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Q16690

- DUS5_HUMAN

UniProt

Q16690 - DUS5_HUMAN

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Protein

Dual specificity protein phosphatase 5

Gene
DUSP5, VH3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei263 – 2631Phosphocysteine intermediate1 Publication

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein binding Source: IntAct
  3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  4. protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. endoderm formation Source: RefGenome
  2. peptidyl-tyrosine dephosphorylation Source: GOC
  3. protein dephosphorylation Source: RefGenome
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 Reviewed prediction

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

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 – 1834
Beta strandi186 – 1905
Helixi191 – 1944
Helixi197 – 2037
Beta strandi207 – 2104
Beta strandi223 – 2275
Helixi239 – 2413
Helixi242 – 25413
Beta strandi259 – 26810
Helixi269 – 28214
Helixi286 – 29611
Helixi304 – 31714

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ16690.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi53 – 7422Nuclear localization signal Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
HOVERGENiHBG007347.
InParanoidiQ16690.
KOiK04459.
OMAiSPVHQLK.
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

MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV    50
VLRRARGGAV SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR 100
EESAARVVLT SLLACLPAGP RVYFLKGGYE TFYSEYPECC VDVKPISQEK 150
IESERALISQ CGKPVVNVSY RPAYDQGGPV EILPFLYLGS AYHASKCEFL 200
ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS HFQEAIDFID 250
CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV 300
SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ 350
GAYCTFPASV LAPVPTHSTV SELSRSPVAT ATSC 384
Length:384
Mass (Da):42,047
Last modified:November 25, 2008 - v2
Checksum:i2E4B2938F886CB4E
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 113RQL → GHV in AAA64693. 1 Publication
Sequence conflicti71 – 711A → R in AAA64693. 1 Publication
Sequence conflicti105 – 1062AR → F in AAA64693. 1 Publication
Sequence conflicti220 – 2201A → M in AAA64693. 1 Publication
Sequence conflicti220 – 2201A → M in AAB06261. 1 Publication
Sequence conflicti220 – 2201A → M in AAH62545. 1 Publication
Sequence conflicti382 – 3821T → Q in AAA64693. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U15932 mRNA. Translation: AAA64693.2 .
U16996 mRNA. Translation: AAB06261.1 .
AL355512 Genomic DNA. Translation: CAI15120.1 .
BC062545 mRNA. Translation: AAH62545.1 .
CCDSi CCDS7566.1.
PIRi I38890.
RefSeqi NP_004410.3. NM_004419.3.
UniGenei Hs.2128.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G6Z X-ray 2.70 A/B/C 178-384 [» ]
ProteinModelPortali Q16690.
SMRi Q16690. Positions 22-140, 178-320.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108180. 3 interactions.
IntActi Q16690. 1 interaction.
MINTi MINT-8277166.
STRINGi 9606.ENSP00000358596.

Chemistry

ChEMBLi CHEMBL1250380.

PTM databases

PhosphoSitei Q16690.

Polymorphism databases

DMDMi 215273975.

Proteomic databases

MaxQBi Q16690.
PaxDbi Q16690.
PRIDEi Q16690.

Protocols and materials databases

DNASUi 1847.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369583 ; ENSP00000358596 ; ENSG00000138166 .
GeneIDi 1847.
KEGGi hsa:1847.
UCSCi uc001kzd.3. human.

Organism-specific databases

CTDi 1847.
GeneCardsi GC10P112247.
H-InvDB HIX0001673.
HGNCi HGNC:3071. DUSP5.
HPAi HPA055143.
MIMi 603069. gene.
neXtProti NX_Q16690.
PharmGKBi PA27528.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOVERGENi HBG007347.
InParanoidi Q16690.
KOi K04459.
OMAi SPVHQLK.
OrthoDBi EOG75MVWD.
PhylomeDBi Q16690.
TreeFami TF105122.

Enzyme and pathway databases

SignaLinki Q16690.

Miscellaneous databases

ChiTaRSi DUSP5. human.
EvolutionaryTracei Q16690.
GeneWikii DUSP5.
GenomeRNAii 1847.
NextBioi 7565.
PROi Q16690.
SOURCEi Search...

Gene expression databases

Bgeei Q16690.
CleanExi HS_DUSP5.
Genevestigatori Q16690.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000340. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
PRINTSi PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 135 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

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