, 37°C, HEPES buffer (50 mM at pH 8.0) with 10 mM NaCl, 0.01% w/v Brij 35 and 0.5 mM DTT as additives
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.183
Ethacrynic acid
pH and temperature not specified in the publication
0.209
N-ethylmaleimide
pH and temperature not specified in the publication
0.09
norstitic acid
pH and temperature not specified in the publication
-
0.025
ZnCl2
pH 8.0, 37°C. Biphasic curve with IC50 values of 0.025 and 0.49 mM, indicating that there may be two zinc binding sites in the enzyme
0.49
ZnCl2
pH 8.0, 37°C. Biphasic curve with IC50 values of 0.025 and 0.49 mM, indicating that there may be two zinc binding sites in the enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.06
cell lysate, mutant enzyme R45A, pH and temperature not specified in the publication
0.2
purified mutant enzyme R45A, pH and temperature not specified in the publication
0.3
cell lysate, mutant enzyme R78A, pH and temperature not specified in the publication
0.4
0.9
purified mutant enzyme R78A, pH and temperature not specified in the publication
1.4
purified mutant enzyme H81A, pH and temperature not specified in the publication
1.8
purified wild type enzyme, pH and temperature not specified in the publication
0.4
cell lysate, wild type enzyme, pH and temperature not specified in the publication
0.4
cell lysate, mutant enzyme H81A, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8
good activity with Tris/HCl buffer, bicine buffer, bis-Tris propane buffer, and HEPES buffer. Bicine buffer and bis-Tris propane buffer giving slightly higher activity than Tris·HCl and bicine buufer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 9
5.6 - 9
at pH 5.6, the activity is 2% of that at pH 7.5, and no activity is detected at pH 9.0
5.6 - 9
-
at pH 5.6, the activity is 2% of that at pH 7.5, and no activity is detected at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
colocalization of the enzyme (PHP14) with Arp3 and F-actin at the leading edge of migrating cells. PHP14 is recruited to the actin remodeling sites in parallel with Arp3 during lamellipodia formation
brenda
in patients with hepatocellular carcinoma, low expression of LHPP correlated with increased tumour severity and reduced overall survival
brenda
colocalization of the enzyme (PHP14) with Arp3 and F-actin at the leading edge of migrating cells. PHP14 is recruited to the actin remodeling sites in parallel with Arp3 during lamellipodia formation
brenda
enzyme (PHP14) expression is upregulated in fibrotic liver and mainly in hepatic stellate cells
brenda
enzyme (PHP14) expression is upregulated in fibrotic liver and mainly in hepatic stellate cells
brenda
hepatic expression of LHPP in the hepatocellular carcinoma mouse model reduces tumour burden and prevents the loss of liver function
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
enzyme downregulation does not induce cell death, but significantly increases the acetylcholine content in SN-56 cells
malfunction
enzyme knockdown in highly metastatic lung cancer CL1-5 cells inhibits migration and invasion in vitro, but does not alter cell proliferation rates, while enzyme overexpression in H1299 cells promotes migration and invasion in vitro, but again does not alter cell proliferation
malfunction
-
cell proliferation is inhibited and cell apoptosis is significantly increased following knockdown of 14 kDa phosphohistidine phosphatase
malfunction
-
decreased expression of PHPT-1 in human CD4 T cells results in an increase in KCa3.1 channel activity and increases Ca2+ influx and proliferation after T cell receptor activation
malfunction
-
depletion of the enzyme significantly reduces glucose- and mitochondrial fuel- but not KCl-induced insulin secretion
malfunction
DELTAsixA cells have lower intracellular potassium levels than wild-type cells
malfunction
PHPT-1(-/-) mice exhibit neonatal hyperinsulinemic hypoglycemia due to impaired trafficking of K(ATP) channels to the plasma membrane in pancreatic beta-cells in response to low glucose and leptin. The defect in K(ATP) channel trafficking in PHPT-1(-/-) beta-cells is due to the failure of PHPT-1 to directly activate transient receptor potential channel 4 (TRPC4), resulting in decreased Ca2+ influx and impaired downstream activation of AMPK
malfunction
PHP14 knockdown impairs Arp3 localization at the leading edge of lamellipodia, as well as lamellipodia formation
malfunction
Pgam5-/- T cells cause accelerated and more severe Graft versus host disease (GvHD) in mice
