P28563 (DUS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 1
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Mitogen-activated protein kinase phosphatase 1
Short name=MAP kinase phosphatase 1
Short name=MKP-1
Protein-tyrosine phosphatase 3CH134
Protein-tyrosine phosphatase ERP

Gene names

Name:	Dusp1
Synonyms:	3ch134, Mkp1, Ptpn10, Ptpn16

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	367 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Nucleus By similarity.
Induction	By growth factors.
Post-translational modification	Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 rhodanese domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Nucleus
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular response to hormone stimulus Inferred from electronic annotation. Source: Compara endoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome intracellular signal transduction Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara protein dephosphorylation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of apoptotic process Inferred from Biological aspect of Ancestor. Source: RefGenome response to cAMP Inferred from electronic annotation. Source: Compara response to calcium ion Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to light stimulus Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	nucleoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/threonine phosphatase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 367	367	Dual specificity protein phosphatase 1		PRO_0000094791
Regions
	Domain	20 – 137	118	Rhodanese
	Domain	175 – 367	193	Tyrosine-protein phosphatase
Sites
	Active site	258	1	Phosphocysteine intermediate
Amino acid modifications
	Modified residue	359	1	Phosphoserine; by MAPK1 and MAPK3 Ref.5
	Modified residue	364	1	Phosphoserine; by MAPK1 and MAPK3 Ref.5
Experimental info
	Mutagenesis	258	1	C → S: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	P28563 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 50B5F90FEBBD19AB	FASTA	367	39,370
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence of a growth factor-inducible immediate early gene and characterization of its encoded protein." Charles C.H., Abler A.S., Lau L.F. Oncogene 7:187-190(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Structure, mapping, and expression of erp, a growth factor-inducible gene encoding a nontransmembrane protein tyrosine phosphatase, and effect of ERP on cell growth." Noguchi T., Metz R., Chen L., Mattei M.-G., Carrasco D., Bravo R. Mol. Cell. Biol. 13:5195-5205(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Liver.
[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]. Strain: Czech II. Tissue: Mammary gland.
[4]	"MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo." Sun H., Charles C.H., Lau L.F., Tonks N.K. Cell 75:487-493(1993) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation." Brondello J.M., Pouyssegur J., McKenzie F.R. Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-359 AND SER-364.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61940 mRNA. Translation: CAA43944.1. S64851 Genomic DNA. Translation: AAB27882.1. BC006967 mRNA. Translation: AAH06967.1.
IPI	IPI00122070.
PIR	S24411. A54681.
RefSeq	NP_038670.1. NM_013642.3.
UniGene	Mm.239041.
3D structure databases
ProteinModelPortal	P28563.
SMR	P28563. Positions 13-136, 172-314.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29877N.
STRING	10090.ENSMUSP00000025025.
PTM databases
PhosphoSite	P28563.
Proteomic databases
PRIDE	P28563.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
GeneID	19252.
KEGG	mmu:19252.
Organism-specific databases
CTD	1843.
MGI	MGI:105120. Dusp1.
Phylogenomic databases
eggNOG	COG2453.
HOGENOM	HOG000294080.
HOVERGEN	HBG007347.
InParanoid	P28563.
KO	K04459.
OMA	VLDCRSF.
OrthoDB	EOG4T1HMT.
Gene expression databases
ArrayExpress	P28563.
Bgee	P28563.
CleanEx	MM_DUSP1.
Genevestigator	P28563.
GermOnline	ENSMUSG00000024190. Mus musculus.
Family and domain databases
Gene3D	3.40.250.10. 1 hit.
InterPro	IPR020417. Atypical_DUSP. IPR020420. Atypical_DUSP_famB. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR008343. MKP. IPR001763. Rhodanese-like_dom. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. PF00581. Rhodanese. 1 hit. [Graphical view]
PIRSF	PIRSF000939. MAPK_Ptase. 1 hit.
PRINTS	PR01908. ADSPHPHTASE. PR01910. ADSPHPHTASEB. PR01764. MAPKPHPHTASE.
SMART	SM00195. DSPc. 1 hit. SM00450. RHOD. 1 hit. [Graphical view]
SUPFAM	SSF52821. Rhodanese-like. 1 hit.
PROSITE	PS50206. RHODANESE_3. 1 hit. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P28563.
ChEMBL	CHEMBL5623.
NextBio	296092.
SOURCE	Search...

Entry information

Entry name

DUS1_MOUSE

Accession

Primary (citable) accession number: P28563

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program