Q64623 (DUS1_RAT) 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 CL100
Protein-tyrosine phosphatase non-receptor type 16

Gene names

Name:	Dusp1
Synonyms:	Cl100, Mkp1, Ptpn16

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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 By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Nucleus By similarity.
Tissue specificity	Brain. High level expression seen in the cingulate gyrus within the retrospinal cortex, ventral and medial divisions of the anterior thalamus and the medial geniculate nucleus. Expressed at moderate levels in the parietal and temporal cortex. Expressed in the cerebellum. Ref.3 Ref.4 Ref.5
Induction	Exhibits night/day variations with a 100-fold increased expression at night in the pineal gland (at protein level). Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. Ref.4 Ref.5
Post-translational modification	Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation By similarity.
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 expression pattern PubMed 15358679. Source: RGD endoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome intracellular signal transduction Inferred from direct assay Ref.2. Source: RGD negative regulation of apoptotic process Inferred from mutant phenotype PubMed 15059639. Source: RGD positive regulation of apoptotic process Inferred from mutant phenotype PubMed 9228085. Source: RGD protein dephosphorylation Inferred from direct assay PubMed 12435803. Source: RGD response to cAMP Inferred from expression pattern PubMed 15358679. Source: RGD response to calcium ion Inferred from expression pattern Ref.2. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 8804359. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern PubMed 17403137. Source: RGD response to hydrogen peroxide Inferred from expression pattern PubMed 7540516. Source: RGD response to light stimulus Inferred from expression pattern Ref.4. Source: RGD response to retinoic acid Inferred from expression pattern PubMed 15494319. Source: RGD response to testosterone stimulus Inferred from expression pattern PubMed 8804359. Source: RGD
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 direct assay PubMed 12435803. Source: RGD
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_0000094792
Regions
	Domain	20 – 137	118	Rhodanese
	Domain	175 – 367	193	Tyrosine-protein phosphatase
Sites
	Active site	258	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	359	1	Phosphoserine; by MAPK1 and MAPK3 By similarity
	Modified residue	364	1	Phosphoserine; by MAPK1 and MAPK3 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q64623 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5112ADF290499139	FASTA	367	39,541
	10 20 30 40 50 60 MVMEVGILDA GGLRALLRER AAQCLLLDCR SFFAFNAGHI VGSVNVRFST IVRRRAKGAM 70 80 90 100 110 120 GLEHIVPNTE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARSTQVFF 130 140 150 160 170 180 LQGGYEAFSA SCPELCSKQS TPMGLSLPLS 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 NSALNYLQSP ITTSPSC

References

[1]	"Pathways regulating CL100 gene expression in pituitary cells." Muda M., Schlegel W., Arkinstall S. Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Lung.
[2]	"MAP kinase phosphatase-1 gene transcription in rat neuroendocrine cells is modulated by a calcium-sensitive block to elongation in the first exon." Ryser S., Tortola S., van Haasteren G., Muda M., Li S., Schlegel W. J. Biol. Chem. 276:33319-33327(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Wistar Furth.
[3]	"Isolation and characterization of a human dual specificity protein-tyrosine phosphatase gene." Kwak S.P., Hakes D.J., Martell K.J., Dixon J.E. J. Biol. Chem. 269:3596-3604(1994) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Mitogen-activated protein kinase phosphatase-1 (MKP-1): >100-fold nocturnal and norepinephrine-induced changes in the rat pineal gland." Price D.M., Chik C.L., Terriff D., Weller J., Humphries A., Carter D.A., Klein D.C., Ho A.K. FEBS Lett. 577:220-226(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[5]	"Night/day changes in pineal expression of >600 genes: central role of adrenergic/cAMP signaling." Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q., Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F., Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C. J. Biol. Chem. 284:7606-7622(2009) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X84004 mRNA. Translation: CAA58828.1. AF357203 Genomic DNA. Translation: AAK55327.1.
IPI	IPI00327942.
PIR	S52265.
RefSeq	NP_446221.2. NM_053769.3.
UniGene	Rn.98260.
3D structure databases
ProteinModelPortal	Q64623.
SMR	Q64623. Positions 171-313.
ModBase	Search...
Proteomic databases
PRIDE	Q64623.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000005383; ENSRNOP00000005383; ENSRNOG00000003977.
GeneID	114856.
KEGG	rno:114856.
UCSC	RGD:620897. rat.
Organism-specific databases
CTD	1843.
RGD	620897. Dusp1.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104321.
HOGENOM	HOG000294080.
HOVERGEN	HBG007347.
InParanoid	Q64623.
KO	K04459.
OMA	VLDCRSF.
OrthoDB	EOG4T1HMT.
Gene expression databases
Genevestigator	Q64623.
GermOnline	ENSRNOG00000003977. Rattus norvegicus.
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
NextBio	618903.

Entry information

Entry name

DUS1_RAT

Accession

Primary (citable) accession number: Q64623
Secondary accession number(s): Q548G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program