Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99956

- DUS9_HUMAN

UniProt

Q99956 - DUS9_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual specificity protein phosphatase 9

Gene

DUSP9

Organism
Homo sapiens (Human)
Status
Reviewed - 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: RefGenome
  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: RefGenome
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: 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

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 – 2084
Beta strandi211 – 2144
Helixi218 – 2203
Helixi222 – 2276
Beta strandi230 – 2356
Beta strandi237 – 2393
Turni243 – 2464
Beta strandi251 – 2544
Helixi259 – 2646
Helixi265 – 28117
Beta strandi285 – 2895
Beta strandi291 – 2955
Helixi296 – 30914
Helixi313 – 32311
Helixi331 – 34414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:May 1, 1997 - v1
Checksum:iF8598CA95AB379B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14724.1.
RefSeqi NP_001386.1. NM_001395.3.
XP_005274712.1. XM_005274655.2.
UniGenei Hs.144879.
Hs.744909.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HXP X-ray 1.83 A 201-345 [» ]
3LJ8 X-ray 2.70 A 202-347 [» ]
ProteinModelPortali Q99956.
SMRi Q99956. Positions 3-144, 202-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108185. 9 interactions.
IntActi Q99956. 9 interactions.
STRINGi 9606.ENSP00000345853.

PTM databases

PhosphoSitei Q99956.

Polymorphism databases

DMDMi 3913541.

Proteomic databases

MaxQBi Q99956.
PaxDbi Q99956.
PRIDEi Q99956.

Protocols and materials databases

DNASUi 1852.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342782 ; ENSP00000345853 ; ENSG00000130829 .
ENST00000370167 ; ENSP00000359186 ; ENSG00000130829 .
GeneIDi 1852.
KEGGi hsa:1852.
UCSCi uc004fhx.4. human.

Organism-specific databases

CTDi 1852.
GeneCardsi GC0XP152907.
HGNCi HGNC:3076. DUSP9.
HPAi HPA003336.
MIMi 300134. gene.
neXtProti NX_Q99956.
PharmGKBi PA27533.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOGENOMi HOG000294079.
HOVERGENi HBG007347.
InParanoidi Q99956.
KOi K18498.
OMAi EPDRDSM.
PhylomeDBi Q99956.
TreeFami TF105122.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
SignaLinki Q99956.

Miscellaneous databases

EvolutionaryTracei Q99956.
GenomeRNAii 1852.
NextBioi 7585.
PROi Q99956.
SOURCEi Search...

Gene expression databases

Bgeei Q99956.
CleanExi HS_DUSP9.
ExpressionAtlasi Q99956. baseline and differential.
Genevestigatori Q99956.

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.
[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.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1997) [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(2005) [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 15, 1998
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 130 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