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Q91790 (DUS1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 1-A

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
XCL100
XCL100-alfa
Gene names
Name:dusp1-a
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-188' and 'Tyr-190', regulating its activity during the meiotic cell cycle. Ref.1 Ref.2

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.1 Ref.2

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.1 Ref.2

Subcellular location

Nucleus Ref.1.

Tissue specificity

Expressed in XIK-2 kidney cells. Ref.1

Developmental stage

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

Induction

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

Post-translational modification

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

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 rhodanese domain.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Dual specificity protein phosphatase 1-A
PRO_0000421473

Regions

Domain21 – 138118Rhodanese
Domain175 – 369195Tyrosine-protein phosphatase

Sites

Active site2601Phosphocysteine intermediate By similarity UniProtKB P28563

Amino acid modifications

Modified residue1681Phosphothreonine; by MAPK1 Ref.2

Experimental info

Mutagenesis1681T → E: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2
Mutagenesis1681T → V: Abolishes threonine phosphorylation; when associated with S-260. No effect on phosphatase activity and MAPK1 binding; when associated with S-260. Ref.2
Mutagenesis2601C → 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

Sequences

Sequence LengthMass (Da)Tools
Q91790 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 14336CA5EC35AAF7

FASTA36940,264
        10         20         30         40         50         60 
MVNMETCAMD CCVLKALLAE RAHKCLILDC RSFFSFSSCS IVGSSNVRLS TIVKRRAKGS 

        70         80         90        100        110        120 
MGLEHIVPNE EQRCRLVAGM YEAVVLLDER TSELDMLRKD STMMLAVNAL CRDSRGSSIY 

       130        140        150        160        170        180 
FLKGGYETFS AQCPEFCTKN SPPVGLSLPL CANNVPGSAD SNCTPCGTPL YDQGGPVEIL 

       190        200        210        220        230        240 
PFLYLGSAYH ASRKDMLDTL GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN 

       250        260        270        280        290        300 
EAIDFIDSVK NSGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN 

       310        320        330        340        350        360 
FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH SGANSLSYLQ 


NPITTSPSC 

« Hide

References

[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 kidney.
[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: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83742 mRNA. Translation: CAA58710.1.
AJ320158 mRNA. Translation: CAC44126.1.
RefSeqNP_001080570.1. NM_001087101.1.
UniGeneXl.1243.

3D structure databases

ProteinModelPortalQ91790.
SMRQ91790. Positions 173-315.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380262.
KEGGxla:380262.

Organism-specific databases

CTD1843.
XenbaseXB-GENE-975062. dusp1.

Phylogenomic databases

HOVERGENHBG007347.
KOK04459.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDUS1A_XENLA
AccessionPrimary (citable) accession number: Q91790
Secondary accession number(s): Q90W59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families