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Protein

Dual specificity protein phosphatase 10

Gene

Dusp10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. It preferably dephosphorylates p38.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei409Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • dephosphorylation Source: MGI
  • inactivation of MAPK activity Source: UniProtKB
  • negative regulation of epithelial cell migration Source: BHF-UCL
  • negative regulation of epithelial cell proliferation Source: BHF-UCL
  • negative regulation of epithelium regeneration Source: BHF-UCL
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of JNK cascade Source: MGI
  • negative regulation of JUN kinase activity Source: MGI
  • negative regulation of oligodendrocyte differentiation Source: Ensembl
  • negative regulation of p38MAPK cascade Source: MGI
  • negative regulation of protein kinase activity by regulation of protein phosphorylation Source: MGI
  • negative regulation of respiratory burst involved in inflammatory response Source: MGI
  • negative regulation of stress-activated MAPK cascade Source: MGI
  • negative regulation of stress-activated protein kinase signaling cascade Source: MGI
  • oligodendrocyte differentiation Source: MGI
  • peptidyl-threonine dephosphorylation Source: MGI
  • peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: MGI
  • positive regulation of regulatory T cell differentiation Source: MGI
  • protein dephosphorylation Source: BHF-UCL
  • regulation of adaptive immune response Source: MGI
  • regulation of brown fat cell differentiation Source: MGI
  • regulation of innate immune response Source: MGI
  • response to lipopolysaccharide Source: MGI

Keywordsi

Molecular functionHydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiR-MMU-112409 RAF-independent MAPK1/3 activation
R-MMU-5675221 Negative regulation of MAPK pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 10 (EC:3.1.3.16By similarity, EC:3.1.3.48By similarity)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1927070 Dusp10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000948141 – 483Dual specificity protein phosphatase 10Add BLAST483

Proteomic databases

MaxQBiQ9ESS0
PaxDbiQ9ESS0
PeptideAtlasiQ9ESS0
PRIDEiQ9ESS0

PTM databases

iPTMnetiQ9ESS0
PhosphoSitePlusiQ9ESS0

Expressioni

Gene expression databases

BgeeiENSMUSG00000039384
CleanExiMM_DUSP10
ExpressionAtlasiQ9ESS0 baseline and differential
GenevisibleiQ9ESS0 MM

Interactioni

Subunit structurei

Monomer. Interacts with MAPK14.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211005, 1 interactor
IntActiQ9ESS0, 1 interactor
STRINGi10090.ENSMUSP00000045838

Structurei

3D structure databases

ProteinModelPortaliQ9ESS0
SMRiQ9ESS0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini169 – 286RhodanesePROSITE-ProRule annotationAdd BLAST118
Domaini386 – 456Tyrosine-protein phosphataseAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 216Interaction with MAP kinasesBy similarityAdd BLAST17

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1716 Eukaryota
COG2453 LUCA
GeneTreeiENSGT00760000118902
HOGENOMiHOG000069871
HOVERGENiHBG102158
InParanoidiQ9ESS0
KOiK20216
OMAiMTKCSKS
OrthoDBiEOG091G0V6S
TreeFamiTF105122

Family and domain databases

CDDicd00127 DSPc, 1 hit
Gene3Di3.40.250.10, 1 hit
3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR020417 Atypical_DUSP
IPR000340 Dual-sp_phosphatase_cat-dom
IPR024950 DUSP
IPR008343 MKP
IPR029021 Prot-tyrosine_phosphatase-like
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf
IPR016130 Tyr_Pase_AS
IPR000387 TYR_PHOSPHATASE_dom
IPR020422 TYR_PHOSPHATASE_DUAL_dom
PANTHERiPTHR10159 PTHR10159, 1 hit
PfamiView protein in Pfam
PF00782 DSPc, 1 hit
PF00581 Rhodanese, 1 hit
PRINTSiPR01908 ADSPHPHTASE
PR01764 MAPKPHPHTASE
SMARTiView protein in SMART
SM00195 DSPc, 1 hit
SM00450 RHOD, 1 hit
SUPFAMiSSF52799 SSF52799, 1 hit
SSF52821 SSF52821, 1 hit
PROSITEiView protein in PROSITE
PS50206 RHODANESE_3, 1 hit
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
PS50054 TYR_PHOSPHATASE_DUAL, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti48T → A in BAB17680 (PubMed:11060451).Curated1
Sequence conflicti113P → S in BAB27966 (PubMed:16141072).Curated1
Sequence conflicti386Q → R in BAB17680 (PubMed:11060451).Curated1

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_006497188.2
XP_006497252.1, XM_006497189.1
UniGeneiMm.404024

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiDUS10_MOUSE
AccessioniPrimary (citable) accession number: Q9ESS0
Secondary accession number(s): Q8R3L3, Q9CZY9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: July 27, 2011
Last modified: March 28, 2018
This is version 135 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health