Q9D7X3 (DUS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 3
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
T-DSP11
Vaccinia H1-related phosphatase
Short name=VHR

Gene names

Name:

Dusp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2 By similarity. Ref.5
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with VRK3, which seems to activate it's phosphatase activity. Ref.5
Subcellular location	Nucleus Ref.5.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of ERK1 and ERK2 cascade Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of JNK cascade Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of T cell activation Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of T cell receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of mitotic cell cycle Inferred from Biological aspect of Ancestor. Source: RefGenome protein dephosphorylation Inferred from direct assay PubMed 18035061. Source: MGI
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome immunological synapse Inferred from electronic annotation. Source: Compara nucleoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	MAP kinase phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from direct assay PubMed 11432789. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	Dual specificity protein phosphatase 3		PRO_0000094796
Regions
	Domain	99 – 169	71	Tyrosine-protein phosphatase
Sites
	Active site	124	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9D7X3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 62E519E41BE575D5	FASTA	185	20,472
	10 20 30 40 50 60 MSSSFELSVQ DLNDLLSDGS GCYSLPSQPC NEVVPRVYVG NASVAQDITQ LQKLGITHVL 70 80 90 100 110 120 NAAEGRSFMH VNTSASFYED SGITYLGIKA NDTQEFNLSA YFERATDFID QALAHKNGRV 130 140 150 160 170 180 LVHCREGYSR SPTLVIAYLM MRQKMDVKSA LSTVRQNREI GPNDGFLAQL CQLNDRLAKE GKVKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of novel putative dual specificity protein phosphatases T-DSP6 and T-DSP11 with low molecular masses containing a single catalytic domain but not cdc25 homology domain." Aoyama K., Matsuda T., Aoki N. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. Tissue: Stomach.
[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].
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 90-104 AND 159-176, MASS SPECTROMETRY. Tissue: Hippocampus.
[5]	"Negative regulation of ERK activity by VRK3-mediated activation of VHR phosphatase." Kang T.H., Kim K.T. Nat. Cell Biol. 8:863-869(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VRK3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF280809 mRNA. Translation: AAK69507.1. AK008734 mRNA. Translation: BAB25864.1. BC016269 mRNA. Translation: AAH16269.1.
IPI	IPI00110990.
RefSeq	NP_082483.1. NM_028207.3.
UniGene	Mm.196295. Mm.489869.
3D structure databases
ProteinModelPortal	Q9D7X3.
SMR	Q9D7X3. Positions 7-184.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4093702.
PTM databases
PhosphoSite	Q9D7X3.
Proteomic databases
PaxDb	Q9D7X3.
PRIDE	Q9D7X3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000003612; ENSMUSP00000003612; ENSMUSG00000003518. ENSMUST00000107172; ENSMUSP00000102790; ENSMUSG00000003518.
GeneID	72349.
KEGG	mmu:72349.
UCSC	uc007lqa.2. mouse.
Organism-specific databases
CTD	1845.
MGI	MGI:1919599. Dusp3.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00550000074474.
HOGENOM	HOG000233767.
HOVERGEN	HBG001524.
InParanoid	Q9D7X3.
KO	K04459.
OrthoDB	EOG46Q6TP.
Gene expression databases
ArrayExpress	Q9D7X3.
Bgee	Q9D7X3.
Genevestigator	Q9D7X3.
GermOnline	ENSMUSG00000003518. Mus musculus.
Family and domain databases
InterPro	IPR020417. Atypical_DUSP. IPR020405. Atypical_DUSP_famA. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PRINTS	PR01908. ADSPHPHTASE. PR01909. ADSPHPHTASEA.
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	336089.
SOURCE	Search...

Entry information

Entry name

DUS3_MOUSE

Accession

Primary (citable) accession number: Q9D7X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program