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Protein

Dual specificity protein phosphatase 2

Gene

DUSP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.

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)DescriptionActionsGraphical viewLength
Active sitei257Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

  • MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  • protein tyrosine/threonine phosphatase activity Source: ProtInc
  • protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  • endoderm formation Source: GO_Central
  • inactivation of MAPK activity Source: ProtInc
  • protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS08264-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ05923.
SIGNORiQ05923.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 2 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity protein phosphatase PAC-1
Gene namesi
Name:DUSP2
Synonyms:PAC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3068. DUSP2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1844.
OpenTargetsiENSG00000158050.
PharmGKBiPA27525.

Chemistry databases

ChEMBLiCHEMBL2157858.

Polymorphism and mutation databases

BioMutaiDUSP2.
DMDMi464334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000947931 – 314Dual specificity protein phosphatase 2Add BLAST314

Proteomic databases

EPDiQ05923.
PaxDbiQ05923.
PeptideAtlasiQ05923.
PRIDEiQ05923.

PTM databases

DEPODiQ05923.
iPTMnetiQ05923.
PhosphoSitePlusiQ05923.

Expressioni

Tissue specificityi

Expressed in hematopoietic tissues.

Inductioni

By mitogens.

Gene expression databases

BgeeiENSG00000158050.
CleanExiHS_DUSP2.
GenevisibleiQ05923. HS.

Organism-specific databases

HPAiHPA071920.

Interactioni

Protein-protein interaction databases

BioGridi108177. 1 interactor.
IntActiQ05923. 2 interactors.
MINTiMINT-8214530.
STRINGi9606.ENSP00000288943.

Chemistry databases

BindingDBiQ05923.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi174 – 176Combined sources3
Turni177 – 179Combined sources3
Beta strandi180 – 182Combined sources3
Helixi188 – 197Combined sources10
Beta strandi200 – 204Combined sources5
Beta strandi206 – 213Combined sources8
Beta strandi215 – 221Combined sources7
Helixi236 – 248Combined sources13
Beta strandi253 – 255Combined sources3
Beta strandi258 – 262Combined sources5
Helixi263 – 274Combined sources12
Helixi279 – 287Combined sources9
Helixi305 – 311Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M3GNMR-A170-314[»]
ProteinModelPortaliQ05923.
SMRiQ05923.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 144RhodanesePROSITE-ProRule annotationAdd BLAST122
Domaini237 – 302Tyrosine-protein phosphataseAdd BLAST66

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ05923.
KOiK04459.
OMAiCLAYLMQ.
OrthoDBiEOG091G0249.
PhylomeDBiQ05923.
TreeFamiTF105122.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00404. PTPc_motif. 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.

Q05923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP
60 70 80 90 100
WNALLRRRAR GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE
110 120 130 140 150
LRPDSPAHVL LAALLHETRA GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA
160 170 180 190 200
LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL FLGSCSHSSD LQGLQACGIT
210 220 230 240 250
AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI GFIDWVKNSG
260 270 280 290 300
GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF
310
MGQLLQFETQ VLCH
Length:314
Mass (Da):34,400
Last modified:February 1, 1994 - v1
Checksum:iFDD3543C6DE10CA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11329 mRNA. Translation: AAA50779.1.
U23853 Genomic DNA. Translation: AAA86112.1.
AC012307 Genomic DNA. Translation: AAY24222.1.
CH471207 Genomic DNA. Translation: EAW71385.1.
BC007771 mRNA. Translation: AAH07771.1.
CCDSiCCDS2016.1.
PIRiA57126.
RefSeqiNP_004409.1. NM_004418.3.
UniGeneiHs.1183.

Genome annotation databases

EnsembliENST00000288943; ENSP00000288943; ENSG00000158050.
GeneIDi1844.
KEGGihsa:1844.
UCSCiuc002svk.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11329 mRNA. Translation: AAA50779.1.
U23853 Genomic DNA. Translation: AAA86112.1.
AC012307 Genomic DNA. Translation: AAY24222.1.
CH471207 Genomic DNA. Translation: EAW71385.1.
BC007771 mRNA. Translation: AAH07771.1.
CCDSiCCDS2016.1.
PIRiA57126.
RefSeqiNP_004409.1. NM_004418.3.
UniGeneiHs.1183.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M3GNMR-A170-314[»]
ProteinModelPortaliQ05923.
SMRiQ05923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108177. 1 interactor.
IntActiQ05923. 2 interactors.
MINTiMINT-8214530.
STRINGi9606.ENSP00000288943.

Chemistry databases

BindingDBiQ05923.
ChEMBLiCHEMBL2157858.

PTM databases

DEPODiQ05923.
iPTMnetiQ05923.
PhosphoSitePlusiQ05923.

Polymorphism and mutation databases

BioMutaiDUSP2.
DMDMi464334.

Proteomic databases

EPDiQ05923.
PaxDbiQ05923.
PeptideAtlasiQ05923.
PRIDEiQ05923.

Protocols and materials databases

DNASUi1844.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288943; ENSP00000288943; ENSG00000158050.
GeneIDi1844.
KEGGihsa:1844.
UCSCiuc002svk.5. human.

Organism-specific databases

CTDi1844.
DisGeNETi1844.
GeneCardsiDUSP2.
HGNCiHGNC:3068. DUSP2.
HPAiHPA071920.
MIMi603068. gene.
neXtProtiNX_Q05923.
OpenTargetsiENSG00000158050.
PharmGKBiPA27525.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1716. Eukaryota.
COG2453. LUCA.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ05923.
KOiK04459.
OMAiCLAYLMQ.
OrthoDBiEOG091G0249.
PhylomeDBiQ05923.
TreeFamiTF105122.

Enzyme and pathway databases

BioCyciZFISH:HS08264-MONOMER.
BRENDAi3.1.3.16. 2681.
ReactomeiR-HSA-112409. RAF-independent MAPK1/3 activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
SignaLinkiQ05923.
SIGNORiQ05923.

Miscellaneous databases

EvolutionaryTraceiQ05923.
GeneWikiiDUSP2.
GenomeRNAii1844.
PROiQ05923.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158050.
CleanExiHS_DUSP2.
GenevisibleiQ05923. HS.

Family and domain databases

CDDicd00127. DSPc. 1 hit.
Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00404. PTPc_motif. 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...

Entry informationi

Entry nameiDUS2_HUMAN
AccessioniPrimary (citable) accession number: Q05923
Secondary accession number(s): Q53T45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 30, 2016
This is version 168 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.