EC number:3.1.3.16

Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.16
Description:Protein-serine/threonine phosphatase.
Alternative Name: Serine/threonine specific protein phosphatase.
Protein phosphatase-2C.
Protein phosphatase-2B.
Protein phosphatase-2A.
Protein phosphatase-1.
Prosite: PDOC50969; PDOC00792; PDOC00785; PDOC00115;
PDB:
PDBScop
3N3C 8091321; 8091322;
3MQ3 8091321; 8091322;
4N0G 8091312; 8091313; 8091312; 8091313;
4YZG 8091309; 8091310; 8091309; 8091310;
4YZH 8091309; 8091310;
 » show all
Cath: 1.10.10.430; 1.10.1740.220; 1.10.238.10; 1.10.287.1920; 1.20.5.1840; 1.20.5.2760; 3.30.450.350; 3.60.21.10; 3.60.40.10; 3.90.190.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.16
BRENDA Enzyme Link: BRENDA 3.1.3.16
KEGG Enzyme Link: KEGG3.1.3.16
BioCyc Enzyme Link: BioCyc 3.1.3.16
ExPASy Enzyme Link: ExPASy3.1.3.16
EC2PDB Enzyme Link: EC2PDB 3.1.3.16
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.16
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.16
IntEnz Enzyme Link: IntEnz 3.1.3.16
MEDLINE Enzyme Link: MEDLINE 3.1.3.16

EC number:3.1.3.16

MSA:

3.1.3.16;
Phylogenetic Tree:

3.1.3.16;
Uniprot:
M-CSA:
RHEA:47004 H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities.Ingebritsen TS, Cohen P1983 May 26301824
The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle.Tonks NK, Cohen P1984 Nov 156092084
Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein.Deutscher J, Kessler U, Hengstenberg W1985 Sep2993239
CSTP1, a novel protein phosphatase, blocks cell cycle, promotes cell apoptosis, and suppresses tumor growth of bladder cancer by directly dephosphorylating Akt at Ser473 site.Zhuo DX, Zhang XW, Jin B, Zhang Z, Xie BS, Wu CL, Gong K, Mao ZB201323799035
Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase.Zheng H, Ji C, Gu S, Shi B, Wang J, Xie Y, Mao Y2005 Jun 1715883030
Substrate specificity of phosphoprotein phosphatase from spleen.SUNDARARAJAN TA, SARMA PS1959 Mar13638262
C-terminal domain phosphatase-like family members (AtCPLs) differentially regulate Arabidopsis thaliana abiotic stress signaling, growth, and development.Koiwa H, Barb AW, Xiong L, Li F, McCully MG, Lee BH, Sokolchik I, Zhu J, Gong Z, Reddy M, Sharkhuu A, Manabe Y, Yokoi S, Zhu JK, Bressan RA, Hasegawa PM2002 Aug 612149434
Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.Hausmann S, Shuman S2002 Jun 1411934898
RHEA:20629 H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities.Ingebritsen TS, Cohen P1983 May 26301824
The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle.Tonks NK, Cohen P1984 Nov 156092084
Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein.Deutscher J, Kessler U, Hengstenberg W1985 Sep2993239
CSTP1, a novel protein phosphatase, blocks cell cycle, promotes cell apoptosis, and suppresses tumor growth of bladder cancer by directly dephosphorylating Akt at Ser473 site.Zhuo DX, Zhang XW, Jin B, Zhang Z, Xie BS, Wu CL, Gong K, Mao ZB201323799035
Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase.Zheng H, Ji C, Gu S, Shi B, Wang J, Xie Y, Mao Y2005 Jun 1715883030
Substrate specificity of phosphoprotein phosphatase from spleen.SUNDARARAJAN TA, SARMA PS1959 Mar13638262
C-terminal domain phosphatase-like family members (AtCPLs) differentially regulate Arabidopsis thaliana abiotic stress signaling, growth, and development.Koiwa H, Barb AW, Xiong L, Li F, McCully MG, Lee BH, Sokolchik I, Zhu J, Gong Z, Reddy M, Sharkhuu A, Manabe Y, Yokoi S, Zhu JK, Bressan RA, Hasegawa PM2002 Aug 612149434
Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.Hausmann S, Shuman S2002 Jun 1411934898