malfunction
enzyme knockdown impairs the migration ability of macrophages but does not affect their ability to activate hepatic stellate cells in vitro. Enzyme inhibition decreases the expression of the fibrogenic signature at the early stage of liver fibrogenesis and the activation of hepatic stellate cells in vivo
malfunction
an enzyme deletion has an phosphocarrier protein NPr-dependent colonization defect in the mouse intestine
malfunction
-
DELTAsixA cells have lower intracellular potassium levels than wild-type cells
-
metabolism
-
the enzyme downregulates the activity of ATP-citrate lyase by dephosphorylation
metabolism
-
the enzyme reduces the activity of ATP-citrate lyase by dephosphorylation at His760 in the active site and, thus controls the main intermediate metabolism of the cell
metabolism
the enzyme targets a phosphotransferase system. A model is suggested in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues
metabolism
PHP14 promotes hepatic stellate cell migration, especially, promotes 3D floating collagen matrices contraction but inhibits stress released matrices contraction. Mechanistically, the PI3Kgamma/AKT/Rac1 pathway is involved in migration regulated by PHP14. Moreover, PHP14 specifically mediates the TGF-beta1 signaling to PI3Kgamma/AKT pathway and regulates HSC migration, and thus participates in liver fibrosis
metabolism
LHPP is a protein histidine phosphatase and tumour suppressor, suggesting that deregulated histidine phosphorylation is oncogenic
metabolism
LHPP is a protein histidine phosphatase and tumour suppressor, suggesting that deregulated histidine phosphorylation is oncogenic
metabolism
-
the enzyme targets a phosphotransferase system. A model is suggested in which SixA removes phosphoryl groups from the PTSNtr by acting on NPr. The PTSNtr is a widely conserved bacterial pathway that regulates diverse metabolic processes through the phosphorylation states of its protein components, EINtr, NPr, and EIIANtr, which receive phosphoryl groups on histidine residues
-
physiological function
-
enzyme overexpression reduces the acetylcholine level and induces cell death
physiological function
enzyme overexpression induces apoptosis in umbilical-vein endothelial cells
physiological function
the enzyme is involved in cytoskeletal reorganization and therfore is functionally important in lung cancer cell migration and the invasion of lung cancer cells, mediated partly through modulation of actin cytoskeleton rearrangement
physiological function
-
the enzyme plays a regulatory role in a G protein-sensitive step involved in nutrient-induced insulin secretion. The enzyme is not involved in metabolic cell viability and cell proliferation
physiological function
the enzyme does not affects ArcB/ArcA signaling in vivo
physiological function
critical role for PHPT-1 in normal pancreatic b-cell function
physiological function
role for PHP14 in the dynamic regulation of the actin cytoskeleton and cell migration
physiological function
the enzyme (PHP14) regulates hepatic stellate cells migration in liver fibrosis via mediating TGF-beta1 signaling to PI3Kgamma/AKT/Rac1 pathway
physiological function
the enzyme plays a central role to negatively regulate CD4+ T cells. It specifically associates with and dephosphorylates the catalytic histidine (H118) on nucleoside diphosphate kinase B (NDPK-B). By dephosphorylating NDPK-B, the enzyme (PGAM5) negatively regulates CD4+ T cells by inhibiting NDPK-B mediated histidine phosphorylation and activation of the K+ channel KCa3.1, which is required for T cell receptor stimulated Ca2+ influx and cytokine production
physiological function
the enzyme is upregulated in fibrotic liver tissue and involved in the migration and lamellipodia formation of hepatic stellate cells. The enzyme regulates macrophage recruitment, infiltration, and migration by affecting podosome formation of macrophages
physiological function
the enzyme is involved in tumor progression in HCC, lung, pancreatic cancer, and clear cell renal carcinoma
physiological function
enzyme knockdown promotes brown adipocyte differentiation whereas ectopic expression of the enzyme suppresses brown adipocyte differentiation
physiological function
the enzyme acts as a regulator of His-Asp phosphorelay
physiological function
the enzyme induces phenotypic maturation in chicken dendritic cells, activates TLR signaling and inhibits Wnt signaling, increases dendritic cell-mediated T cell proliferation and CD4+ cell differentiation, and upregulates expression of pro-inflammatory cytokines (interleukin-12 and interferon-gamma)
