DUSP10

Functionⁱ

Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.3 Publications

Catalytic activityⁱ

H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10044
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
EC:
3.1.3.48
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10044
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
zoom
=
L-tyrosyl-[protein]
L-tyrosine residue
zoom
+
phosphate
zoom
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-seryl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-seryl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
EC:
3.1.3.16
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
O-phospho-L-seryl-[protein]
O-phospho-L-serine residue
zoom
=
L-seryl-[protein]
L-serine residue
zoom
+
phosphate
zoom
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
EC:
3.1.3.16
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "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.
- Ref.10
  "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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
O-phospho-L-threonyl-[protein]
O-phospho-L-threonine residue
zoom
=
L-threonyl-[protein]
L-threonine residue
zoom
+
phosphate
zoom

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	408	Phosphocysteine intermediate2 Publications		1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protein phosphatase

Molecular function

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAⁱ	3.1.3.16 2681 3.1.3.48 2681
Reactomeⁱ	R-HSA-112409 RAF-independent MAPK1/3 activation R-HSA-5675221 Negative regulation of MAPK pathway
SABIO-RKⁱ	Q9Y6W6
SignaLinkⁱ	Q9Y6W6
SIGNORⁱ	Q9Y6W6

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dual specificity protein phosphatase 10 (EC:3.1.3.162 Publications, EC:3.1.3.482 Publications) 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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3065 DUSP10
MIMⁱ	608867 gene
neXtProtⁱ	NX_Q9Y6W6

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	180 – 181	FM → DD: Reduced enzyme activity with MAPK14. 1 Publication		2
Mutagenesisⁱ	203 – 204	RR → AA: Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14. 1 Publication		2

Organism-specific databases

DisGeNET More...DisGeNETⁱ	11221
Open Targets More...OpenTargetsⁱ	ENSG00000143507
PharmGKBⁱ	PA27520

Miscellaneous databases

Pharosⁱ	Q9Y6W6

Pharosⁱ

Q9Y6W6

Chemistry databases

ChEMBLⁱ	CHEMBL2396511

ChEMBLⁱ

CHEMBL2396511

Polymorphism and mutation databases

BioMutaⁱ	DUSP10
DMDMⁱ	20138090

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000094813	1 – 482	Dual specificity protein phosphatase 10Add BLAST		482

Proteomic databases

MassIVEⁱ	Q9Y6W6
PaxDbⁱ	Q9Y6W6
PeptideAtlas More...PeptideAtlasⁱ	Q9Y6W6
PRIDEⁱ	Q9Y6W6
ProteomicsDBⁱ	86803 [Q9Y6W6-1] 86804 [Q9Y6W6-2]

PTM databases

DEPODⁱ	Q9Y6W6
iPTMnetⁱ	Q9Y6W6
PhosphoSitePlusⁱ	Q9Y6W6

Expressionⁱ

Tissue specificityⁱ

Expressed in keratinocytes (at protein level) (PubMed:29043977). Detected in brain (PubMed:16806267).2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000143507 Expressed in 212 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis
ExpressionAtlasⁱ	Q9Y6W6 baseline and differential
Genevisibleⁱ	Q9Y6W6 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA016758

HPAⁱ

HPA016758

Interactionⁱ

Subunit structureⁱ

Monomer.

Interacts with MAPK14.

3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P45984	3	EBI-3443946,EBI-713568

With

Entry

#Exp.

IntAct

Notes

P45984

3

EBI-3443946,EBI-713568

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	116389, 24 interactors
ELMⁱ	Q9Y6W6
IntActⁱ	Q9Y6W6, 22 interactors
Molecular INTeraction database More...MINTⁱ	Q9Y6W6
STRINGⁱ	9606.ENSP00000355866

Chemistry databases

BindingDBⁱ

Q9Y6W6

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	152 – 160	Combined sources	9
Beta strandⁱ	173 – 176	Combined sources	4
Helixⁱ	180 – 185	Combined sources	6
Beta strandⁱ	186 – 188	Combined sources	3
Helixⁱ	199 – 206	Combined sources	8
Helixⁱ	212 – 217	Combined sources	6
Helixⁱ	224 – 230	Combined sources	7
Beta strandⁱ	233 – 236	Combined sources	4
Helixⁱ	243 – 245	Combined sources	3
Beta strandⁱ	248 – 250	Combined sources	3
Helixⁱ	251 – 261	Combined sources	11
Beta strandⁱ	267 – 269	Combined sources	3
Helixⁱ	272 – 276	Combined sources	5
Turnⁱ	277 – 279	Combined sources	3
Helixⁱ	281 – 283	Combined sources	3
Beta strandⁱ	284 – 286	Combined sources	3
Beta strandⁱ	323 – 326	Combined sources	4
Beta strandⁱ	329 – 332	Combined sources	4
Helixⁱ	336 – 338	Combined sources	3
Helixⁱ	340 – 345	Combined sources	6
Beta strandⁱ	348 – 353	Combined sources	6
Beta strandⁱ	356 – 358	Combined sources	3
Helixⁱ	363 – 365	Combined sources	3
Beta strandⁱ	368 – 372	Combined sources	5
Beta strandⁱ	378 – 380	Combined sources	3
Helixⁱ	384 – 386	Combined sources	3
Helixⁱ	387 – 399	Combined sources	13
Beta strandⁱ	403 – 407	Combined sources	5
Beta strandⁱ	409 – 413	Combined sources	5
Helixⁱ	414 – 426	Combined sources	13
Helixⁱ	431 – 441	Combined sources	11
Helixⁱ	449 – 463	Combined sources	15
Helixⁱ	478 – 482	Combined sources	5

Show more details

3D structure databases

SMRⁱ	Q9Y6W6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q9Y6W6

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	168 – 285	RhodanesePROSITE-ProRule annotationAdd BLAST		118
Domainⁱ	384 – 453	Tyrosine-protein phosphataseAdd BLAST		70

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	199 – 215	Interaction with MAP kinasesAdd BLAST		17

Sequence similaritiesⁱ

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1716 Eukaryota COG2453 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157671
HOGENOMⁱ	HOG000069871
InParanoidⁱ	Q9Y6W6
KEGG Orthology (KO) More...KOⁱ	K20216
OMAⁱ	QRMNIGY
Database of Orthologous Groups More...OrthoDBⁱ	1576308at2759
PhylomeDBⁱ	Q9Y6W6
TreeFamⁱ	TF105122

Family and domain databases

Gene3Dⁱ	3.40.250.10, 1 hit 3.90.190.10, 1 hit
InterProⁱ	View protein in InterPro IPR020417 Atypical_DUSP IPR000340 Dual-sp_phosphatase_cat-dom 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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00782 DSPc, 1 hit PF00581 Rhodanese, 1 hit
PRINTSⁱ	PR01908 ADSPHPHTASE PR01764 MAPKPHPHTASE
SMARTⁱ	View protein in SMART SM00195 DSPc, 1 hit SM00450 RHOD, 1 hit
SUPFAMⁱ	SSF52799 SSF52799, 1 hit SSF52821 SSF52821, 1 hit
PROSITEⁱ	View 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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: Q9Y6W6-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSANPGSN SHPPVIATTV 
        60         70         80         90        100
VSLKAANLTY MPSSSGSARS LNCGCSSASC CTVATYDKDN QAQTQAIAAG 
       110        120        130        140        150
TTTTAIGTST TCPANQMVNN NENTGSLSPS SGVGSPVSGT PKQLASIKII 
       160        170        180        190        200
YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF MEYNKSHIQG AVHINCADKI 
       210        220        230        240        250
SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT NEPSRVMPSQ 
       260        270        280        290        300
PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREVGGGA 
       310        320        330        340        350
SAASSLLPQP IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY 
       360        370        380        390        400
VINVTTHLPL YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC 
       410        420        430        440        450
GKGLLIHCQA GVSRSATIVI AYLMKHTRMT MTDAYKFVKG KRPIISPNLN 
       460        470        480 
FMGQLLEFEE DLNNGVTPRI LTPKLMGVET VV

