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Protein

Dual specificity protein phosphatase 10

Gene

DUSP10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation2 Publications
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei408Phosphocysteine intermediate2 Publications1

GO - Molecular functioni

  • MAP kinase phosphatase activity Source: UniProtKB
  • MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  • phosphatase activity Source: UniProtKB
  • phosphoprotein phosphatase activity Source: ProtInc
  • protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS07066-MONOMER.
BRENDAi3.1.3.16. 2681.
3.1.3.48. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ9Y6W6.
SIGNORiQ9Y6W6.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 10 (EC:3.1.3.162 Publications, EC:3.1.3.482 Publications)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 5
Short name:
MAP kinase phosphatase 5
Short name:
MKP-5
Gene namesi
Name:DUSP10
Synonyms:MKP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3065. DUSP10.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • Golgi apparatus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180 – 181FM → DD: Reduced enzyme activity with MAPK14. 1 Publication2
Mutagenesisi203 – 204RR → AA: Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14. 1 Publication2

Organism-specific databases

DisGeNETi11221.
OpenTargetsiENSG00000143507.
PharmGKBiPA27520.

Chemistry databases

ChEMBLiCHEMBL2396511.

Polymorphism and mutation databases

BioMutaiDUSP10.
DMDMi20138090.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000948131 – 482Dual specificity protein phosphatase 10Add BLAST482

Proteomic databases

PaxDbiQ9Y6W6.
PeptideAtlasiQ9Y6W6.
PRIDEiQ9Y6W6.

PTM databases

DEPODiQ9Y6W6.
iPTMnetiQ9Y6W6.
PhosphoSitePlusiQ9Y6W6.

Expressioni

Tissue specificityi

Detected in brain.1 Publication

Gene expression databases

BgeeiENSG00000143507.
CleanExiHS_DUSP10.
ExpressionAtlasiQ9Y6W6. baseline and differential.
GenevisibleiQ9Y6W6. HS.

Organism-specific databases

HPAiHPA016758.

Interactioni

Subunit structurei

Monomer. Interacts with MAPK14.3 Publications

Protein-protein interaction databases

BioGridi116389. 15 interactors.
IntActiQ9Y6W6. 10 interactors.
MINTiMINT-8208613.
STRINGi9606.ENSP00000355866.

Chemistry databases

BindingDBiQ9Y6W6.

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi152 – 160Combined sources9
Beta strandi173 – 176Combined sources4
Helixi180 – 185Combined sources6
Beta strandi186 – 188Combined sources3
Helixi199 – 206Combined sources8
Helixi212 – 217Combined sources6
Helixi224 – 230Combined sources7
Beta strandi233 – 236Combined sources4
Helixi243 – 245Combined sources3
Beta strandi248 – 250Combined sources3
Helixi251 – 261Combined sources11
Beta strandi267 – 269Combined sources3
Helixi272 – 276Combined sources5
Turni277 – 279Combined sources3
Helixi281 – 283Combined sources3
Beta strandi284 – 286Combined sources3
Beta strandi323 – 326Combined sources4
Beta strandi329 – 332Combined sources4
Helixi336 – 338Combined sources3
Helixi340 – 345Combined sources6
Beta strandi348 – 353Combined sources6
Beta strandi356 – 358Combined sources3
Helixi363 – 365Combined sources3
Beta strandi368 – 372Combined sources5
Beta strandi378 – 380Combined sources3
Helixi384 – 386Combined sources3
Helixi387 – 399Combined sources13
Beta strandi403 – 407Combined sources5
Beta strandi409 – 413Combined sources5
Helixi414 – 426Combined sources13
Helixi431 – 441Combined sources11
Helixi449 – 463Combined sources15
Helixi478 – 482Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZZWX-ray1.60A/B320-467[»]
2OUCX-ray2.20A/B148-287[»]
2OUDX-ray2.80A315-482[»]
3TG1X-ray2.71B139-288[»]
ProteinModelPortaliQ9Y6W6.
SMRiQ9Y6W6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6W6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini168 – 285RhodanesePROSITE-ProRule annotationAdd BLAST118
Domaini384 – 453Tyrosine-protein phosphataseAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 215Interaction with MAP kinasesAdd BLAST17

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9Y6W6.
KOiK20216.
OMAiKKMTKCS.
OrthoDBiEOG091G0V6S.
PhylomeDBiQ9Y6W6.
TreeFamiTF105122.

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.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y6W6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV
60 70 80 90 100
VSLKAANLTY MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG
110 120 130 140 150
TTTTAIGTST TCPANQMVNN NENTGSLSPS SGVGSPVSGT PKQLASIKII
160 170 180 190 200
YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF MEYNKSHIQG AVHINCADKI
210 220 230 240 250
SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT NEPSRVMPSQ
260 270 280 290 300
PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA
310 320 330 340 350
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY
360 370 380 390 400
VINVTTHLPL YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC
410 420 430 440 450
GKGLLIHCQA GVSRSATIVI AYLMKHTRMT MTDAYKFVKG KRPIISPNLN
460 470 480
FMGQLLEFEE DLNNGVTPRI LTPKLMGVET VV
Length:482
Mass (Da):52,642
Last modified:November 1, 1999 - v1
Checksum:iA8CB74ABF9498CD4
GO
Isoform 2 (identifier: Q9Y6W6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-342: Missing.

