[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Foreskin; DOI=10.1038/359644a0; PubMed=1406996 [NCBI, ExPASy, EBI, Israel, Japan] Keyes S.M., Emslie E.A.; "Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase."; Nature 359:644-647(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. PubMed=8106404 [NCBI, ExPASy, EBI, Israel, Japan] Kwak S.P., Hakes D.J., Martell K.J., Dixon J.E.; "Isolation and characterization of a human dual specificity protein-tyrosine phosphatase gene."; J. Biol. Chem. 269:3596-3604(1994).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-56 AND HIS-187. Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; 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).

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.
INTERACTION:
P28482:MAPK1; NbExp=2; IntAct=EBI-975493, EBI-959949;
P62988:RPS27A; NbExp=1; IntAct=EBI-975493, EBI-413034;
Q13309:SKP2; NbExp=1; IntAct=EBI-975493, EBI-456291;
TISSUE SPECIFICITY: Expressed at high levels in the lung, liver placenta and pancreas. Moderate levels seen in the heart and skeletal muscle. Lower levels found in the brain and kidney.
INDUCTION: By oxidative stress and heat shock.
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

X68277; CAA48338.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ301957; ABB96250.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022463; AAH22463.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S29090; S29090.

NP_004408.1; -.

3D structure databases

HSSP

Q05923; 1M3G. [HSSP ENTRY / PDB]

SMR

P28562; 171-313.

ModBase

P28562.

Protein-protein interaction databases

IntAct

P28562; -.

PTM databases

PhosphoSite

P28562; -.

Polymorphism databases

NIEHS-SNPs

DUSP1.

Organism-specific databases

HIX0005420; -.

HGNC:3064; DUSP1.

CAB018554; -.

600714; gene. [NCBI / EBI]

PharmGKB

PA27519; -.

GeneCards

P28562.

Gene expression databases

ArrayExpress

P28562; -.

CleanEx

HS_DUSP1; -.

GermOnline

ENSG00000120129; Homo sapiens.

Ontologies

GO:0017017;	Molecular function: MAP kinase tyrosine/serine/threonine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0004726;	Molecular function: non-membrane spanning protein tyrosine phosphatase activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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).
GO:0006979;	Biological process: response to oxidative stress (traceable author statement from ProtInc).
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

ENSG00000120129; Homo sapiens. [Contig view]

GeneID

1843; -.

KEGG

hsa:1843; -.

Phylogenomic databases

HOGENOM

P28562; -.

HOVERGEN

P28562; -.

Other

P28562; -.

7547; -.

DUSP1; Homo sapiens.

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

Keywords

Cell cycle; Hydrolase; Polymorphism; Protein phosphatase; Stress response.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Dual specificity protein phosphatase 1.`	`PRO_0000094790`
`DOMAIN`	`20 137`	`118`	`Rhodanese.`
`DOMAIN`	`175 367`	`193`	`Tyrosine-protein phosphatase.`
`ACT_SITE`	`258 258`		`Phosphocysteine intermediate (By similarity).`
`VARIANT`	`56 56`	`1`	`A -> T.`	`VAR_025201`
`VARIANT`	`187 187`	`1`	`Y -> H.`	`VAR_025202`

Sequence information

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

Molecular weight: 39298 Da [This is the MW of the unprocessed precursor]

CRC64: 11BD1D39A9FCD51F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVMEVGTLDA GGLRALLGER AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARAAQVFF 

       130        140        150        160        170        180 
LKGGYEAFSA SCPELCSKQS TPMGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILPF 

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

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

       310        320        330        340        350        360 
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHST NSALSYLQSP 


ITTSPSC

P28562 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