Length:482

Mass (Da):52,642

Last modified:November 1, 1999 - v1

Checksum:ⁱA8CB74ABF9498CD4

GO

Isoform 2 (identifier: Q9Y6W6-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MQRLNIGYVI NVTTHLPLYH YEKGLFNYKR LPATDSNKQN LRQYFEEAFE 
        60         70         80         90        100
FIEEAHQCGK GLLIHCQAGV SRSATIVIAY LMKHTRMTMT DAYKFVKGKR 
       110        120        130        140
PIISPNLNFM GQLLEFEEDL NNGVTPRILT PKLMGVETVV

Show »

Length:140

Mass (Da):16,110

Checksum:ⁱCE151F365D042516

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0B4J2F5	A0A0B4J2F5_HUMAN		Dual-specificity protein phosphatas... Dual-specificity protein phosphatase 10	DUSP10	66	Annotation score:

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_036549	1 – 342	Missing in isoform 2. 2 PublicationsAdd BLAST		342

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB026436 mRNA Translation: BAA81668.1 AF179212 mRNA Translation: AAD51857.1 AK022513 mRNA Translation: BAB14070.1 AL590966 Genomic DNA No translation available. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS1528.1 [Q9Y6W6-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_009138.1, NM_007207.5 [Q9Y6W6-1]

Genome annotation databases

Ensemblⁱ	ENST00000366899; ENSP00000355866; ENSG00000143507 [Q9Y6W6-1]
GeneIDⁱ	11221
KEGGⁱ	hsa:11221
UCSC genome browser More...UCSCⁱ	uc001hmy.3 human [Q9Y6W6-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9Y6W6-2	Uncharacterized protein		wild yak		605	UniRef100_A0A5A9QZA8

Protein	Similar proteins		Species	Score	Length	Source
Q9Y6W6	Dual specificity protein phosphatase 10		MOUSE		483	UniRef90_Q9Y6W6
Dual specificity protein phosphatase 10		BOVIN		482
Uncharacterized protein		MACMU		505
Uncharacterized protein		CERAT		505
Uncharacterized protein		MACNE		488
+138
Q9Y6W6-2	Dual specificity phosphatase 10		PANTR		488	UniRef90_A0A2I3TAP3
DUSP10 isoform 1		PONAB		482
Uncharacterized protein		wild yak		605
Uncharacterized protein		MANLE		505
Uncharacterized protein		RHIRO		500
+16

Protein	Similar proteins		Species	Score	Length	Source
Q9Y6W6	Dual specificity protein phosphatase 10		MOUSE		483	UniRef50_Q9Y6W6
Dual specificity protein phosphatase 10		BOVIN		482
Uncharacterized protein		MACMU		505
Uncharacterized protein		CERAT		505
Uncharacterized protein		MACNE		488
+332

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB026436 mRNA Translation: BAA81668.1 AF179212 mRNA Translation: AAD51857.1 AK022513 mRNA Translation: BAB14070.1 AL590966 Genomic DNA No translation available. 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
CCDSⁱ	CCDS1528.1 [Q9Y6W6-1]
RefSeqⁱ	NP_009138.1, NM_007207.5 [Q9Y6W6-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1ZZW	X-ray	1.60	A/B	320-467	[»]
	2OUC	X-ray	2.20	A/B	148-287	[»]
	2OUD	X-ray	2.80	A	315-482	[»]
	3TG1	X-ray	2.71	B	139-288	[»]
SMRⁱ	Q9Y6W6
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	116389, 24 interactors
ELMⁱ	Q9Y6W6
IntActⁱ	Q9Y6W6, 22 interactors
MINTⁱ	Q9Y6W6
STRINGⁱ	9606.ENSP00000355866

