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Protein

Dual specificity protein phosphatase 1-A

Gene

dusp1-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity during the meiotic cell cycle.2 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.2 PublicationsPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei260 – 2601Phosphocysteine intermediateBy similarityPROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. inactivation of MAPK activity Source: UniProtKB
  2. meiotic cell cycle Source: UniProtKB-KW
  3. mitotic cell cycle arrest Source: UniProtKB
  4. negative regulation of MAPK cascade Source: UniProtKB
  5. negative regulation of meiotic cell cycle Source: UniProtKB
  6. peptidyl-threonine dephosphorylation Source: UniProtKB
  7. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  8. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Meiosis, Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 1-A (EC:3.1.3.162 Publications, EC:3.1.3.482 Publications)
Alternative name(s):
XCL1001 Publication
XCL100-alfa1 Publication
Gene namesi
Name:dusp1-aImported
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-975062. dusp1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681T → E: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. 1 Publication
Mutagenesisi168 – 1681T → V: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. 1 Publication
Mutagenesisi260 – 2601C → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Dual specificity protein phosphatase 1-APRO_0000421473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681Phosphothreonine; by MAPK11 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

Expressed in XIK-2 kidney cells.1 Publication

Developmental stagei

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.1 Publication

Inductioni

By serum stimulation, heat shock and oxidative stress.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ91790.
SMRiQ91790. Positions 173-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 138118RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini175 – 369195Tyrosine-protein phosphataseCuratedSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.Sequence Analysis

Phylogenomic databases

HOVERGENiHBG007347.
KOiK04459.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91790-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVNMETCAMD CCVLKALLAE RAHKCLILDC RSFFSFSSCS IVGSSNVRLS
60 70 80 90 100
TIVKRRAKGS MGLEHIVPNE EQRCRLVAGM YEAVVLLDER TSELDMLRKD
110 120 130 140 150
STMMLAVNAL CRDSRGSSIY FLKGGYETFS AQCPEFCTKN SPPVGLSLPL
160 170 180 190 200
CANNVPGSAD SNCTPCGTPL YDQGGPVEIL PFLYLGSAYH ASRKDMLDTL
210 220 230 240 250
GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN EAIDFIDSVK
260 270 280 290 300
NSGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
310 320 330 340 350
FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH
360
SGANSLSYLQ NPITTSPSC
Length:369
Mass (Da):40,264
Last modified:November 1, 1996 - v1
Checksum:i14336CA5EC35AAF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83742 mRNA. Translation: CAA58710.1.
AJ320158 mRNA. Translation: CAC44126.1.
RefSeqiNP_001080570.1. NM_001087101.1.
UniGeneiXl.1243.

Genome annotation databases

GeneIDi380262.
KEGGixla:380262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83742 mRNA. Translation: CAA58710.1.
AJ320158 mRNA. Translation: CAC44126.1.
RefSeqiNP_001080570.1. NM_001087101.1.
UniGeneiXl.1243.

3D structure databases

ProteinModelPortaliQ91790.
SMRiQ91790. Positions 173-315.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi380262.
KEGGixla:380262.

Organism-specific databases

CTDi1843.
XenbaseiXB-GENE-975062. dusp1.

Phylogenomic databases

HOVERGENiHBG007347.
KOiK04459.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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 kidney1 Publication.
  2. "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.
    Tissue: OvaryImported.

Entry informationi

Entry nameiDUS1A_XENLA
AccessioniPrimary (citable) accession number: Q91790
Secondary accession number(s): Q90W59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.