Dual specificity protein phosphatase 1

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P28562 (DUS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

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):
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 names

Name:	DUSP1
Synonyms:	CL100, MKP1, PTPN10, VH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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'.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate. A phosphoprotein + H₂O = a protein + phosphate.
Tissue specificity	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. Ref.2
Induction	By oxidative stress and heat shock.
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 Stress response
Coding sequence diversity	Polymorphism
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 endoderm formation Inferred from Biological aspect of Ancestor. Source: RefGenome inactivation of MAPK activity Inferred from Biological aspect of Ancestor. Source: RefGenome
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 non-membrane spanning protein tyrosine phosphatase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
MAPK1	P28482	3	EBI-975493,EBI-959949
SKP2	Q13309	3	EBI-975493,EBI-456291
UBB	P0CG47	2	EBI-975493,EBI-413034

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_0000094790

Regions

Domain

20 – 137

118

Rhodanese

Domain

175 – 367

193

Tyrosine-protein phosphatase

Sites

Active site

258

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

359

Phosphoserine; by MAPK1 and MAPK3 By similarity

Modified residue

364

Phosphoserine; by MAPK1 and MAPK3 By similarity

Natural variations

Natural variant

A → T. Ref.3
Corresponds to variant rs34013988 [ dbSNP | Ensembl ].

VAR_025201

Natural variant

187

Y → H. Ref.3
Corresponds to variant rs34471628 [ dbSNP | Ensembl ].

VAR_025202

Sequences

Sequence

Length

Mass (Da)

Tools

P28562 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 11BD1D39A9FCD51F
Show »

FASTA

367

39,298

        10         20         30         40         50         60 
MVMEVGTLDA GGLRALLGER AAQCLLLDCR SFFAFNAGHI AGSVNVRFST IVRRRAKGAM 

        70         80         90        100        110        120 
GLEHIVPNAE LRGRLLAGAY HAVVLLDERS AALDGAKRDG TLALAAGALC REARAAQVFF 

       130        140        150        160        170        180 
LKGGYEAFSA SCPELCSKQS TPMGLSLPLS TSVPDSAESG CSSCSTPLYD QGGPVEILPF 

       190        200        210        220        230        240 
LYLGSAYHAS RKDMLDALGI TALINVSANC PNHFEGHYQY KSIPVEDNHK ADISSWFNEA 

       250        260        270        280        290        300 
IDFIDSIKNA GGRVFVHCQA GISRSATICL AYLMRTNRVK LDEAFEFVKQ RRSIISPNFS 

       310        320        330        340        350        360 
FMGQLLQFES QVLAPHCSAE AGSPAMAVLD RGTSTTTVFN FPVSIPVHST NSALSYLQSP 


ITTSPSC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1406996] [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: 8106404] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00003928.
PIR	S29090.
RefSeq	NP_004408.1. NM_004417.3.
UniGene	Hs.171695.
3D structure databases
ProteinModelPortal	P28562.
SMR	P28562. Positions 6-140, 172-314.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28562. 10 interactions.
STRING	P28562.
PTM databases
PhosphoSite	P28562.
Polymorphism databases
DMDM	1346900.
Proteomic databases
PRIDE	P28562.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000239223; ENSP00000239223; ENSG00000120129.
GeneID	1843.
KEGG	hsa:1843.
UCSC	uc003mbv.1. human.
Organism-specific databases
CTD	1843.
GeneCards	GC05M172195.
H-InvDB	HIX0005420.
HGNC	HGNC:3064. DUSP1.
HPA	CAB018554.
MIM	600714. gene.
neXtProt	NX_P28562.
PharmGKB	PA27519.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10172.
GeneTree	ENSGT00600000084364.
HOGENOM	HBG713414.
HOVERGEN	HBG007347.
InParanoid	P28562.
OMA	VLDCRSF.
OrthoDB	EOG4T1HMT.
PhylomeDB	P28562.
Enzyme and pathway databases
Pathway_Interaction_DB	fcer1pathway. Fc-epsilon receptor I signaling in mast cells. p38alphabetapathway. Regulation of p38-alpha and p38-beta.
Gene expression databases
ArrayExpress	P28562.
Bgee	P28562.
CleanEx	HS_DUSP1.
Genevestigator	P28562.
GermOnline	ENSG00000120129. Homo sapiens.
Family and domain databases
InterPro	IPR020417. Dual-sp_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR014393. Dual_MAP_Kinase_Phosphatase. IPR008343. MAPK_phosph. IPR001763. Rhodanese-like. IPR000387. Tyr/Dual-specificity_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
Gene3D	G3DSA:3.40.250.10. Rhodanese-like. 1 hit.
KO	K04459.
Pfam	PF00782. DSPc. 1 hit. PF00581. Rhodanese. 1 hit. [Graphical view]
PIRSF	PIRSF000939. MAPK_Ptase. 1 hit.
PRINTS	PR01908. ADSPHPHTASE. 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	7547.
SOURCE	Search...

Entry information

Entry name

DUS1_HUMAN

Accession

Primary (citable) accession number: P28562
Secondary accession number(s): D3DQL9, Q2V508

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Relevant documents

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Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents