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Q16690

- DUS5_HUMAN

UniProt

Q16690 - DUS5_HUMAN

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Protein

Dual specificity protein phosphatase 5

Gene

DUSP5

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei263 – 2631Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
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 – 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.
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

        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 .
CCDSi CCDS7566.1.
PIRi I38890.
RefSeqi NP_004410.3. NM_004419.3.
UniGenei Hs.2128.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000118902.
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: November 26, 2014
This is version 138 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