Q91790 (DUS1A_XENLA) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 91. History...
Names and origin
|Protein names||Recommended name:|
Dual specificity protein phosphatase 1-A
|Organism||Xenopus laevis (African clawed frog)|
|Taxonomic identifier||8355 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus|
|Sequence length||369 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Expressed in XIK-2 kidney cells. Ref.1
Present in both immature and mature oocytes (at protein level). Expressed at a constant level during oocyte growth as well as during oocyte maturation. Levels decline somewhat during cleavage (stages 3-6). Levels rise dramatically during the mid-blastula transition. This higher level of expression is then maintained through gastrulation and all subsequent developmental stages. Ref.1
By serum stimulation, heat shock and oxidative stress. Ref.1
Phosphorylated by MAPK1/ERK2 at Thr-168 and at one or more serine residues in a progesterone-dependent manner. Phosphorylation reduces its rate of degradation but does not seem to affect phosphatase activity. Ref.2
Contains 1 rhodanese domain.
Contains 1 tyrosine-protein phosphatase domain.
|Gene Ontology (GO)|
|Biological_process||inactivation of MAPK activity|
Inferred from electronic annotation. Source: GOCmeiosis
Inferred from electronic annotation. Source: UniProtKB-KWmitotic cell cycle arrestnegative regulation of meiotic cell cyclepeptidyl-tyrosine dephosphorylation
Inferred from electronic annotation. Source: GOCresponse to stress
Inferred from electronic annotation. Source: UniProtKB-KW
|Molecular_function||MAP kinase tyrosine/serine/threonine phosphatase activity|
Inferred from electronic annotation. Source: InterProprotein tyrosine phosphatase activity
Inferred from electronic annotation. Source: UniProtKB-EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 369||369||Dual specificity protein phosphatase 1-A||PRO_0000421473|
|Domain||21 – 138||118||Rhodanese|
|Domain||175 – 369||195||Tyrosine-protein phosphatase|
|Active site||260||1||Phosphocysteine intermediate By similarity UniProtKB P28563|
Amino acid modifications
|Modified residue||168||1||Phosphothreonine; by MAPK1 Ref.2|
|Mutagenesis||168||1||T → E: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2|
|Mutagenesis||168||1||T → V: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2|
|Mutagenesis||260||1||C → S: Loss of phosphatase activity. Increases stability. Enables stable complex formation with active MAPK1. Abolishes threonine phosphorylation; when associated with E-168 or V-168. No effect on phosphatase activity and MAPK1 binding; when associated with E-168 or V-168. Ref.2|
|||"XCL100, an inducible nuclear MAP kinase phosphatase from Xenopus laevis: its role in MAP kinase inactivation in differentiated cells and its expression during early development."|
Lewis T., Groom L.A., Sneddon A.A., Smythe C., Keyse S.M.
J. Cell Sci. 108:2885-2896(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Tissue: Embryonic kidney.
|||"Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes."|
Sohaskey M.L., Ferrell J.E. Jr.
Mol. Biol. Cell 13:454-468(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-168, PHOSPHORYLATION AT SERINE RESIDUES, MUTAGENESIS OF THR-168 AND CYS-260.
|X83742 mRNA. Translation: CAA58710.1.|
AJ320158 mRNA. Translation: CAC44126.1.
|RefSeq||NP_001080570.1. NM_001087101.1. |
3D structure databases
|SMR||Q91790. Positions 173-315. |
Protocols and materials databases
Genome annotation databases
|Xenbase||XB-GENE-975062. dusp1. |
Family and domain databases
|Gene3D||18.104.22.168. 1 hit. |
|InterPro||IPR020417. Atypical_DUSP. |
|PANTHER||PTHR10159. PTHR10159. 1 hit. |
|Pfam||PF00782. DSPc. 1 hit. |
PF00581. Rhodanese. 1 hit.
|PIRSF||PIRSF000939. MAPK_Ptase. 1 hit. |
|PRINTS||PR01908. ADSPHPHTASE. |
|SMART||SM00195. DSPc. 1 hit. |
SM00450. RHOD. 1 hit.
|SUPFAM||SSF52821. SSF52821. 1 hit. |
|PROSITE||PS50206. RHODANESE_3. 1 hit. |
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
|Accession||Primary (citable) accession number: Q91790|
Secondary accession number(s): Q90W59
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families