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Protein

Dual specificity protein phosphatase 5

Gene

DUSP5

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

Functioni

Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei263Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • activation of MAPK activity Source: Reactome
  • dephosphorylation Source: UniProtKB
  • endoderm formation Source: GO_Central
  • MAPK cascade Source: Reactome
  • peptidyl-threonine dephosphorylation Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS06468-MONOMER.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ16690.
SIGNORiQ16690.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 5 (EC:3.1.3.161 Publication, EC:3.1.3.481 Publication)
Alternative name(s):
Dual specificity protein phosphatase hVH3
Gene namesi
Name:DUSP5
Synonyms:VH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:3071. DUSP5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1847.
OpenTargetsiENSG00000138166.
PharmGKBiPA27528.

Chemistry databases

ChEMBLiCHEMBL1250380.

Polymorphism and mutation databases

BioMutaiDUSP5.
DMDMi215273975.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000948021 – 384Dual specificity protein phosphatase 5Add BLAST384

Proteomic databases

MaxQBiQ16690.
PaxDbiQ16690.
PeptideAtlasiQ16690.
PRIDEiQ16690.

PTM databases

DEPODiQ16690.
iPTMnetiQ16690.
PhosphoSitePlusiQ16690.

Expressioni

Gene expression databases

BgeeiENSG00000138166.
CleanExiHS_DUSP5.
GenevisibleiQ16690. HS.

Organism-specific databases

HPAiHPA055143.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284824EBI-7487376,EBI-959949

Protein-protein interaction databases

BioGridi108180. 2 interactors.
IntActiQ16690. 1 interactor.
MINTiMINT-8277166.
STRINGi9606.ENSP00000358596.

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi180 – 183Combined sources4
Beta strandi186 – 190Combined sources5
Helixi191 – 194Combined sources4
Helixi197 – 203Combined sources7
Beta strandi207 – 210Combined sources4
Beta strandi223 – 227Combined sources5
Helixi239 – 241Combined sources3
Helixi242 – 254Combined sources13
Beta strandi259 – 268Combined sources10
Helixi269 – 282Combined sources14
Helixi286 – 296Combined sources11
Helixi304 – 317Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G6ZX-ray2.70A/B/C178-384[»]
ProteinModelPortaliQ16690.
SMRiQ16690.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16690.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 141RhodanesePROSITE-ProRule annotationAdd BLAST123
Domaini180 – 384Tyrosine-protein phosphataseAdd BLAST205

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi53 – 74Nuclear localization signalSequence analysisAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi79 – 82Poly-Gly4

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ16690.
KOiK04459.
OMAiTICMAYI.
OrthoDBiEOG091G0249.
PhylomeDBiQ16690.
TreeFamiTF105122.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. 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.

Q16690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV
60 70 80 90 100
VLRRARGGAV SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR
110 120 130 140 150
EESAARVVLT SLLACLPAGP RVYFLKGGYE TFYSEYPECC VDVKPISQEK
160 170 180 190 200
IESERALISQ CGKPVVNVSY RPAYDQGGPV EILPFLYLGS AYHASKCEFL
210 220 230 240 250
ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS HFQEAIDFID
260 270 280 290 300
CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV
310 320 330 340 350
SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ
360 370 380
GAYCTFPASV LAPVPTHSTV SELSRSPVAT ATSC
Length:384
Mass (Da):42,047
Last modified:November 25, 2008 - v2
Checksum:i2E4B2938F886CB4E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 11RQL → GHV in AAA64693 (PubMed:7961985).Curated3
Sequence conflicti71A → R in AAA64693 (PubMed:7961985).Curated1
Sequence conflicti105 – 106AR → F in AAA64693 (PubMed:7961985).Curated2
Sequence conflicti220A → M in AAA64693 (PubMed:7961985).Curated1
Sequence conflicti220A → M in AAB06261 (PubMed:7836374).Curated1
Sequence conflicti220A → M in AAH62545 (PubMed:15489334).Curated1
Sequence conflicti382T → Q in AAA64693 (PubMed:7961985).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020298154E → D.Corresponds to variant rs2282238dbSNPEnsembl.1
Natural variantiVAR_059777220A → T.Corresponds to variant rs1889566dbSNPEnsembl.1
Natural variantiVAR_059778220A → V.Corresponds to variant rs1889565dbSNPEnsembl.1
Natural variantiVAR_047368322P → L.Corresponds to variant rs35101549dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15932 mRNA. Translation: AAA64693.2.
U16996 mRNA. Translation: AAB06261.1.
AL355512 Genomic DNA. Translation: CAI15120.1.
BC062545 mRNA. Translation: AAH62545.1.
CCDSiCCDS7566.1.
PIRiI38890.
RefSeqiNP_004410.3. NM_004419.3.
UniGeneiHs.2128.

Genome annotation databases

EnsembliENST00000369583; ENSP00000358596; ENSG00000138166.
GeneIDi1847.
KEGGihsa:1847.
UCSCiuc001kzd.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15932 mRNA. Translation: AAA64693.2.
U16996 mRNA. Translation: AAB06261.1.
AL355512 Genomic DNA. Translation: CAI15120.1.
BC062545 mRNA. Translation: AAH62545.1.
CCDSiCCDS7566.1.
PIRiI38890.
RefSeqiNP_004410.3. NM_004419.3.
UniGeneiHs.2128.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G6ZX-ray2.70A/B/C178-384[»]
ProteinModelPortaliQ16690.
SMRiQ16690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108180. 2 interactors.
IntActiQ16690. 1 interactor.
MINTiMINT-8277166.
STRINGi9606.ENSP00000358596.

Chemistry databases

ChEMBLiCHEMBL1250380.

PTM databases

DEPODiQ16690.
iPTMnetiQ16690.
PhosphoSitePlusiQ16690.

Polymorphism and mutation databases

BioMutaiDUSP5.
DMDMi215273975.

Proteomic databases

MaxQBiQ16690.
PaxDbiQ16690.
PeptideAtlasiQ16690.
PRIDEiQ16690.

Protocols and materials databases

DNASUi1847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369583; ENSP00000358596; ENSG00000138166.
GeneIDi1847.
KEGGihsa:1847.
UCSCiuc001kzd.4. human.

Organism-specific databases

CTDi1847.
DisGeNETi1847.
GeneCardsiDUSP5.
H-InvDBHIX0001673.
HGNCiHGNC:3071. DUSP5.
HPAiHPA055143.
MIMi603069. gene.
neXtProtiNX_Q16690.
OpenTargetsiENSG00000138166.
PharmGKBiPA27528.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ16690.
KOiK04459.
OMAiTICMAYI.
OrthoDBiEOG091G0249.
PhylomeDBiQ16690.
TreeFamiTF105122.

Enzyme and pathway databases

BioCyciZFISH:HS06468-MONOMER.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ16690.
SIGNORiQ16690.

Miscellaneous databases

ChiTaRSiDUSP5. human.
EvolutionaryTraceiQ16690.
GeneWikiiDUSP5.
GenomeRNAii1847.
PROiQ16690.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138166.
CleanExiHS_DUSP5.
GenevisibleiQ16690. HS.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. 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 nameiDUS5_HUMAN
AccessioniPrimary (citable) accession number: Q16690
Secondary accession number(s): Q12997, Q5T603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 156 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.