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Protein

Dual specificity protein phosphatase 1

Gene

DUSP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei258 – 2581Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Stress response

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
SABIO-RKP28562.
SignaLinkiP28562.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 1 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity protein phosphatase hVH1
Mitogen-activated protein kinase phosphatase 1
Short name:
MAP kinase phosphatase 1
Short name:
MKP-1
Protein-tyrosine phosphatase CL100
Gene namesi
Name:DUSP1
Synonyms:CL100, MKP1, PTPN10, VH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3064. DUSP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27519.

Polymorphism and mutation databases

BioMutaiDUSP1.
DMDMi1346900.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Dual specificity protein phosphatase 1PRO_0000094790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei359 – 3591Phosphoserine; by MAPK1 and MAPK3By similarity
Modified residuei364 – 3641Phosphoserine; by MAPK1 and MAPK3By 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

MaxQBiP28562.
PaxDbiP28562.
PRIDEiP28562.

PTM databases

DEPODiP28562.
PhosphoSiteiP28562.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

By oxidative stress and heat shock.

Gene expression databases

BgeeiP28562.
CleanExiHS_DUSP1.
GenevisibleiP28562. HS.

Organism-specific databases

HPAiCAB018554.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284826EBI-975493,EBI-959949
MAPK14Q165394EBI-975493,EBI-73946
MAPK3P273615EBI-975493,EBI-73995
SKP2Q133093EBI-975493,EBI-456291
UBBP0CG472EBI-975493,EBI-413034

Protein-protein interaction databases

BioGridi108176. 17 interactions.
IntActiP28562. 15 interactions.
MINTiMINT-8217028.
STRINGi9606.ENSP00000239223.

Structurei

3D structure databases

ProteinModelPortaliP28562.
SMRiP28562. Positions 13-136, 172-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiP28562.
KOiK04459.
OMAiSFNSSHI.
OrthoDBiEOG75MVWD.
PhylomeDBiP28562.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
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.
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.

P28562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMEVGTLDA GGLRALLGER AAQCLLLDCR SFFAFNAGHI AGSVNVRFST
60 70 80 90 100
IVRRRAKGAM GLEHIVPNAE LRGRLLAGAY HAVVLLDERS AALDGAKRDG
110 120 130 140 150
TLALAAGALC REARAAQVFF LKGGYEAFSA SCPELCSKQS TPMGLSLPLS
160 170 180 190 200
TSVPDSAESG CSSCSTPLYD QGGPVEILPF LYLGSAYHAS RKDMLDALGI
210 220 230 240 250
TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA IDFIDSIKNA
260 270 280 290 300
GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS
310 320 330 340 350
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHST
360
NSALSYLQSP ITTSPSC
Length:367
Mass (Da):39,298
Last modified:February 1, 1996 - v3
Checksum:i11BD1D39A9FCD51F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561A → T.1 Publication
Corresponds to variant rs34013988 [ dbSNP | Ensembl ].
VAR_025201
Natural varianti187 – 1871Y → H.1 Publication
Corresponds to variant rs34471628 [ dbSNP | Ensembl ].
VAR_025202

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68277 mRNA. Translation: CAA48338.1.
DQ301957 Genomic DNA. Translation: ABB96250.1.
CH471062 Genomic DNA. Translation: EAW61425.1.
CH471062 Genomic DNA. Translation: EAW61426.1.
BC022463 mRNA. Translation: AAH22463.1.
CCDSiCCDS4380.1.
PIRiS29090.
RefSeqiNP_004408.1. NM_004417.3.
UniGeneiHs.171695.

Genome annotation databases

EnsembliENST00000239223; ENSP00000239223; ENSG00000120129.
GeneIDi1843.
KEGGihsa:1843.
UCSCiuc003mbv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68277 mRNA. Translation: CAA48338.1.
DQ301957 Genomic DNA. Translation: ABB96250.1.
CH471062 Genomic DNA. Translation: EAW61425.1.
CH471062 Genomic DNA. Translation: EAW61426.1.
BC022463 mRNA. Translation: AAH22463.1.
CCDSiCCDS4380.1.
PIRiS29090.
RefSeqiNP_004408.1. NM_004417.3.
UniGeneiHs.171695.

3D structure databases

ProteinModelPortaliP28562.
SMRiP28562. Positions 13-136, 172-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108176. 17 interactions.
IntActiP28562. 15 interactions.
MINTiMINT-8217028.
STRINGi9606.ENSP00000239223.

Chemistry

BindingDBiP28562.
ChEMBLiCHEMBL6026.

PTM databases

DEPODiP28562.
PhosphoSiteiP28562.

Polymorphism and mutation databases

BioMutaiDUSP1.
DMDMi1346900.

Proteomic databases

MaxQBiP28562.
PaxDbiP28562.
PRIDEiP28562.

Protocols and materials databases

DNASUi1843.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000239223; ENSP00000239223; ENSG00000120129.
GeneIDi1843.
KEGGihsa:1843.
UCSCiuc003mbv.2. human.

Organism-specific databases

CTDi1843.
GeneCardsiGC05M172195.
HGNCiHGNC:3064. DUSP1.
HPAiCAB018554.
MIMi600714. gene.
neXtProtiNX_P28562.
PharmGKBiPA27519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiP28562.
KOiK04459.
OMAiSFNSSHI.
OrthoDBiEOG75MVWD.
PhylomeDBiP28562.
TreeFamiTF105122.

Enzyme and pathway databases

BRENDAi3.1.3.16. 2681.
SABIO-RKP28562.
SignaLinkiP28562.

Miscellaneous databases

ChiTaRSiDUSP1. human.
GeneWikiiDUSP1.
GenomeRNAii1843.
NextBioi7547.
PROiP28562.
SOURCEiSearch...

Gene expression databases

BgeeiP28562.
CleanExiHS_DUSP1.
GenevisibleiP28562. HS.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase."
    Keyes S.M., Emslie E.A.
    Nature 359:644-647(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Foreskin.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-56 AND HIS-187.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDUS1_HUMAN
AccessioniPrimary (citable) accession number: P28562
Secondary accession number(s): D3DQL9, Q2V508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.