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There are several matches for 'phosphoserine phosphatase'.
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10668 matches
showing page 1 of 534
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protein
1)
Homo sapiens
PSPH -
Phosphoserine
phosphatase
; Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates; Belongs to the HAD-like hydrolase superfamily. SerB family.
[a.k.a. ENSP00000390952, ENST00000427797.5, PSPH-209,
Phosphoserine phosphatase
,
phosphoserine phosphatase
, ...]
2)
Mus musculus
Psph -
Phosphoserine
phosphatase
; Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity); Belongs to the HAD-like hydrolase superfamily. SerB family.
[a.k.a. ENSMUST00000178244, XM_017320574.1, XP_030109871,
Phosphoserine phosphatase
]
3)
Drosophila melanogaster
aay -
Phosphoserine
phosphatase
; Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity); Belongs to the HAD-like hydrolase superfamily. SerB family.
[a.k.a. FBgn0023129, aay-PA, 39085,
Phosphoserine phosphatase
]
4)
Caenorhabditis elegans
Y62E10A.13 - Uncharacterized protein.
[a.k.a. Y62E10A.13f, NP_001293892, 178304,
Phosphoserine phosphatase
]
5)
Escherichia coli K12
serB - 3-
phosphoserine
phosphatase
; Catalyzes the dephosphorylation of
phosphoserine
(P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr). Belongs to the HAD-like hydrolase superfamily. SerB family.
[a.k.a. b4388, AAC77341.1, ECK4380,
Phosphoserine phosphatase
]
6)
Saccharomyces cerevisiae
SER2 -
Phosphoserine
phosphatase
of the phosphoglycerate pathway; involved in serine and glycine biosynthesis, expression is regulated by the available nitrogen source.
[a.k.a. YGR208W, NP_011724.1, G7744,
phosphoserine phosphatase
,
Phosphoserine phosphatase
, ...]
7)
Homo sapiens
DUSP5 - Dual specificity protein
phosphatase
5; Dual specificity protein
phosphatase
; active with phosphotyrosine,
phosphoserine
and phosphothreonine residues. The highest relative activity is toward ERK1; Belongs to the protein-tyrosine
phosphatase
family. Non- receptor class dual specificity subfamily.
[a.k.a. 3.1.3.16, U16996, R-HSA-112409]
8)
Homo sapiens
DUPD1 - Dual specificity
phosphatase
DUPD1; Dual specificity
phosphatase
able to dephosphorylate phosphotyrosine,
phosphoserine
and phosphothreonine residues, with a preference for phosphotyrosine as a substrate. Belongs to the protein-tyrosine
phosphatase
family. Non- receptor class dual specificity subfamily.
[a.k.a. XP_011538049.1, 3.1.3.16, CCDS31223.1]
9)
Homo sapiens
DUSP12 - Dual specificity protein
phosphatase
12; Dual specificity
phosphatase
; can dephosphorylate both phosphotyrosine and
phosphoserine
or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro) (By similarity). Has
phosphatase
activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates.
[a.k.a. 3.1.3.16, BT006633, ENSG00000081721]
10)
Homo sapiens
DUSP8 - Dual specificity protein
phosphatase
8; Has
phosphatase
activity with synthetic
phosphatase
substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation. Expected to display protein
phosphatase
activity toward phosphotyrosine,
phosphoserine
and phosphothreonine residues.
[a.k.a. Dual specificity protein phosphatase hVH-5, 3.1.3.16, XP_011518235]
11)
Homo sapiens
CDKN3 - Cyclin-dependent kinase inhibitor 3; May play a role in cell cycle regulation. Dual specificity
phosphatase
active toward substrates containing either phosphotyrosine or
phosphoserine
residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner.
[a.k.a. NP_001317102, 3.1.3.16, ENSP00000480289]
12)
Homo sapiens
MTM1 - Myotubularin; Lipid
phosphatase
which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and
phosphoserine
-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not fo [...]
[a.k.a. XM_011531173, AAC51682.1, LRG_839]
13)
Homo sapiens
DUSP28 - Dual specificity
phosphatase
28; Has
phosphatase
activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with
phosphoserine
. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site ; Belongs to the protein-tyrosine
phosphatase
family. Non- receptor class dual specificity subfamily.
[a.k.a. 3.1.3.16, NP_001028747, CCDS33418.1]
14)
Mus musculus
Dusp12 - Dual specificity protein
phosphatase
12; Dual specificity
phosphatase
; can dephosphorylate both phosphotyrosine and
phosphoserine
or phosphothreonine residues. Can dephosphorylate glucokinase (in vitro). Has
phosphatase
activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate and other in vitro substrates.
[a.k.a. 3.1.3.16, ENSMUST00000163252, BAB23328.1]
15)
Mus musculus
Dupd1 - Dual specificity
phosphatase
DUPD1; Dual specificity
phosphatase
able to dephosphorylate phosphotyrosine,
phosphoserine
and phosphothreonine residues, with a preference for phosphotyrosine as a substrate.
[a.k.a. 3.1.3.16, ENSMUSG00000063821, ENSMUST00000073870]
16)
Mus musculus
Dusp8 - Dual specificity protein
phosphatase
8; Has
phosphatase
activity with synthetic
phosphatase
substrates and negatively regulates mitogen-activated protein kinase activity, presumably by catalysing their dephosphorylation. Expected to display protein
phosphatase
activity toward phosphotyrosine,
phosphoserine
and phosphothreonine residues (Probable).
[a.k.a. 3.1.3.16, Neuronal tyrosine threonine phosphatase 1, uc009kmo.2]
17)
Mus musculus
Cdkn3 - Cyclin-dependent kinase inhibitor 3; May play a role in cell cycle regulation. Dual specificity
phosphatase
active toward substrates containing either phosphotyrosine or
phosphoserine
residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner (By similarity).
[a.k.a. 3.1.3.16, CCDS49466.1, XM_006519594.3]
18)
Mus musculus
Epm2a - Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen
phosphatase
, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with
phosphoserine
and phosphothreonine substrates (in vitro). Has also been shown to dephosphorylate MAPT. Shows strong
phosphatase
activity towards complex carbohy [...]
[a.k.a. 3.1.3.16, laforin, NM_010146]
19)
Mus musculus
Mtm1 - Myotubularin; Lipid
phosphatase
which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been shown to dephosphorylate phosphotyrosine- and
phosphoserine
-containing peptides. Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome. Plays a role in vacuolar formation and morphology (By similarity). Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle mainte [...]
[a.k.a. Mtm1-213, NM_019926.3, ENSMUST00000134859]
20)
Mus musculus
Dusp28 - Dual specificity
phosphatase
28; Has
phosphatase
activity with the synthetic substrate 6,8- difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with
phosphoserine
. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site.
[a.k.a. 3.1.3.16, BAE37397.1, uc007cbu.1]
10668 matches
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