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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)DescriptionActionsGraphical viewLength
Active sitei290Phosphocysteine intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • activation of MAPK activity Source: Reactome
  • inactivation of MAPK activity Source: ProtInc
  • JNK cascade Source: ProtInc
  • MAPK cascade Source: Reactome
  • protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS05453-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ99956.
SIGNORiQ99956.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3076. DUSP9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi1852.
OpenTargetsiENSG00000130829.
PharmGKBiPA27533.

Polymorphism and mutation databases

BioMutaiDUSP9.
DMDMi3913541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000948121 – 384Dual specificity protein phosphatase 9Add BLAST384

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineCombined sources1
Modified residuei262PhosphoserineCombined sources1
Modified residuei351PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99956.
MaxQBiQ99956.
PaxDbiQ99956.
PeptideAtlasiQ99956.
PRIDEiQ99956.

PTM databases

DEPODiQ99956.
iPTMnetiQ99956.
PhosphoSitePlusiQ99956.

Expressioni

Gene expression databases

BgeeiENSG00000130829.
CleanExiHS_DUSP9.
GenevisibleiQ99956. HS.

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. 11 interactors.
IntActiQ99956. 11 interactors.
STRINGi9606.ENSP00000345853.

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi205 – 208Combined sources4
Beta strandi211 – 214Combined sources4
Helixi218 – 220Combined sources3
Helixi222 – 227Combined sources6
Beta strandi230 – 235Combined sources6
Beta strandi237 – 239Combined sources3
Turni243 – 246Combined sources4
Beta strandi251 – 254Combined sources4
Helixi259 – 264Combined sources6
Helixi265 – 281Combined sources17
Beta strandi285 – 289Combined sources5
Beta strandi291 – 295Combined sources5
Helixi296 – 309Combined sources14
Helixi313 – 323Combined sources11
Helixi331 – 344Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ99956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 139RhodanesePROSITE-ProRule annotationAdd BLAST122
Domaini203 – 384Tyrosine-protein phosphataseAdd BLAST182

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1717. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294079.
HOVERGENiHBG007347.
InParanoidiQ99956.
KOiK18498.
OMAiYLMQKRH.
OrthoDBiEOG091G0249.
PhylomeDBiQ99956.
TreeFamiTF105122.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
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:May 1, 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_001305432.1. NM_001318503.1.
NP_001386.1. NM_001395.3.
XP_011529426.1. XM_011531124.1.
UniGeneiHs.144879.
Hs.744909.

Genome annotation databases

EnsembliENST00000342782; ENSP00000345853; ENSG00000130829.
ENST00000370167; ENSP00000359186; ENSG00000130829.
GeneIDi1852.
KEGGihsa:1852.
UCSCiuc004fhx.5. human.

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_001305432.1. NM_001318503.1.
NP_001386.1. NM_001395.3.
XP_011529426.1. XM_011531124.1.
UniGeneiHs.144879.
Hs.744909.

3D structure databases

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

Protein-protein interaction databases

BioGridi108185. 11 interactors.
IntActiQ99956. 11 interactors.
STRINGi9606.ENSP00000345853.

PTM databases

DEPODiQ99956.
iPTMnetiQ99956.
PhosphoSitePlusiQ99956.

Polymorphism and mutation databases

BioMutaiDUSP9.
DMDMi3913541.

Proteomic databases

EPDiQ99956.
MaxQBiQ99956.
PaxDbiQ99956.
PeptideAtlasiQ99956.
PRIDEiQ99956.

Protocols and materials databases

DNASUi1852.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342782; ENSP00000345853; ENSG00000130829.
ENST00000370167; ENSP00000359186; ENSG00000130829.
GeneIDi1852.
KEGGihsa:1852.
UCSCiuc004fhx.5. human.

Organism-specific databases

CTDi1852.
DisGeNETi1852.
GeneCardsiDUSP9.
HGNCiHGNC:3076. DUSP9.
HPAiHPA003336.
MIMi300134. gene.
neXtProtiNX_Q99956.
OpenTargetsiENSG00000130829.
PharmGKBiPA27533.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1717. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294079.
HOVERGENiHBG007347.
InParanoidiQ99956.
KOiK18498.
OMAiYLMQKRH.
OrthoDBiEOG091G0249.
PhylomeDBiQ99956.
TreeFamiTF105122.

Enzyme and pathway databases

BioCyciZFISH:HS05453-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ99956.
SIGNORiQ99956.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000130829.
CleanExiHS_DUSP9.
GenevisibleiQ99956. HS.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 2 hits.
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...

Entry informationi

Entry nameiDUS9_HUMAN
AccessioniPrimary (citable) accession number: Q99956
Secondary accession number(s): D3DWU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: November 30, 2016
This is version 150 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

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 one 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.