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Q9Y6W6 (DUS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 10

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Mitogen-activated protein kinase phosphatase 5
Short name=MAP kinase phosphatase 5
Short name=MKP-5
Gene names
Name:DUSP10
Synonyms:MKP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. Ref.9

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.7 Ref.9

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.7 Ref.9

Subunit structure

Monomer. Interacts with MAPK14. Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Detected in brain. Ref.7

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 componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Traceable author statement Ref.1. Source: ProtInc

inactivation of MAPK activity

Inferred from direct assay Ref.9. Source: UniProtKB

negative regulation of JNK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of JUN kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of respiratory burst involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of stress-activated MAPK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein dephosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of adaptive immune response

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to stress

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionMAP kinase phosphatase activity

Inferred from direct assay Ref.9. Source: UniProtKB

MAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphatase activity

Inferred from direct assay Ref.7. Source: UniProtKB

phosphoprotein phosphatase activity

Traceable author statement Ref.1. Source: ProtInc

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6W6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y6W6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-342: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Dual specificity protein phosphatase 10
PRO_0000094813

Regions

Domain168 – 285118Rhodanese
Domain384 – 45370Tyrosine-protein phosphatase
Region199 – 21517Interaction with MAP kinases

Sites

Active site4081Phosphocysteine intermediate Probable

Natural variations

Alternative sequence1 – 342342Missing in isoform 2.
VSP_036549

Experimental info

Mutagenesis180 – 1812FM → DD: Reduced enzyme activity with MAPK14. Ref.9
Mutagenesis203 – 2042RR → AA: Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14. Ref.9

Secondary structure

............................................................ 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A8CB74ABF9498CD4

FASTA48252,642
        10         20         30         40         50         60 
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV VSLKAANLTY 

        70         80         90        100        110        120 
MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG TTTTAIGTST TCPANQMVNN 

       130        140        150        160        170        180 
NENTGSLSPS SGVGSPVSGT PKQLASIKII YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF 

       190        200        210        220        230        240 
MEYNKSHIQG AVHINCADKI SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT 

       250        260        270        280        290        300 
NEPSRVMPSQ PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA 

       310        320        330        340        350        360 
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY VINVTTHLPL 

       370        380        390        400        410        420 
YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI 

       430        440        450        460        470        480 
AYLMKHTRMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET 


VV 

« Hide

Isoform 2 [UniParc].

Checksum: CE151F365D042516
Show »

FASTA14016,110

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5."
Tanoue T., Moriguchi T., Nishida E.
J. Biol. Chem. 274:19949-19956(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases."
Theodosiou A., Smith A., Gillieron C., Arkinstall S., Ashworth A.
Oncogene 18:6981-6988(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Brain, Lung, PNS and Testis.
[7]"Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase."
Jeong D.G., Yoon T.S., Kim J.H., Shim M.Y., Jung S.K., Son J.H., Ryu S.E., Kim S.J.
J. Mol. Biol. 360:946-955(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 320-467, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, ACTIVE SITE.
[8]"Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5."
Tao X., Tong L.
Protein Sci. 16:880-886(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 148-287, SUBUNIT, ACTIVE SITE.
[9]"A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5."
Zhang Y.Y., Wu J.W., Wang Z.X.
Sci. Signal. 4:RA88-RA88(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 139-288 IN COMPLEX WITH MAPK14, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAPK14, MUTAGENESIS OF 180-PHE-MET-181 AND 203-ARG-ARG-204.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026436 mRNA. Translation: BAA81668.1.
AF179212 mRNA. Translation: AAD51857.1.
AK022513 mRNA. Translation: BAB14070.1.
AL590966 Genomic DNA. Translation: CAH71120.1.
CH471100 Genomic DNA. Translation: EAW93283.1.
CH471100 Genomic DNA. Translation: EAW93285.1.
CH471100 Genomic DNA. Translation: EAW93286.1.
CH471100 Genomic DNA. Translation: EAW93287.1.
BC020608 mRNA. Translation: AAH20608.1.
BC031405 mRNA. Translation: AAH31405.1.
BC063826 mRNA. Translation: AAH63826.1.
RefSeqNP_009138.1. NM_007207.4.
NP_653329.1. NM_144728.2.
NP_653330.1. NM_144729.2.
UniGeneHs.497822.
Hs.732301.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZZWX-ray1.60A/B320-467[»]
2OUCX-ray2.20A/B148-287[»]
2OUDX-ray2.80A315-482[»]
3TG1X-ray2.71B139-288[»]
ProteinModelPortalQ9Y6W6.
SMRQ9Y6W6. Positions 148-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116389. 11 interactions.
IntActQ9Y6W6. 10 interactions.
MINTMINT-8208613.
STRING9606.ENSP00000355866.

PTM databases

PhosphoSiteQ9Y6W6.

Polymorphism databases

DMDM20138090.

Proteomic databases

PaxDbQ9Y6W6.
PRIDEQ9Y6W6.

Protocols and materials databases

DNASU11221.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323825; ENSP00000322015; ENSG00000143507. [Q9Y6W6-2]
ENST00000366899; ENSP00000355866; ENSG00000143507. [Q9Y6W6-1]
ENST00000544095; ENSP00000441302; ENSG00000143507. [Q9Y6W6-2]
GeneID11221.
KEGGhsa:11221.
UCSCuc001hmx.2. human. [Q9Y6W6-2]
uc001hmy.2. human. [Q9Y6W6-1]

Organism-specific databases

CTD11221.
GeneCardsGC01M221874.
HGNCHGNC:3065. DUSP10.
HPAHPA016758.
MIM608867. gene.
neXtProtNX_Q9Y6W6.
PharmGKBPA27520.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000069871.
HOVERGENHBG102158.
InParanoidQ9Y6W6.
KOK04459.
OMATCPANQM.
OrthoDBEOG75QR5B.
PhylomeDBQ9Y6W6.
TreeFamTF105122.

Enzyme and pathway databases

BRENDA3.1.3.48. 2681.
SignaLinkQ9Y6W6.

Gene expression databases

BgeeQ9Y6W6.
CleanExHS_DUSP10.
GenevestigatorQ9Y6W6.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
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.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6W6.
GeneWikiDUSP10.
GenomeRNAi11221.
NextBio42707.
PROQ9Y6W6.
SOURCESearch...

Entry information

Entry nameDUS10_HUMAN
AccessionPrimary (citable) accession number: Q9Y6W6
Secondary accession number(s): D3DTB4, Q6GSI4, Q9H9Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM