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Reviewed, UniProtKB/Swiss-Prot Q05923 (DUS2_HUMAN)

Last modified June 16, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dual specificity protein phosphatase 2
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    Dual specificity protein phosphatase PAC-1
Gene names
Name: DUSP2
Synonyms: PAC1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Subcellular location

Nucleus.

Tissue specificity

In hematopoietic tissues.

Induction

By mitogens.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Dual specificity protein phosphatase 2
PRO_0000094793

Regions

Domain23 – 144122Rhodanese
Domain237 – 30266Tyrosine-protein phosphatase

Sites

Active site2571Phosphocysteine intermediate By similarity

Secondary structure

........................ 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05923-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: FDD3543C6DE10CA5

FASTA31434,400
        10         20         30         40         50         60 
MGLEAARELE CAALGTLLRD PREAERTLLL DCRPFLAFCR RHVRAARPVP WNALLRRRAR 

        70         80         90        100        110        120 
GPPAAVLACL LPDRALRTRL VRGELARAVV LDEGSASVAE LRPDSPAHVL LAALLHETRA 

       130        140        150        160        170        180 
GPTAVYFLRG GFDGFQGCCP DLCSEAPAPA LPPTGDKTSR SDSRAPVYDQ GGPVEILPYL 

       190        200        210        220        230        240 
FLGSCSHSSD LQGLQACGIT AVLNVSASCP NHFEGLFRYK SIPVEDNQMV EISAWFQEAI 

       250        260        270        280        290        300 
GFIDWVKNSG GRVLVHCQAG ISRSATICLA YLMQSRRVRL DEAFDFVKQR RGVISPNFSF 

       310 
MGQLLQFETQ VLCH 

« Hide

References

« Hide 'large scale' references
[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: 7681221] [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: 7590752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: B-cell.
[4]"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: 12575935] [Abstract]
Cited for: STRUCTURE BY NMR OF 170-314.
+Additional computationally mapped references.

Cross-references

Sequence databases

L11329 mRNA. Translation: AAA50779.1.
U23853 Genomic DNA. Translation: AAA86112.1.
BC007771 mRNA. Translation: AAH07771.1.
IPIIPI00016729.
PIRA57126.
RefSeqNP_004409.1.
UniGeneHs.1183

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1M3GNMR-A170-314[»]
ModBaseSearch...

Proteomic databases

PRIDEQ05923.

Genome annotation databases

EnsemblENSG00000158050. Homo sapiens. [Contig view]
GeneID1844.
KEGGhsa:1844.

Organism-specific databases

GeneCardsGC02M096230.
H-InvDBHIX0002269.
HGNCHGNC:3068. DUSP2.
MIM603068. gene.
PharmGKBPA27525.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ05923.
HOVERGENQ05923.
OMAQ05923. NQMVEIS.

Enzyme and pathway databases

BRENDA3.1.3.16. 247.
3.1.3.48. 247.

Gene expression databases

ArrayExpressQ05923.
BgeeQ05923.
CleanExHS_DUSP2.
GermOnlineENSG00000158050. Homo sapiens.

Family and domain databases

InterProIPR014393. Dual_MAP_Kinase_Phosphatase.
IPR008343. MAPK_phosph.
IPR001763. Rhodanese-like.
IPR000387. Tyr_Pase.
IPR016130. Tyr_Pase_AS.
IPR000340. Tyr_Pase_dual_specific.
[Graphical view]
Gene3DG3DSA:3.40.250.10. Rhodanese-like. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSPR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio7551.
SOURCESearch...

Entry information

Entry nameDUS2_HUMAN
AccessionPrimary (citable) accession number: Q05923
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents