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Q64623

- DUS1_RAT

UniProt

Q64623 - DUS1_RAT

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Protein
Dual specificity protein phosphatase 1
Gene
Dusp1, Cl100, Mkp1, Ptpn16
Organism
Rattus norvegicus (Rat)
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 By similarity.

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 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular response to hormone stimulus Source: RGD
  2. endoderm formation Source: RefGenome
  3. inactivation of MAPK activity Source: UniProtKB
  4. intracellular signal transduction Source: RGD
  5. mitotic cell cycle arrest Source: UniProtKB
  6. negative regulation of DNA biosynthetic process Source: RGD
  7. negative regulation of ERK1 and ERK2 cascade Source: RGD
  8. negative regulation of MAP kinase activity Source: UniProtKB
  9. negative regulation of MAPK cascade Source: UniProtKB
  10. negative regulation of apoptotic process Source: RGD
  11. negative regulation of meiotic cell cycle Source: UniProtKB
  12. peptidyl-threonine dephosphorylation Source: UniProtKB
  13. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  14. positive regulation of apoptotic process Source: RGD
  15. protein dephosphorylation Source: RGD
  16. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  17. response to cAMP Source: RGD
  18. response to calcium ion Source: RGD
  19. response to estradiol Source: RGD
  20. response to glucocorticoid Source: RGD
  21. response to hydrogen peroxide Source: RGD
  22. response to light stimulus Source: RGD
  23. response to organic substance Source: RGD
  24. response to retinoic acid Source: RGD
  25. response to testosterone Source: RGD
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 CL100
Protein-tyrosine phosphatase non-receptor type 16
Gene namesi
Name:Dusp1
Synonyms:Cl100, Mkp1, Ptpn16
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi620897. Dusp1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Dual specificity protein phosphatase 1
PRO_0000094792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591Phosphoserine; by MAPK1 and MAPK3 By similarity
Modified residuei364 – 3641Phosphoserine; by MAPK1 and MAPK3 By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ64623.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

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.2 Publications

Gene expression databases

GenevestigatoriQ64623.

Interactioni

Protein-protein interaction databases

BioGridi250421. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ64623.
SMRiQ64623. Positions 171-313.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 137118Rhodanese
Add
BLAST
Domaini175 – 367193Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00700000104321.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ64623.
KOiK04459.
OMAiSFNSSHI.
OrthoDBiEOG75MVWD.
PhylomeDBiQ64623.
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.

Q64623-1 [UniParc]FASTAAdd to Basket

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MVMEVGILDA GGLRALLRER AAQCLLLDCR SFFAFNAGHI VGSVNVRFST    50
IVRRRAKGAM GLEHIVPNTE LRGRLLAGAY HAVVLLDERS AALDGAKRDG 100
TLALAAGALC REARSTQVFF LQGGYEAFSA SCPELCSKQS TPMGLSLPLS 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
NSALNYLQSP ITTSPSC 367
Length:367
Mass (Da):39,541
Last modified:November 1, 1996 - v1
Checksum:i5112ADF290499139
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84004 mRNA. Translation: CAA58828.1.
AF357203 Genomic DNA. Translation: AAK55327.1.
PIRiS52265.
RefSeqiNP_446221.2. NM_053769.3.
UniGeneiRn.98260.

Genome annotation databases

EnsembliENSRNOT00000005383; ENSRNOP00000005383; ENSRNOG00000003977.
GeneIDi114856.
KEGGirno:114856.
UCSCiRGD:620897. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84004 mRNA. Translation: CAA58828.1 .
AF357203 Genomic DNA. Translation: AAK55327.1 .
PIRi S52265.
RefSeqi NP_446221.2. NM_053769.3.
UniGenei Rn.98260.

3D structure databases

ProteinModelPortali Q64623.
SMRi Q64623. Positions 171-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250421. 1 interaction.

Proteomic databases

PRIDEi Q64623.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000005383 ; ENSRNOP00000005383 ; ENSRNOG00000003977 .
GeneIDi 114856.
KEGGi rno:114856.
UCSCi RGD:620897. rat.

Organism-specific databases

CTDi 1843.
RGDi 620897. Dusp1.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00700000104321.
HOGENOMi HOG000294080.
HOVERGENi HBG007347.
InParanoidi Q64623.
KOi K04459.
OMAi SFNSSHI.
OrthoDBi EOG75MVWD.
PhylomeDBi Q64623.
TreeFami TF105122.

Miscellaneous databases

NextBioi 618903.
PROi Q64623.

Gene expression databases

Genevestigatori Q64623.

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

  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. Cited for: TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiDUS1_RAT
AccessioniPrimary (citable) accession number: Q64623
Secondary accession number(s): Q548G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 118 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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