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Protein

Dual specificity protein phosphatase 9

Gene

DUSP9

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

Functioni

Inactivates MAP kinases. Has a specificity for the ERK family.

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 sitei290 – 2901Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: Ensembl
  2. phosphoprotein phosphatase activity Source: ProtInc
  3. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. inactivation of MAPK activity Source: ProtInc
  2. JNK cascade Source: ProtInc
  3. protein dephosphorylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
SignaLinkiQ99956.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 9 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 4
Short name:
MAP kinase phosphatase 4
Short name:
MKP-4
Gene namesi
Name:DUSP9
Synonyms:MKP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3076. DUSP9.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Dual specificity protein phosphatase 9PRO_0000094812Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei351 – 3511Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99956.
PaxDbiQ99956.
PRIDEiQ99956.

PTM databases

DEPODiQ99956.
PhosphoSiteiQ99956.

Expressioni

Gene expression databases

BgeeiQ99956.
CleanExiHS_DUSP9.
ExpressionAtlasiQ99956. baseline and differential.
GenevestigatoriQ99956.

Organism-specific databases

HPAiHPA003336.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK14Q165393EBI-3906678,EBI-73946
Mapk14P478112EBI-3906678,EBI-298727From a different organism.

Protein-protein interaction databases

BioGridi108185. 9 interactions.
IntActiQ99956. 9 interactions.
STRINGi9606.ENSP00000345853.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi205 – 2084Combined sources
Beta strandi211 – 2144Combined sources
Helixi218 – 2203Combined sources
Helixi222 – 2276Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi237 – 2393Combined sources
Turni243 – 2464Combined sources
Beta strandi251 – 2544Combined sources
Helixi259 – 2646Combined sources
Helixi265 – 28117Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi291 – 2955Combined sources
Helixi296 – 30914Combined sources
Helixi313 – 32311Combined sources
Helixi331 – 34414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HXPX-ray1.83A201-345[»]
3LJ8X-ray2.70A202-347[»]
ProteinModelPortaliQ99956.
SMRiQ99956. Positions 3-144, 202-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 139122RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini203 – 384182Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294079.
HOVERGENiHBG007347.
InParanoidiQ99956.
KOiK18498.
OMAiEPDRDSM.
PhylomeDBiQ99956.
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.
[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.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGLGRSCLW LRRELSPPRP RLLLLDCRSR ELYESARIGG ALSVALPALL
60 70 80 90 100
LRRLRRGSLS VRALLPGPPL QPPPPAPVLL YDQGGGRRRR GEAEAEAEEW
110 120 130 140 150
EAESVLGTLL QKLREEGYLA YYLQGGFSRF QAECPHLCET SLAGRAGSSM
160 170 180 190 200
APVPGPVPVV GLGSLCLGSD CSDAESEADR DSMSCGLDSE GATPPPVGLR
210 220 230 240 250
ASFPVQILPN LYLGSARDSA NLESLAKLGI RYILNVTPNL PNFFEKNGDF
260 270 280 290 300
HYKQIPISDH WSQNLSRFFP EAIEFIDEAL SQNCGVLVHC LAGVSRSVTV
310 320 330 340 350
TVAYLMQKLH LSLNDAYDLV KRKKSNISPN FNFMGQLLDF ERSLRLEERH
360 370 380
SQEQGSGGQA SAASNPPSFF TTPTSDGAFE LAPT
Length:384
Mass (Da):41,868
Last modified:April 30, 1997 - v1
Checksum:iF8598CA95AB379B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08302 mRNA. Translation: CAA69610.1.
U52111 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72847.1.
CH471172 Genomic DNA. Translation: EAW72848.1.
CH471172 Genomic DNA. Translation: EAW72849.1.
CCDSiCCDS14724.1.
RefSeqiNP_001386.1. NM_001395.3.
XP_005274712.1. XM_005274655.2.
UniGeneiHs.144879.
Hs.744909.

Genome annotation databases

EnsembliENST00000342782; ENSP00000345853; ENSG00000130829.
ENST00000370167; ENSP00000359186; ENSG00000130829.
GeneIDi1852.
KEGGihsa:1852.
UCSCiuc004fhx.4. human.

Polymorphism databases

DMDMi3913541.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08302 mRNA. Translation: CAA69610.1.
U52111 Genomic DNA. No translation available.
CH471172 Genomic DNA. Translation: EAW72847.1.
CH471172 Genomic DNA. Translation: EAW72848.1.
CH471172 Genomic DNA. Translation: EAW72849.1.
CCDSiCCDS14724.1.
RefSeqiNP_001386.1. NM_001395.3.
XP_005274712.1. XM_005274655.2.
UniGeneiHs.144879.
Hs.744909.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HXPX-ray1.83A201-345[»]
3LJ8X-ray2.70A202-347[»]
ProteinModelPortaliQ99956.
SMRiQ99956. Positions 3-144, 202-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108185. 9 interactions.
IntActiQ99956. 9 interactions.
STRINGi9606.ENSP00000345853.

PTM databases

DEPODiQ99956.
PhosphoSiteiQ99956.

Polymorphism databases

DMDMi3913541.

Proteomic databases

MaxQBiQ99956.
PaxDbiQ99956.
PRIDEiQ99956.

Protocols and materials databases

DNASUi1852.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342782; ENSP00000345853; ENSG00000130829.
ENST00000370167; ENSP00000359186; ENSG00000130829.
GeneIDi1852.
KEGGihsa:1852.
UCSCiuc004fhx.4. human.

Organism-specific databases

CTDi1852.
GeneCardsiGC0XP152907.
HGNCiHGNC:3076. DUSP9.
HPAiHPA003336.
MIMi300134. gene.
neXtProtiNX_Q99956.
PharmGKBiPA27533.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294079.
HOVERGENiHBG007347.
InParanoidiQ99956.
KOiK18498.
OMAiEPDRDSM.
PhylomeDBiQ99956.
TreeFamiTF105122.

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
SignaLinkiQ99956.

Miscellaneous databases

ChiTaRSiDUSP9. human.
EvolutionaryTraceiQ99956.
GenomeRNAii1852.
NextBioi7585.
PROiQ99956.
SOURCEiSearch...

Gene expression databases

BgeeiQ99956.
CleanExiHS_DUSP9.
ExpressionAtlasiQ99956. baseline and differential.
GenevestigatoriQ99956.

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.
[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.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4."
    Muda M., Boschert U., Smith A., Antonsonn B., Gillieron C., Chabert C., Camps M., Martinou I., Ashworth A., Arkinstall S.
    J. Biol. Chem. 272:5141-5151(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 201-345.

Entry informationi

Entry nameiDUS9_HUMAN
AccessioniPrimary (citable) accession number: Q99956
Secondary accession number(s): D3DWU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 1998
Last sequence update: April 30, 1997
Last modified: February 3, 2015
This is version 133 of the entry and version 1 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.