physiological function
-
the enzyme does not affects ArcB/ArcA signaling in vivo
-
additional information
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
additional information
-
H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. H2O2-induced oxidation does not impact hPHPT1 function negatively
Show AA Sequence and Transmembrane Helices (1239 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13700
13701
14000
16000
16000
-
x * 16000, MALDI-TOF mass spectrometry or SDS-PAGE, the enzyme forms multimers consisting of up to more than 35 protein molecules
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
multimer
-
x * 16000, MALDI-TOF mass spectrometry or SDS-PAGE, the enzyme forms multimers consisting of up to more than 35 protein molecules
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, with 20 mM CaCl2, 50 mM NaCl, 0.5 mM dithiothreitol and 6% (w/v) PEG 6 K using a reservoir containing 100 mM MES-K buffer (pH 6.6), 40 mM CaCl2, 50 mM NaCl and 12% (w/v) PEG 6 K at 10°C
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M Bis-tris, pH 5.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C73A
H53A
R45A
the specific activity of the mutant is decreased by one order of magnitude compared to the wild type enzyme
R78A
the specific activity of the mutant is decreased by about 30% compared to the wild type enzyme
S112E
the phosphomimetic mutant is able to efficiently dephosphorylate substrates
H105A
the mutant enzyme shows no dephosphorylation of nucleoside diphosphate kinase B
additional information
-
deletion of 9 N-terminal amino acids results in inactive enzyme, while 4 C-terminal residues can be deleted without losing enzyme activity
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Mono-Q column chromatography, and Sephacryl S-100 gel filtration
DEAE-cellulose column chromatography, Sephadex G-200 gel filtration, Mono-Q column chromatography, and Superose 12 gel filtration
MonoQ column chromatography
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
-
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
-
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
-
DEAE-cellulose column chromatography, Sephadex G-200 gel filtration, Mono-Q column chromatography, and Superose 12 gel filtration
DEAE-cellulose column chromatography, Sephadex G-200 gel filtration, Mono-Q column chromatography, and Superose 12 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in SH-SY5Y cells and in primary cultures of cortical neurons from embryonic (E19) rats
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulated specifically in tumours
long-term exposure (24 h) of INS 832/13 cells or rat islets to high glucose (30 mM) increases the expression of the enzyme. Such increases in enzyme expression are also seen in islets derived from the Zucker diabetic fatty rat compared with islets from the lean control animals
-
PHP14 expression is upregulated in fibrotic liver and mainly in hepatic stellate cells. TGF-beta1 can induce PHP14 expression in hepatic stellate cells accompanied with the activation of hepatic stellate cells
the enzyme expression levels do not change during white adipocyte differentiation
the expression level of the enzyme is significantly decreased at an early stage of brown adipocyte differentiation (day 2) and then recovers at a late phase of differentiation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
high PHPT1 expression levels are associated with larger tumour size, higher Fuhrman nuclear grade and advanced pathological tumor-node-metastasis stage in clear-cell renal cell carcinoma
medicine
-
the knockdown of enzyme expression by lentivirus delivered siRNA is a therapeutic approach for the treatment of hepatocellular carcinoma
medicine
the enzyme is a therapeutic target for liver fibrosis. Fibrosis-associated inflammatory infiltration is significantly suppressed after enzyme knockdown
medicine
the enzyme can be used for the development of novel vaccines to control Eimeria tenella infection in chicken
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hamada, K.; Kato, M.; Mizuno, T.; Hakoshima, T.
Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay
Acta Crystallogr. Sect. D
55
269-271
1999
Escherichia coli (P76502), Escherichia coli
brenda
Kamath, V.; Kyathanahalli, C.N.; Jayaram, B.; Syed, I.; Olson, L.K.; Ludwig, K.; Klumpp, S.; Krieglstein, J.; Kowluru, A.