Chemistry databases

BindingDBⁱ	Q9Y6W6
ChEMBLⁱ	CHEMBL2396511

PTM databases

DEPODⁱ	Q9Y6W6
iPTMnetⁱ	Q9Y6W6
PhosphoSitePlusⁱ	Q9Y6W6

Polymorphism and mutation databases

BioMutaⁱ	DUSP10
DMDMⁱ	20138090

Proteomic databases

MassIVEⁱ	Q9Y6W6
PaxDbⁱ	Q9Y6W6
PeptideAtlasⁱ	Q9Y6W6
PRIDEⁱ	Q9Y6W6
ProteomicsDBⁱ	86803 [Q9Y6W6-1] 86804 [Q9Y6W6-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	11221

DNASUⁱ

11221

Genome annotation databases

Ensemblⁱ	ENST00000366899; ENSP00000355866; ENSG00000143507 [Q9Y6W6-1]
GeneIDⁱ	11221
KEGGⁱ	hsa:11221
UCSCⁱ	uc001hmy.3 human [Q9Y6W6-1]

Organism-specific databases

CTDⁱ	11221
DisGeNETⁱ	11221
GeneCardsⁱ	DUSP10
HGNCⁱ	HGNC:3065 DUSP10
HPAⁱ	HPA016758
MIMⁱ	608867 gene
neXtProtⁱ	NX_Q9Y6W6
OpenTargetsⁱ	ENSG00000143507
PharmGKBⁱ	PA27520
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1716 Eukaryota COG2453 LUCA
GeneTreeⁱ	ENSGT00940000157671
HOGENOMⁱ	HOG000069871
InParanoidⁱ	Q9Y6W6
KOⁱ	K20216
OMAⁱ	QRMNIGY
OrthoDBⁱ	1576308at2759
PhylomeDBⁱ	Q9Y6W6
TreeFamⁱ	TF105122

Enzyme and pathway databases

BRENDAⁱ	3.1.3.16 2681 3.1.3.48 2681
Reactomeⁱ	R-HSA-112409 RAF-independent MAPK1/3 activation R-HSA-5675221 Negative regulation of MAPK pathway
SABIO-RKⁱ	Q9Y6W6
SignaLinkⁱ	Q9Y6W6
SIGNORⁱ	Q9Y6W6

Miscellaneous databases

EvolutionaryTraceⁱ	Q9Y6W6
GeneWikiⁱ	DUSP10
GenomeRNAiⁱ	11221
Pharosⁱ	Q9Y6W6
Protein Ontology More...PROⁱ	PR:Q9Y6W6
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000143507 Expressed in 212 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis
ExpressionAtlasⁱ	Q9Y6W6 baseline and differential
Genevisibleⁱ	Q9Y6W6 HS

Family and domain databases

Gene3Dⁱ	3.40.250.10, 1 hit 3.90.190.10, 1 hit
InterProⁱ	View protein in InterPro IPR020417 Atypical_DUSP IPR000340 Dual-sp_phosphatase_cat-dom 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
Pfamⁱ	View protein in Pfam PF00782 DSPc, 1 hit PF00581 Rhodanese, 1 hit
PRINTSⁱ	PR01908 ADSPHPHTASE PR01764 MAPKPHPHTASE
SMARTⁱ	View protein in SMART SM00195 DSPc, 1 hit SM00450 RHOD, 1 hit
SUPFAMⁱ	SSF52799 SSF52799, 1 hit SSF52821 SSF52821, 1 hit
PROSITEⁱ	View 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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DUS10_HUMAN
Accessionⁱ	Q9Y6W6Primary (citable) accession number: Q9Y6W6 Secondary accession number(s): D3DTB4, Q6GSI4, Q9H9Z5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
	Last sequence update:	November 1, 1999
	Last modified:	October 16, 2019
	This is version 177 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
SIMILARITY comments
Index of protein domains and families
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9Y6W6 (DUS10_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Dual specificity protein phosphatase 10

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Golgi apparatus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