Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Qadota, H.; McGaha, L.A.; Mercer, K.B.; Stark, T.J.; Ferrara, T.M.; Benian, G.M.
    A novel protein phosphatase is a binding partner for the protein kinase domains of UNC-89 (obscurin) in Caenorhabditis elegans (2008), Mol. Biol. Cell, 19, 2424-2432.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.16 expressed in Saccharomyces cerevisiae and Escherichia coli Caenorhabditis elegans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.16 AlF4-
-
 Caenorhabditis elegans
3.1.3.16 BeF3-
-
 Caenorhabditis elegans
3.1.3.16 additional information SCPL-1 is not inhibited by the typical phosphatase inhibitors NaF, BeCl2, AlCl3, and Na3VO4 Caenorhabditis elegans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.16 Mg2+ SCPL-1 is dependent on Mg2+ Caenorhabditis elegans

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.16 Caenorhabditis elegans
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.16 muscle
-
 Caenorhabditis elegans
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.16 4-nitrophenyl phosphate + H2O
-
 Caenorhabditis elegans 4-nitrophenol + phosphate
-
 ?
3.1.3.16 UNC-89 + H2O the protein kinase 2 region of UNC-89 specifically interacts with SCPL-1 Caenorhabditis elegans ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.16 SCPL-1
-
 Caenorhabditis elegans
3.1.3.16 SCPL-1a isozyme Caenorhabditis elegans
3.1.3.16 SCPL-1b isozyme Caenorhabditis elegans
3.1.3.16 small CTD phosphatase-like-1 the protein contains a C-terminal domain phosphatase type domain Caenorhabditis elegans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.16 5
-
 around pH 5.0 Caenorhabditis elegans