Regulation of glucose- and mitochondrial fuel-induced insulin secretion by a cytosolic protein histidine phosphatase in pancreatic beta-cells
Am. J. Physiol. Endocrinol. Metab.
299
E276-E286
2010
Rattus norvegicus
brenda
Klumpp, S.; Bechmann, G.; Maeurer, A.; Selke, D.; Krieglstein, J.
ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates
Biochem. Biophys. Res. Commun.
306
110-115
2003
Oryctolagus cuniculus
brenda
Ma, R.; Kanders, E.; Sundh, U.B.; Geng, M.; Ek, P.; Zetterqvist, O.; Li, J.P.
Mutational study of human phosphohistidine phosphatase: effect on enzymatic activity
Biochem. Biophys. Res. Commun.
337
887-891
2005
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Wong, C.; Faiola, B.; Wu, W.; Kennelly, P.J.
Phosphohistidine and phospholysine phosphatase activities in the rat: potential protein-lysine and protein-histidine phosphatases?
Biochem. J.
296
293-296
1993
Rattus norvegicus
brenda
Gong, W.; Li, Y.; Cui, G.; Hu, J.; Fang, H.; Jin, C.; Xia, B.
Solution structure and catalytic mechanism of human protein histidine phosphatase 1
Biochem. J.
418
337-344
2009
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Attwood, P.V.; Ludwig, K.; Bergander, K.; Besant, P.G.; Adina-Zada, A.; Krieglstein, J.; Klumpp, S.
Chemical phosphorylation of histidine-containing peptides based on the sequence of histone H4 and their dephosphorylation by protein histidine phosphatase
Biochim. Biophys. Acta
1804
199-205
2010
Homo sapiens
brenda
Klumpp, S.; Ma, N.T.; Baeumer, N.; Bechmann, G.; Krieglstein, J.
Relevance of glycine and cysteine residues as well as N- and C-terminals for the activity of protein histidine phosphatase
Biochim. Biophys. Acta
1804
206-211
2010
Homo sapiens
brenda
Eissing, A.; Fischer, D.; Rauch, I.; Baumann, A.; Schebb, N.H.; Karst, U.; Rose, K.; Klumpp, S.; Krieglstein, J.
Acetylcholine content and viability of cholinergic neurons are influenced by the activity of protein histidine phosphatase
BMC Neurosci.
13
31
2012
Mus musculus
brenda
Klumpp, S.; Faber, D.; Fischer, D.; Litterscheid, S.; Krieglstein, J.
Role of protein histidine phosphatase for viability of neuronal cells
Brain Res.
1264
7-12
2009
Homo sapiens
brenda
Seeger, A.; Rose, K.; Ma, N.T.; Kremmer, E.; Klumpp, S.; Krieglstein, J.
Influence of protein histidine phosphatase overexpression and down-regulation on human umbilical-vein endothelial cell viability
Cell Biol. Int.
36
245-249
2012
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Ek, P.; Pettersson, G.; Ek, B.; Gong, F.; Li, J.P.; Zetterqvist, O.
Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase
Eur. J. Biochem.
269
5016-5023
2002
Homo sapiens (Q9NRX4), Homo sapiens, Sus scrofa
brenda
Matthews, H.R.; MacKintosh, C.
Protein histidine phosphatase activity in rat liver and spinach leaves
FEBS Lett.
364
51-54
1995
Rattus norvegicus, Spinacia oleracea
brenda
Busam, R.D.; Thorsell, A.G.; Flores, A.; Hammarstroem, M.; Persson, C.; Hallberg, B.M.
First structure of a eukaryotic phosphohistidine phosphatase
J. Biol. Chem.
281
33830-33834
2006
Homo sapiens (Q9NRX4)
brenda
Klumpp, S.; Hermesmeier, J.; Selke, D.; Bechmann, G.; Van den Brulle, J.; Weidner, G.; Scharm, B.; Gussow, D.; Baumeister, R.; Kellner, R.; Krieglstein, J.
