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Q9ESS0 (DUS10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Subunit structure

Monomer. Interacts with MAPK14 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Dual specificity protein phosphatase 10
PRO_0000094814

Regions

Domain169 – 286118Rhodanese
Domain386 – 45671Tyrosine-protein phosphatase
Region200 – 21617Interaction with MAP kinases By similarity

Sites

Active site4091Phosphocysteine intermediate By similarity

Experimental info

Sequence conflict481T → A in BAB17680. Ref.1
Sequence conflict1131P → S in BAB27966. Ref.2
Sequence conflict3861Q → R in BAB17680. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9ESS0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7797A1877D986AA8

FASTA48352,532
        10         20         30         40         50         60 
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSASPGSG SHAPVLATAV VTLKAANLTY 

        70         80         90        100        110        120 
MPSSSGSARS LNCGCSSTSC CTVATYDKDH QAQTQAIAAG TATTAIGTST TCPANQMVNN 

       130        140        150        160        170        180 
NENTGSVLSP SGGVGSPVSG TPKQLASIKI IYPNDLAKKM TKCSKSHLPS QGPVIIDCRP 

       190        200        210        220        230        240 
FMEYNKSHIQ GAVHINCADK ISRRRLQQGK ITVLDLISCR EGKDSFKRIF SKEIIVYDEN 

       250        260        270        280        290        300 
TNEPSRVTPS QPLHIVLESL KREGKEPLVL KGGLSSFKQN HGNLCDNSLQ LQECREVGGG 

       310        320        330        340        350        360 
ASAASSMLPQ SVPTTPDIEN AELTPILPFL FLGNEQDAQD LDTMQRLNIG YVINVTTHLP 

       370        380        390        400        410        420 
LYHYEKGLFN YKRLPATDSN KQNLRQYFEE AFEFIEEAHQ CGKGLLIHCQ AGVSRSATIV 

       430        440        450        460        470        480 
IAYLMKHTRM TMTDAYKFVK GKRPIISPNL NFMGQLLEFE EDLNNGVTPR ILTPKLMGME 


TVV

« Hide

References

« Hide 'large scale' references
[1]"Expression and comparative chromosomal mapping of MKP-5 genes DUSP10/Dusp10."
Masuda K., Shima H., Kikuchi K., Watanabe Y., Matsuda Y.
Cytogenet. Cell Genet. 90:71-74(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Embryo, Kidney, Pancreas, Thymus and Urinary bladder.
[3]"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].
Strain: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB037908 mRNA. Translation: BAB17680.1.
AK011995 mRNA. Translation: BAB27966.1.
AK035293 mRNA. Translation: BAC29019.1.
AK050528 mRNA. Translation: BAC34308.1.
AK088024 mRNA. Translation: BAC40102.1.
AK088186 mRNA. Translation: BAC40196.1.
AK088357 mRNA. Translation: BAC40300.1.
AK142568 mRNA. Translation: BAE25109.1.
BC025066 mRNA. Translation: AAH25066.1.
IPIIPI00113513.
RefSeqNP_071302.2. NM_022019.5.
UniGeneMm.404024.

3D structure databases

ProteinModelPortalQ9ESS0.
SMRQ9ESS0. Positions 149-288, 322-468.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9ESS0. 1 interaction.
STRING10090.ENSMUSP00000045838.

Proteomic databases

PaxDbQ9ESS0.
PRIDEQ9ESS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048655; ENSMUSP00000045838; ENSMUSG00000039384.
GeneID63953.
KEGGmmu:63953.

Organism-specific databases

CTD11221.
MGIMGI:1927070. Dusp10.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00700000104093.
HOGENOMHOG000069871.
HOVERGENHBG102158.
InParanoidQ8R3L3.
KOK04459.
OMANEHDAQD.
OrthoDBEOG4W0XD5.

Gene expression databases

ArrayExpressQ9ESS0.
BgeeQ9ESS0.
CleanExMM_DUSP10.
GenevestigatorQ9ESS0.
GermOnlineENSMUSG00000039384. Mus musculus.

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. Rhodanese-like. 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

NextBio319811.
SOURCESearch...

Entry information

Entry nameDUS10_MOUSE
AccessionPrimary (citable) accession number: Q9ESS0
Secondary accession number(s): Q8R3L3, Q9CZY9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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