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P28563

- DUS1_MOUSE

UniProt

P28563 - DUS1_MOUSE

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Protein

Dual specificity protein phosphatase 1

Gene
Dusp1, 3ch134, Mkp1, Ptpn10, Ptpn16
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei258 – 2581Phosphocysteine intermediate

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: UniProtKB
  2. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  3. protein tyrosine/threonine phosphatase activity Source: Ensembl
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to hormone stimulus Source: Ensembl
  2. endoderm formation Source: RefGenome
  3. inactivation of MAPK activity Source: UniProtKB
  4. intracellular signal transduction Source: Ensembl
  5. mitotic cell cycle arrest Source: UniProtKB
  6. negative regulation of apoptotic process Source: Ensembl
  7. negative regulation of MAPK cascade Source: UniProtKB
  8. negative regulation of MAP kinase activity Source: UniProtKB
  9. negative regulation of meiotic cell cycle Source: UniProtKB
  10. peptidyl-threonine dephosphorylation Source: UniProtKB
  11. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  12. positive regulation of apoptotic process Source: Ensembl
  13. protein dephosphorylation Source: RefGenome
  14. regulation of apoptotic process Source: RefGenome
  15. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  16. response to calcium ion Source: Ensembl
  17. response to cAMP Source: Ensembl
  18. response to estradiol Source: Ensembl
  19. response to glucocorticoid Source: Ensembl
  20. response to hydrogen peroxide Source: Ensembl
  21. response to light stimulus Source: Ensembl
  22. response to retinoic acid Source: Ensembl
  23. response to testosterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
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 namesi
Name:Dusp1
Synonyms:3ch134, Mkp1, Ptpn10, Ptpn16
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:105120. Dusp1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581C → S: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Dual specificity protein phosphatase 1PRO_0000094791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591Phosphoserine; by MAPK1 and MAPK31 Publication
Modified residuei364 – 3641Phosphoserine; by MAPK1 and MAPK31 Publication

Post-translational modificationi

Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP28563.

PTM databases

PhosphoSiteiP28563.

Expressioni

Inductioni

By growth factors.

Gene expression databases

ArrayExpressiP28563.
BgeeiP28563.
CleanExiMM_DUSP1.
GenevestigatoriP28563.

Interactioni

Protein-protein interaction databases

BioGridi202482. 3 interactions.
DIPiDIP-29877N.
STRINGi10090.ENSMUSP00000025025.

Structurei

3D structure databases

ProteinModelPortaliP28563.
SMRiP28563. Positions 13-136, 172-314.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118RhodaneseAdd
BLAST
Domaini175 – 367193Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiP28563.
KOiK04459.
OMAiSFNSSHI.
OrthoDBiEOG75MVWD.
PhylomeDBiP28563.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28563-1 [UniParc]FASTAAdd to Basket

« Hide

MVMEVGILDA GGLRALLREG AAQCLLLDCR SFFAFNAGHI AGSVNVRFST    50
IVRRRAKGAM GLEHIVPNAE LRGRLLAGAY HAVVLLDERS ASLDGAKRDG 100
TLALAAGALC REARSTQVFF LQGGYEAFSA SCPELCSKQS TPTGLSLPLS 150
TSVPDSAESG CSSCSTPLYD QGGPVEILSF LYLGSAYHAS RKDMLDALGI 200
TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA IDFIDSIKDA 250
GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 300
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHPT 350
NSALNYLKSP ITTSPSC 367
Length:367
Mass (Da):39,370
Last modified:December 1, 1992 - v1
Checksum:i50B5F90FEBBD19AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61940 mRNA. Translation: CAA43944.1.
S64851 Genomic DNA. Translation: AAB27882.1.
BC006967 mRNA. Translation: AAH06967.1.
CCDSiCCDS28552.1.
PIRiA54681. S24411.
RefSeqiNP_038670.1. NM_013642.3.
UniGeneiMm.239041.

Genome annotation databases

EnsembliENSMUST00000025025; ENSMUSP00000025025; ENSMUSG00000024190.
GeneIDi19252.
KEGGimmu:19252.
UCSCiuc008bee.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61940 mRNA. Translation: CAA43944.1 .
S64851 Genomic DNA. Translation: AAB27882.1 .
BC006967 mRNA. Translation: AAH06967.1 .
CCDSi CCDS28552.1.
PIRi A54681. S24411.
RefSeqi NP_038670.1. NM_013642.3.
UniGenei Mm.239041.

3D structure databases

ProteinModelPortali P28563.
SMRi P28563. Positions 13-136, 172-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202482. 3 interactions.
DIPi DIP-29877N.
STRINGi 10090.ENSMUSP00000025025.

Chemistry

BindingDBi P28563.
ChEMBLi CHEMBL5623.

PTM databases

PhosphoSitei P28563.

Proteomic databases

PRIDEi P28563.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025025 ; ENSMUSP00000025025 ; ENSMUSG00000024190 .
GeneIDi 19252.
KEGGi mmu:19252.
UCSCi uc008bee.2. mouse.

Organism-specific databases

CTDi 1843.
MGIi MGI:105120. Dusp1.

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000294080.
HOVERGENi HBG007347.
InParanoidi P28563.
KOi K04459.
OMAi SFNSSHI.
OrthoDBi EOG75MVWD.
PhylomeDBi P28563.
TreeFami TF105122.

Miscellaneous databases

NextBioi 296092.
PROi P28563.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28563.
Bgeei P28563.
CleanExi MM_DUSP1.
Genevestigatori P28563.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
PRINTSi PR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiDUS1_MOUSE
AccessioniPrimary (citable) accession number: P28563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 3, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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