Protein histidine phosphatase: A novel enzyme with potency for neuronal signaling
J. Cereb. Blood Flow Metab.
22
1420-1424
2003
Caenorhabditis elegans, Mus musculus, Oryctolagus cuniculus (P83468), Rattus norvegicus
brenda
Shen, H.; Yang, P.; Liu, Q.; Tian, Y.
Nuclear expression and clinical significance of phosphohistidine phosphatase 1 in clear-cell renal cell carcinoma
J. Int. Med. Res.
43
747-757
2015
Homo sapiens
brenda
Xu, A.; Hao, J.; Zhang, Z.; Tian, T.; Jiang, S.; Hao, J.; Liu, C.; Huang, L.; Xiao, X.; He, D.
14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion
Lung Cancer
67
48-56
2010
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Hakoshima, T.; Ichihara, H.
Structure of SixA, a histidine protein phosphatase of the ArcB histidine-containing phosphotransfer domain in Escherichia coli
Methods Enzymol.
422
288-304
2007
Escherichia coli
brenda
Baeumer, N.; Maeurer, A.; Krieglstein, J.; Klumpp, S.
Expression of protein histidine phosphatase in Escherichia coli, purification, and determination of enzyme activity
Methods Mol. Biol.
365
247-260
2007
Escherichia coli
brenda
Han, S.X.; Wang, L.J.; Zhao, J.; Zhang, Y.; Li, M.; Zhou, X.; Wang, J.; Zhu, Q.
14-kDa phosphohistidine phosphatase plays an important role in hepatocellular carcinoma cell proliferation
Oncol. Lett.
4
658-664
2012
Homo sapiens
brenda
Ludwig, K.; Habbach, S.; Krieglstein, J.; Klumpp, S.; Koenig, S.
MALDI-TOF high mass calibration up to 200 kDa using human recombinant 16 kDa protein histidine phosphatase aggregates
PLoS ONE
6
e23612
2011
Homo sapiens
brenda
Srivastava, S.; Zhdanova, O.; Di, L.; Li, Z.; Albaqumi, M.; Wulff, H.; Skolnik, E.Y.
Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3.1
Proc. Natl. Acad. Sci. USA
105
14442-14446
2008
Homo sapiens
brenda
Ek, P.; Ek, B.; Zetterqvist, O.e.
Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine
Ups. J. Med. Sci.
120
20-27
2015
Homo sapiens
brenda
McCullough, B.S.; Barrios, A.M.
Facile, fluorogenic assay for protein histidine phosphatase activity
Biochemistry
57
2584-2589
2018
Homo sapiens (Q9NRX4)
brenda
Xu, A.; Li, X.; Li, S.; Sun, L.; Wu, S.; Zhang, B.; Huang, J.
A novel role for 14-kDa phosphohistidine phosphatase in lamellipodia formation
Cell Adh. Migr.
11
488-495
2017
Homo sapiens (Q9NRX4)
brenda
Srivastava, S.; Li, Z.; Soomro, I.; Sun, Y.; Wang, J.; Bao, L.; Coetzee, W.A.; Stanley, C.A.; Li, C.; Skolnik, E.Y.
Regulation of KATP channel trafficking in pancreatic bea-cells by protein histidine phosphorylation
Diabetes
67
849-860
2018
Mus musculus (Q9DAK9)
brenda
Wieland, T.; Attwood, P.V.
Alterations in reversible protein histidine phosphorylation as intracellular signals in cardiovascular disease
Front. Pharmacol.
6
173
2015
Mammalia
brenda
Xu, A.; Li, Y.; Zhao, W.; Hou, F.; Li, X.; Sun, L.; Chen, W.; Yang, A.; Wu, S.; Zhang, B.; Yao, J.; Wang, H.; Huang, J.
PHP14 regulates hepatic stellate cells migration in liver fibrosis via mediating TGF-beta1 signaling to PI3Kgama/AKT/Rac1 pathway
J. Mol. Med.
96
119-133
2018
Homo sapiens (Q9NRX4)
brenda
Schulte, J.E.; Goulian, M.
