Q99956 (DUS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DUSP9
Synonyms:	MKP4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inactivates MAP kinases. Has a specificity for the ERK family.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Cytoplasm.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Traceable author statement Ref.1. Source: ProtInc peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome endoplasmic reticulum Inferred from direct assay. Source: HPA nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 384

384

Dual specificity protein phosphatase 9

PRO_0000094812

Regions

Domain

18 – 139

122

Rhodanese

Domain

203 – 384

182

Tyrosine-protein phosphatase

Sites

Active site

290

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

351

1

Phosphoserine Ref.4

Secondary structure

1

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384

Helix Strand Turn

Details...

Beta strand

205 – 208

4

Beta strand

211 – 214

4

Helix

218 – 220

3

Helix

222 – 227

6

Beta strand

230 – 235

6

Beta strand

237 – 239

3

Turn

243 – 246

4

Beta strand

251 – 254

4

Helix

259 – 264

6

Helix

265 – 281

17

Beta strand

285 – 289

5

Beta strand

291 – 295

5

Helix

296 – 309

14

Helix

313 – 323

11

Helix

331 – 344

14

Sequences

	Sequence		Length	Mass (Da)
	Q99956 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: F8598CA95AB379B7	FASTA	384	41,868
	10 20 30 40 50 60 MEGLGRSCLW LRRELSPPRP RLLLLDCRSR ELYESARIGG ALSVALPALL LRRLRRGSLS 70 80 90 100 110 120 VRALLPGPPL QPPPPAPVLL YDQGGGRRRR GEAEAEAEEW EAESVLGTLL QKLREEGYLA 130 140 150 160 170 180 YYLQGGFSRF QAECPHLCET SLAGRAGSSM APVPGPVPVV GLGSLCLGSD CSDAESEADR 190 200 210 220 230 240 DSMSCGLDSE GATPPPVGLR ASFPVQILPN LYLGSARDSA NLESLAKLGI RYILNVTPNL 250 260 270 280 290 300 PNFFEKNGDF HYKQIPISDH WSQNLSRFFP EAIEFIDEAL SQNCGVLVHC LAGVSRSVTV 310 320 330 340 350 360 TVAYLMQKLH LSLNDAYDLV KRKKSNISPN FNFMGQLLDF ERSLRLEERH SQEQGSGGQA 370 380 SAASNPPSFF TTPTSDGAFE LAPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"Structural genomics of protein phosphatases." Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K. J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 201-345.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00294486.

RefSeq

NP_001386.1. NM_001395.2.

UniGene

Hs.144879.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HXP	X-ray	1.83	A	201-345	[»]
3LJ8	X-ray	2.70	A	202-347	[»]

ProteinModelPortal

Q99956.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q99956. 2 interactions.

STRING

9606.ENSP00000345853.

PTM databases

PhosphoSite

Q99956.

Polymorphism databases

DMDM

3913541.

Proteomic databases

PaxDb

Q99956.

PRIDE

Q99956.

Protocols and materials databases

DNASU

1852.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342782; ENSP00000345853; ENSG00000130829.
ENST00000370167; ENSP00000359186; ENSG00000130829.
ENST00000595095; ENSP00000472478; ENSG00000269798.
ENST00000599661; ENSP00000473122; ENSG00000269798.

GeneID

1852.

KEGG

hsa:1852.

UCSC

uc004fhx.4. human.

Organism-specific databases

CTD

1852.

GeneCards

GC0XP152907.

HGNC

HGNC:3076. DUSP9.

HPA

HPA003336.

MIM

300134. gene.

neXtProt

NX_Q99956.

PharmGKB

PA27533.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000294079.

HOVERGEN

HBG007347.

InParanoid

Q99956.

KO

K04459.

OMA

SGGQESA.

OrthoDB

EOG4X0MT0.

PhylomeDB

Q99956.

Enzyme and pathway databases

BRENDA

3.1.3.48. 2681.

Gene expression databases

ArrayExpress

Q99956.

Bgee

Q99956.

CleanEx

HS_DUSP9.

Genevestigator

Q99956.

GermOnline

ENSG00000130829. Homo sapiens.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PIRSF

PIRSF000939. MAPK_Ptase. 1 hit.

PRINTS

PR01764. MAPKPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q99956.

GenomeRNAi

1852.

NextBio

7585.

SOURCE

Search...

Entry information

Entry name

DUS9_HUMAN

Accession

Primary (citable) accession number: Q99956
Secondary accession number(s): D3DWU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.