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Protein

Dual specificity protein phosphatase 1-B

Gene

dusp1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei260Phosphocysteine intermediatePROSITE-ProRule annotationBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Meiosis

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 1-BBy similarity (EC:3.1.3.16By similarity, EC:3.1.3.48By similarity)
Alternative name(s):
XCL100-beta1 Publication
Gene namesi
Name:dusp1-bBy similarity
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004214741 – 369Dual specificity protein phosphatase 1-BAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei168Phosphothreonine; by MAPK1By similarity1

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ90W58.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 138RhodanesePROSITE-ProRule annotationAdd BLAST118
Domaini175 – 369Tyrosine-protein phosphataseSequence analysisCuratedAdd BLAST195

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

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00404. PTPc_motif. 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.

Q90W58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNMEICAMD CCVFKGLLAE RAHKCLILDC RSFFAFSSSS IIGSSNVRLS
60 70 80 90 100
TIVKRRAKGS MGLEHIIPNE EQRGRLVAGM YEAVVLLDER TSELDMLRKD
110 120 130 140 150
STMMLAVNAL SRDPRGSRIY FLKGGYETFS SQCPEFCNKN SPPVALSLPL
160 170 180 190 200
SPNNVPGSAD SNCTPCGTPL YDQGGPVEIL PFLYLGSAYH ASRKDMLEAL
210 220 230 240 250
GITALINVSA NCPNHFEGHF QYKSIPVEDS HKADISSWFN EAIDFIDSIK
260 270 280 290 300
TCGGRVFVHC QAGISRSATI CLAYLMRTNR VKLDEAFEFV KQRRSIISPN
310 320 330 340 350
FSFMGQLLQF ESQVLAPSCS AEAGSPTISV LDRGTSTTTV FNFPVSIPVH
360
SGANSLSYLQ NPITTSPSC
Length:369
Mass (Da):40,363
Last modified:December 1, 2001 - v1
Checksum:i5E280CA6EF633CC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ320159 mRNA. Translation: CAC44127.1.
RefSeqiNP_001082153.1. NM_001088684.1.
UniGeneiXl.2803.

Genome annotation databases

GeneIDi398254.
KEGGixla:398254.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ320159 mRNA. Translation: CAC44127.1.
RefSeqiNP_001082153.1. NM_001088684.1.
UniGeneiXl.2803.

3D structure databases

ProteinModelPortaliQ90W58.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398254.
KEGGixla:398254.

Organism-specific databases

CTDi398254.

Phylogenomic databases

HOVERGENiHBG007347.
KOiK04459.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00404. PTPc_motif. 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...

Entry informationi

Entry nameiDUS1B_XENLA
AccessioniPrimary (citable) accession number: Q90W58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 82 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

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 one 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.