The phosphohistidine phosphatase SixA targets a phosphotransferase system
mBio
9
e01666-18
2018
Escherichia coli (P76502), Escherichia coli, Escherichia coli K12 (P76502)
brenda
Panda, S.; Srivastava, S.; Li, Z.; Vaeth, M.; Fuhs, S.R.; Hunter, T.; Skolnik, E.Y.
Identification of PGAM5 as a mammalian protein histidine phosphatase that plays a central role to negatively regulate CD4(+) T cells
Mol. Cell
63
457-469
2016
Mus musculus (Q8BX10)
brenda
Hindupur, S.K.; Colombi, M.; Fuhs, S.R.; Matter, M.S.; Guri, Y.; Adam, K.; Cornu, M.; Piscuoglio, S.; Ng, C.K.Y.; Betz, C.; Liko, D.; Quagliata, L.; Moes, S.; Jenoe, P.; Terracciano, L.M.; Heim, M.H.; Hunter, T.; Hall, M.N.
The protein histidine phosphatase LHPP is a tumour suppressor
Nature
555
678-682
2018
Homo sapiens (Q9H008), Homo sapiens, Mus musculus (Q9D7I5), Mus musculus
brenda
Martin, D.R.; Dutta, P.; Mahajan, S.; Varma, S.; Stevens, S.M.
Structural and activity characterization of human PHPT1 after oxidative modification
Sci. Rep.
6
23658
2016
Homo sapiens (Q9NRX4), Homo sapiens
brenda
Kim, H.J.; Jung, H.; Kim, S.; Seo, J.K.; Kee, J.M.
Identification of a target site for covalent inhibition of protein phosphohistidine phosphatase 1
ACS Med. Chem. Lett.
13
1911-1915
2022
Homo sapiens (Q9NRX4)
brenda
Xu, A.; Zhou, J.; Li, Y.; Qiao, L.; Jin, C.; Chen, W.; Sun, L.; Wu, S.; Li, X.; Zhou, D.; Jia, S.; Zhang, B.; Yao, J.; Zhang, X.; You, H.; Huang, J.
14-kDa phosphohistidine phosphatase is a potential therapeutic target for liver fibrosis
Am. J. Physiol. Gastrointest. Liver Physiol.
320
G351-G365
2021
Mus musculus (Q9DAK9)
brenda
Ning, J.; Sala, M.; Reina, J.; Kalagiri, R.; Hunter, T.; McCullough, B.S.
Histidine phosphorylation Protein kinases and phosphatases
Int. J. Mol. Sci.
25
7975
2024
Homo sapiens (Q9NRX4)
brenda
Schulte, J.E.; Roggiani, M.; Shi, H.; Zhu, J.; Goulian, M.
The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr
J. Biol. Chem.
296
100090
2021
Escherichia coli (P76502)
brenda
Kang, J.A.; Kang, H.S.; Bae, K.H.; Lee, S.C.; Oh, K.J.; Kim, W.K.
Roles of protein histidine phosphatase 1 (PHPT1) in brown adipocyte differentiation
J. Microbiol. Biotechnol.
30
306-312
2020
Mus musculus (Q9DAK9)
brenda
Rigden, D.J.
Protein phosphohistidine phosphatases of the HP superfamily
Methods Mol. Biol.
2077
93-107
2020
Escherichia coli (P76502)
brenda
Hunter, T.
A journey from phosphotyrosine to phosphohistidine and beyond
Mol. Cell
82
2190-2200
2022
Homo sapiens (Q9NRX4), Homo sapiens (Q9H008)
brenda
Lakho, S.A.; Haseeb, M.; Huang, J.; Hasan, M.W.; Khand, F.M.; Leghari, A.; Aleem, M.T.; Ali, H.; Song, X.; Xu, L.; Yan, R.; Li, X.
Eimeria tenella 14-kDa phosphohistidine phosphatase stimulates maturation of chicken dendritic cells and mediates DC-induced T cell priming in a Th1 cytokine interface
Res. Vet. Sci.
152
61-71
2022
Eimeria tenella (U6KXP8)
brenda
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