[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; PubMed=1741163 [NCBI, ExPASy, EBI, Israel, Japan] Charles C.H., Abler A.S., Lau L.F.; "cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein."; Oncogene 7:187-190(1992).
[2]	NUCLEOTIDE SEQUENCE. TISSUE=Liver; PubMed=8355678 [NCBI, ExPASy, EBI, Israel, Japan] Noguchi T., Metz R., Chen L., Mattei M.-G., Carrasco D., Bravo R.; "Structure, mapping, and expression of erp, a growth factor-inducible gene encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP on cell growth."; Mol. Cell. Biol. 13:5195-5205(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Czech II; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	CHARACTERIZATION. DOI=10.1016/0092-8674(93)90383-2; PubMed=8221888 [NCBI, ExPASy, EBI, Israel, Japan] Sun H., Charles C.H., Lau L.F., Tonks N.K.; "MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo."; Cell 75:487-493(1993).

Comments

FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase ERK2 on both 'Thr-183' and 'Tyr-185'.
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
CATALYTIC ACTIVITY: A phosphoprotein + H₂O = a protein + phosphate.
INDUCTION: By growth factors.
SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
SIMILARITY: Contains 1 rhodanese domain.
SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X61940; CAA43944.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S64851; AAB27882.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006967; AAH06967.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A54681; S24411.

NP_038670.1; -.

3D structure databases

HSSP

Q05923; 1M3G. [HSSP ENTRY / PDB]

P28563; 171-313.

PTM databases

P28563; -.

Organism-specific databases

MGI

MGI:105120; Dusp1.

Gene expression databases

ArrayExpress

P28563; -.

CleanEx

MM_DUSP1; -.

GermOnline

ENSMUSG00000024190; Mus musculus.

Ontologies

GO:0017017;	Molecular function: MAP kinase tyrosine/serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0004725;	Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0006470;	Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR008343; MAPK_phosph.
IPR014393; MAPK_Ptase.
IPR001763; Rhodanese-like.
IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000340; Tyr_Pase_dual_specific.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.250.10; Rhodanese-like; 1.

Pfam

PF00782; DSPc; 1.
PF00581; Rhodanese; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000939; MAPK_Ptase; 1.

PRINTS

PR01764; MAPKPHPHTASE.

SMART

SM00195; DSPc; 1.
SM00450; RHOD; 1.
SMART graphical view of domain structure.

PROSITE

PS50206; RHODANESE_3; 1.
PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 1.
PS50054; TYR_PHOSPHATASE_DUAL; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000024190; Mus musculus. [Contig view]

GeneID

19252; -.

KEGG

mmu:19252; -.

Phylogenomic databases

HOGENOM

P28563; -.

HOVERGEN

P28563; -.

Other

NextBio

296092; -.

SOURCE

Dusp1; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell cycle; Hydrolase; Protein phosphatase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Dual specificity protein phosphatase 1.`	`PRO_0000094791`
`DOMAIN`	`20 137`	`118`	`Rhodanese.`
`DOMAIN`	`175 367`	`193`	`Tyrosine-protein phosphatase.`
`ACT_SITE`	`258 258`		`Phosphocysteine intermediate.`
`MUTAGEN`	`258 258`		`C->S: Loss of activity.`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 39370 Da [This is the MW of the unprocessed precursor]

CRC64: 50B5F90FEBBD19AB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG TLALAAGALC REARSTQVFF 

       130        140        150        160        170        180 
LQGGYEAFSA SCPELCSKQS TPTGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILSF 

       190        200        210        220        230        240 
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA 

       250        260        270        280        290        300 
IDFIDSIKDA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 

       310        320        330        340        350        360 
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT NSALNYLKSP 


ITTSPSC

P28563 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools