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Protein

Dual specificity protein phosphatase 10

Gene

Dusp10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei409 – 4091Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase phosphatase activity Source: UniProtKB
  2. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  3. phosphatase activity Source: MGI
  4. protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  5. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. inactivation of MAPK activity Source: UniProtKB
  2. negative regulation of JNK cascade Source: MGI
  3. negative regulation of JUN kinase activity Source: MGI
  4. negative regulation of oligodendrocyte differentiation Source: Ensembl
  5. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: MGI
  6. negative regulation of respiratory burst involved in inflammatory response Source: MGI
  7. negative regulation of stress-activated MAPK cascade Source: MGI
  8. oligodendrocyte differentiation Source: MGI
  9. protein dephosphorylation Source: UniProtKB
  10. regulation of adaptive immune response Source: MGI
  11. regulation of brown fat cell differentiation Source: MGI
  12. regulation of innate immune response Source: MGI
  13. response to lipopolysaccharide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Dusp10
Synonyms:Mkp5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1927070. Dusp10.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: MGI
  2. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Dual specificity protein phosphatase 10PRO_0000094814Add
BLAST

Proteomic databases

MaxQBiQ9ESS0.
PaxDbiQ9ESS0.
PRIDEiQ9ESS0.

Expressioni

Gene expression databases

BgeeiQ9ESS0.
CleanExiMM_DUSP10.
ExpressionAtlasiQ9ESS0. baseline and differential.
GenevestigatoriQ9ESS0.

Interactioni

Subunit structurei

Monomer. Interacts with MAPK14 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211005. 1 interaction.
IntActiQ9ESS0. 1 interaction.
STRINGi10090.ENSMUSP00000045838.

Structurei

3D structure databases

ProteinModelPortaliQ9ESS0.
SMRiQ9ESS0. Positions 149-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini169 – 286118RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini386 – 45671Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 21617Interaction with MAP kinasesBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9ESS0.
KOiK04459.
OMAiTCPANQM.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
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.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ESS0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSASPGSG SHAPVLATAV
60 70 80 90 100
VTLKAANLTY MPSSSGSARS LNCGCSSTSC CTVATYDKDH QAQTQAIAAG
110 120 130 140 150
TATTAIGTST TCPANQMVNN NENTGSVLSP SGGVGSPVSG TPKQLASIKI
160 170 180 190 200
IYPNDLAKKM TKCSKSHLPS QGPVIIDCRP FMEYNKSHIQ GAVHINCADK
210 220 230 240 250
ISRRRLQQGK ITVLDLISCR EGKDSFKRIF SKEIIVYDEN TNEPSRVTPS
260 270 280 290 300
QPLHIVLESL KREGKEPLVL KGGLSSFKQN HGNLCDNSLQ LQECREVGGG
310 320 330 340 350
ASAASSMLPQ SVPTTPDIEN AELTPILPFL FLGNEQDAQD LDTMQRLNIG
360 370 380 390 400
YVINVTTHLP LYHYEKGLFN YKRLPATDSN KQNLRQYFEE AFEFIEEAHQ
410 420 430 440 450
CGKGLLIHCQ AGVSRSATIV IAYLMKHTRM TMTDAYKFVK GKRPIISPNL
460 470 480
NFMGQLLEFE EDLNNGVTPR ILTPKLMGME TVV
Length:483
Mass (Da):52,532
Last modified:July 27, 2011 - v2
Checksum:i7797A1877D986AA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481T → A in BAB17680 (PubMed:11060451).Curated
Sequence conflicti113 – 1131P → S in BAB27966 (PubMed:16141072).Curated
Sequence conflicti386 – 3861Q → R in BAB17680 (PubMed:11060451).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15591.1.
RefSeqiNP_071302.2. NM_022019.5.
XP_006497251.1. XM_006497188.1.
XP_006497252.1. XM_006497189.1.
UniGeneiMm.404024.

Genome annotation databases

EnsembliENSMUST00000048655; ENSMUSP00000045838; ENSMUSG00000039384.
GeneIDi63953.
KEGGimmu:63953.
UCSCiuc007dym.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15591.1.
RefSeqiNP_071302.2. NM_022019.5.
XP_006497251.1. XM_006497188.1.
XP_006497252.1. XM_006497189.1.
UniGeneiMm.404024.

3D structure databases

ProteinModelPortaliQ9ESS0.
SMRiQ9ESS0. Positions 149-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211005. 1 interaction.
IntActiQ9ESS0. 1 interaction.
STRINGi10090.ENSMUSP00000045838.

Proteomic databases

MaxQBiQ9ESS0.
PaxDbiQ9ESS0.
PRIDEiQ9ESS0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048655; ENSMUSP00000045838; ENSMUSG00000039384.
GeneIDi63953.
KEGGimmu:63953.
UCSCiuc007dym.1. mouse.

Organism-specific databases

CTDi11221.
MGIiMGI:1927070. Dusp10.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000069871.
HOVERGENiHBG102158.
InParanoidiQ9ESS0.
KOiK04459.
OMAiTCPANQM.
TreeFamiTF105122.

Miscellaneous databases

NextBioi319811.
PROiQ9ESS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESS0.
CleanExiMM_DUSP10.
ExpressionAtlasiQ9ESS0. baseline and differential.
GenevestigatoriQ9ESS0.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
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.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDUS10_MOUSE
AccessioniPrimary (citable) accession number: Q9ESS0
Secondary accession number(s): Q8R3L3, Q9CZY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.