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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

Displays phosphatase activity toward several substrates. The highest relative activity is toward ERK1.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei263 – 2631Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  3. protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. endoderm formation Source: GO_Central
  2. peptidyl-tyrosine dephosphorylation Source: GOC
  3. protein dephosphorylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ16690.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 5 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity protein phosphatase hVH3
Gene namesi
Name:DUSP5
Synonyms:VH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:3071. DUSP5.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27528.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Dual specificity protein phosphatase 5PRO_0000094802Add
BLAST

Proteomic databases

MaxQBiQ16690.
PaxDbiQ16690.
PRIDEiQ16690.

PTM databases

DEPODiQ16690.
PhosphoSiteiQ16690.

Expressioni

Gene expression databases

BgeeiQ16690.
CleanExiHS_DUSP5.
GenevestigatoriQ16690.

Organism-specific databases

HPAiHPA055143.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108180. 3 interactions.
IntActiQ16690. 1 interaction.
MINTiMINT-8277166.
STRINGi9606.ENSP00000358596.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi180 – 1834Combined sources
Beta strandi186 – 1905Combined sources
Helixi191 – 1944Combined sources
Helixi197 – 2037Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi223 – 2275Combined sources
Helixi239 – 2413Combined sources
Helixi242 – 25413Combined sources
Beta strandi259 – 26810Combined sources
Helixi269 – 28214Combined sources
Helixi286 – 29611Combined sources
Helixi304 – 31714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G6ZX-ray2.70A/B/C178-384[»]
ProteinModelPortaliQ16690.
SMRiQ16690. Positions 22-140, 178-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16690.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 141123RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini180 – 384205Tyrosine-protein phosphataseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi53 – 7422Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi79 – 824Poly-Gly

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ16690.
KOiK04459.
OMAiTICMAYI.
OrthoDBiEOG75MVWD.
PhylomeDBiQ16690.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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.
PRINTSiPR01764. 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 113RQL → GHV in AAA64693 (PubMed:7961985).Curated
Sequence conflicti71 – 711A → R in AAA64693 (PubMed:7961985).Curated
Sequence conflicti105 – 1062AR → F in AAA64693 (PubMed:7961985).Curated
Sequence conflicti220 – 2201A → M in AAA64693 (PubMed:7961985).Curated
Sequence conflicti220 – 2201A → M in AAB06261 (PubMed:7836374).Curated
Sequence conflicti220 – 2201A → M in AAH62545 (PubMed:15489334).Curated
Sequence conflicti382 – 3821T → Q in AAA64693 (PubMed:7961985).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541E → D.
Corresponds to variant rs2282238 [ dbSNP | Ensembl ].
VAR_020298
Natural varianti220 – 2201A → T.
Corresponds to variant rs1889566 [ dbSNP | Ensembl ].
VAR_059777
Natural varianti220 – 2201A → V.
Corresponds to variant rs1889565 [ dbSNP | Ensembl ].
VAR_059778
Natural varianti322 – 3221P → L.
Corresponds to variant rs35101549 [ dbSNP | Ensembl ].
VAR_047368

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.3. human.

Polymorphism databases

DMDMi215273975.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2G6ZX-ray2.70A/B/C178-384[»]
ProteinModelPortaliQ16690.
SMRiQ16690. Positions 22-140, 178-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108180. 3 interactions.
IntActiQ16690. 1 interaction.
MINTiMINT-8277166.
STRINGi9606.ENSP00000358596.

Chemistry

ChEMBLiCHEMBL1250380.

PTM databases

DEPODiQ16690.
PhosphoSiteiQ16690.

Polymorphism databases

DMDMi215273975.

Proteomic databases

MaxQBiQ16690.
PaxDbiQ16690.
PRIDEiQ16690.

Protocols and materials databases

DNASUi1847.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369583; ENSP00000358596; ENSG00000138166.
GeneIDi1847.
KEGGihsa:1847.
UCSCiuc001kzd.3. human.

Organism-specific databases

CTDi1847.
GeneCardsiGC10P112247.
H-InvDBHIX0001673.
HGNCiHGNC:3071. DUSP5.
HPAiHPA055143.
MIMi603069. gene.
neXtProtiNX_Q16690.
PharmGKBiPA27528.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ16690.
KOiK04459.
OMAiTICMAYI.
OrthoDBiEOG75MVWD.
PhylomeDBiQ16690.
TreeFamiTF105122.

Enzyme and pathway databases

SignaLinkiQ16690.

Miscellaneous databases

ChiTaRSiDUSP5. human.
EvolutionaryTraceiQ16690.
GeneWikiiDUSP5.
GenomeRNAii1847.
NextBioi7565.
PROiQ16690.
SOURCEiSearch...

Gene expression databases

BgeeiQ16690.
CleanExiHS_DUSP5.
GenevestigatoriQ16690.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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.
PRINTSiPR01764. 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

« Hide 'large scale' publications
  1. "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
    Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
    J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  2. Bottaro D.P.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines."
    Kwak S.P., Dixon J.E.
    J. Biol. Chem. 270:1156-1160(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph.
  6. "Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase."
    Jeong D.G., Cho Y.H., Yoon T.S., Kim J.H., Ryu S.E., Kim S.J.
    Proteins 66:253-258(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 178-384, ACTIVE SITE.

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: February 4, 2015
This is version 140 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

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.