Show »
Length:140
Mass (Da):16,110
Checksum:iCE151F365D042516
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0365491 – 342Missing in isoform 2. 2 PublicationsAdd BLAST342

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026436 mRNA. Translation: BAA81668.1.
AF179212 mRNA. Translation: AAD51857.1.
AK022513 mRNA. Translation: BAB14070.1.
AL590966 Genomic DNA. Translation: CAH71120.1.
CH471100 Genomic DNA. Translation: EAW93283.1.
CH471100 Genomic DNA. Translation: EAW93285.1.
CH471100 Genomic DNA. Translation: EAW93286.1.
CH471100 Genomic DNA. Translation: EAW93287.1.
BC020608 mRNA. Translation: AAH20608.1.
BC031405 mRNA. Translation: AAH31405.1.
BC063826 mRNA. Translation: AAH63826.1.
CCDSiCCDS1528.1. [Q9Y6W6-1]
RefSeqiNP_009138.1. NM_007207.5. [Q9Y6W6-1]
UniGeneiHs.497822.
Hs.732301.

Genome annotation databases

EnsembliENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
GeneIDi11221.
KEGGihsa:11221.
UCSCiuc001hmy.3. human. [Q9Y6W6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026436 mRNA. Translation: BAA81668.1.
AF179212 mRNA. Translation: AAD51857.1.
AK022513 mRNA. Translation: BAB14070.1.
AL590966 Genomic DNA. Translation: CAH71120.1.
CH471100 Genomic DNA. Translation: EAW93283.1.
CH471100 Genomic DNA. Translation: EAW93285.1.
CH471100 Genomic DNA. Translation: EAW93286.1.
CH471100 Genomic DNA. Translation: EAW93287.1.
BC020608 mRNA. Translation: AAH20608.1.
BC031405 mRNA. Translation: AAH31405.1.
BC063826 mRNA. Translation: AAH63826.1.
CCDSiCCDS1528.1. [Q9Y6W6-1]
RefSeqiNP_009138.1. NM_007207.5. [Q9Y6W6-1]
UniGeneiHs.497822.
Hs.732301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZZWX-ray1.60A/B320-467[»]
2OUCX-ray2.20A/B148-287[»]
2OUDX-ray2.80A315-482[»]
3TG1X-ray2.71B139-288[»]
ProteinModelPortaliQ9Y6W6.
SMRiQ9Y6W6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116389. 15 interactors.
IntActiQ9Y6W6. 10 interactors.
MINTiMINT-8208613.
STRINGi9606.ENSP00000355866.

Chemistry databases

BindingDBiQ9Y6W6.
ChEMBLiCHEMBL2396511.

PTM databases

DEPODiQ9Y6W6.
iPTMnetiQ9Y6W6.
PhosphoSitePlusiQ9Y6W6.

Polymorphism and mutation databases

BioMutaiDUSP10.
DMDMi20138090.

Proteomic databases

PaxDbiQ9Y6W6.
PeptideAtlasiQ9Y6W6.
PRIDEiQ9Y6W6.

Protocols and materials databases

DNASUi11221.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
GeneIDi11221.
KEGGihsa:11221.
UCSCiuc001hmy.3. human. [Q9Y6W6-1]

Organism-specific databases

CTDi11221.
DisGeNETi11221.
GeneCardsiDUSP10.
HGNCiHGNC:3065. DUSP10.
HPAiHPA016758.
MIMi608867. gene.
neXtProtiNX_Q9Y6W6.
OpenTargetsiENSG00000143507.
PharmGKBiPA27520.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9Y6W6.
KOiK20216.
OMAiKKMTKCS.
OrthoDBiEOG091G0V6S.
PhylomeDBiQ9Y6W6.
TreeFamiTF105122.

Enzyme and pathway databases

BioCyciZFISH:HS07066-MONOMER.
BRENDAi3.1.3.16. 2681.
3.1.3.48. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ9Y6W6.
SIGNORiQ9Y6W6.

Miscellaneous databases

ChiTaRSiDUSP10. human.
EvolutionaryTraceiQ9Y6W6.
GeneWikiiDUSP10.
GenomeRNAii11221.
PROiQ9Y6W6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143507.
CleanExiHS_DUSP10.
ExpressionAtlasiQ9Y6W6. baseline and differential.
GenevisibleiQ9Y6W6. HS.

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.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
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...

Entry informationi

Entry nameiDUS10_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6W6
Secondary accession number(s): D3DTB4, Q6GSI4, Q9H9Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.