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Q05923

- DUS2_HUMAN

UniProt

Q05923 - DUS2_HUMAN

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Protein
Dual specificity protein phosphatase 2
Gene
DUSP2, PAC1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei257 – 2571Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. protein binding Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: ProtInc
  4. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  5. protein tyrosine/threonine phosphatase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. endoderm formation Source: RefGenome
  2. inactivation of MAPK activity Source: ProtInc
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ05923.

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3068. DUSP2.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Dual specificity protein phosphatase 2
PRO_0000094793Add
BLAST

Proteomic databases

PaxDbiQ05923.
PRIDEiQ05923.

PTM databases

PhosphoSiteiQ05923.

Expressioni

Tissue specificityi

Expressed in hematopoietic tissues.

Inductioni

By mitogens.

Gene expression databases

BgeeiQ05923.
CleanExiHS_DUSP2.
GenevestigatoriQ05923.

Interactioni

Protein-protein interaction databases

BioGridi108177. 2 interactions.
IntActiQ05923. 2 interactions.
MINTiMINT-8214530.
STRINGi9606.ENSP00000288943.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi174 – 1763
Turni177 – 1793
Beta strandi180 – 1823
Helixi188 – 19710
Beta strandi200 – 2045
Beta strandi206 – 2138
Beta strandi215 – 2217
Helixi236 – 24813
Beta strandi253 – 2553
Beta strandi258 – 2625
Helixi263 – 27412
Helixi279 – 2879
Helixi305 – 3117

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3GNMR-A170-314[»]
ProteinModelPortaliQ05923.
SMRiQ05923. Positions 25-143, 170-314.

Miscellaneous databases

EvolutionaryTraceiQ05923.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 144122Rhodanese
Add
BLAST
Domaini237 – 30266Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ05923.
KOiK04459.
OMAiCLAYLMQ.
OrthoDBiEOG75MVWD.
PhylomeDBiQ05923.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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.
PRINTSiPR01764. 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.

Q05923-1 [UniParc]FASTAAdd to Basket

« Hide

MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP    50
WNALLRRRAR GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE 100
LRPDSPAHVL LAALLHETRA GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA 150
LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL FLGSCSHSSD LQGLQACGIT 200
AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI GFIDWVKNSG 250
GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF 300
MGQLLQFETQ VLCH 314
Length:314
Mass (Da):34,400
Last modified:February 1, 1994 - v1
Checksum:iFDD3543C6DE10CA5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi464334.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2016.1.
PIRi A57126.
RefSeqi NP_004409.1. NM_004418.3.
UniGenei Hs.1183.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M3G NMR - A 170-314 [» ]
ProteinModelPortali Q05923.
SMRi Q05923. Positions 25-143, 170-314.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108177. 2 interactions.
IntActi Q05923. 2 interactions.
MINTi MINT-8214530.
STRINGi 9606.ENSP00000288943.

Chemistry

ChEMBLi CHEMBL2157858.

PTM databases

PhosphoSitei Q05923.

Polymorphism databases

DMDMi 464334.

Proteomic databases

PaxDbi Q05923.
PRIDEi Q05923.

Protocols and materials databases

DNASUi 1844.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288943 ; ENSP00000288943 ; ENSG00000158050 .
GeneIDi 1844.
KEGGi hsa:1844.
UCSCi uc002svk.4. human.

Organism-specific databases

CTDi 1844.
GeneCardsi GC02M096808.
HGNCi HGNC:3068. DUSP2.
MIMi 603068. gene.
neXtProti NX_Q05923.
PharmGKBi PA27525.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000294080.
HOVERGENi HBG007347.
InParanoidi Q05923.
KOi K04459.
OMAi CLAYLMQ.
OrthoDBi EOG75MVWD.
PhylomeDBi Q05923.
TreeFami TF105122.

Enzyme and pathway databases

SignaLinki Q05923.

Miscellaneous databases

EvolutionaryTracei Q05923.
GeneWikii DUSP2.
GenomeRNAii 1844.
NextBioi 7551.
PROi Q05923.
SOURCEi Search...

Gene expression databases

Bgeei Q05923.
CleanExi HS_DUSP2.
Genevestigatori Q05923.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi 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 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. "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase."
    Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., Siebenlist U., Kelly K.
    Science 259:1763-1766(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11."
    Yi H., Morton C.C., Weremowicz S., McBride O.W., Kelly K.
    Genomics 28:92-96(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: B-cell.
  6. "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP."
    Farooq A., Plotnikova O., Chaturvedi G., Yan S., Zeng L., Zhang Q., Zhou M.M.
    Structure 11:155-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 170-314.

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: July 9, 2014
This is version 145 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

External Data

Dasty 3

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