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Q16690 (DUS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DUSP5
Synonyms:VH3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subcellular location

Nucleus Potential.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 rhodanese domain.

Contains 1 tyrosine-protein phosphatase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAPK1P284824EBI-7487376,EBI-959949

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Dual specificity protein phosphatase 5
PRO_0000094802

Regions

Domain19 – 141123Rhodanese
Domain180 – 384205Tyrosine-protein phosphatase
Motif53 – 7422Nuclear localization signal Potential
Compositional bias79 – 824Poly-Gly

Sites

Active site2631Phosphocysteine intermediate Ref.6

Natural variations

Natural variant1541E → D.
Corresponds to variant rs2282238 [ dbSNP | Ensembl ].
VAR_020298
Natural variant2201A → T.
Corresponds to variant rs1889566 [ dbSNP | Ensembl ].
VAR_059777
Natural variant2201A → V.
Corresponds to variant rs1889565 [ dbSNP | Ensembl ].
VAR_059778
Natural variant3221P → L.
Corresponds to variant rs35101549 [ dbSNP | Ensembl ].
VAR_047368

Experimental info

Sequence conflict9 – 113RQL → GHV in AAA64693. Ref.1
Sequence conflict711A → R in AAA64693. Ref.1
Sequence conflict105 – 1062AR → F in AAA64693. Ref.1
Sequence conflict2201A → M in AAA64693. Ref.1
Sequence conflict2201A → M in AAB06261. Ref.3
Sequence conflict2201A → M in AAH62545. Ref.5
Sequence conflict3821T → Q in AAA64693. Ref.1

Secondary structure

...................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q16690 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 2E4B2938F886CB4E

FASTA38442,047
        10         20         30         40         50         60 
MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV VLRRARGGAV 

        70         80         90        100        110        120 
SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR EESAARVVLT SLLACLPAGP 

       130        140        150        160        170        180 
RVYFLKGGYE TFYSEYPECC VDVKPISQEK IESERALISQ CGKPVVNVSY RPAYDQGGPV 

       190        200        210        220        230        240 
EILPFLYLGS AYHASKCEFL ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS 

       250        260        270        280        290        300 
HFQEAIDFID CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV 

       310        320        330        340        350        360 
SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ GAYCTFPASV 

       370        380 
LAPVPTHSTV SELSRSPVAT ATSC 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15932 mRNA. Translation: AAA64693.2.
U16996 mRNA. Translation: AAB06261.1.
AL355512 Genomic DNA. Translation: CAI15120.1.
BC062545 mRNA. Translation: AAH62545.1.
PIRI38890.
RefSeqNP_004410.3. NM_004419.3.
UniGeneHs.2128.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G6ZX-ray2.70A/B/C178-384[»]
ProteinModelPortalQ16690.
SMRQ16690. Positions 4-143, 178-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108180. 3 interactions.
IntActQ16690. 1 interaction.
MINTMINT-8277166.
STRING9606.ENSP00000358596.

Chemistry

ChEMBLCHEMBL1250380.

PTM databases

PhosphoSiteQ16690.

Polymorphism databases

DMDM215273975.

Proteomic databases

PaxDbQ16690.
PRIDEQ16690.

Protocols and materials databases

DNASU1847.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369583; ENSP00000358596; ENSG00000138166.
GeneID1847.
KEGGhsa:1847.
UCSCuc001kzd.3. human.

Organism-specific databases

CTD1847.
GeneCardsGC10P112247.
H-InvDBHIX0001673.
HGNCHGNC:3071. DUSP5.
HPAHPA055143.
MIM603069. gene.
neXtProtNX_Q16690.
PharmGKBPA27528.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOVERGENHBG007347.
InParanoidQ16690.
KOK04459.
OMAWQKLKKD.
OrthoDBEOG75MVWD.
PhylomeDBQ16690.
TreeFamTF105122.

Enzyme and pathway databases

SignaLinkQ16690.

Gene expression databases

BgeeQ16690.
CleanExHS_DUSP5.
GenevestigatorQ16690.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSPR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP5. human.
EvolutionaryTraceQ16690.
GeneWikiDUSP5.
GenomeRNAi1847.
NextBio7565.
PROQ16690.
SOURCESearch...

Entry information

Entry nameDUS5_HUMAN
AccessionPrimary (citable) accession number: Q16690
Secondary accession number(s): Q12997, Q5T603
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM