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Q62767 (DUS4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 4

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Mitogen-activated protein kinase phosphatase 2
Short name=MAP kinase phosphatase 2
Short name=MKP-2
Gene names
Name:Dusp4
Synonyms:Mkp2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed at moderate levels in nearly all tissues and cells including brain, spleen, and testes with the higher expression in the heart and lung and lower expression in skeletal muscle and kidney. Undetectable in liver. Expressed in many areas of the brain with very strong expression in the hippocampus, piriform cortex, and the suprachiasmatic nucleus.

Induction

By mitogens and by stress.

Post-translational modification

Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Dual specificity protein phosphatase 4
PRO_0000094800

Regions

Domain42 – 160119Rhodanese
Domain198 – 395198Tyrosine-protein phosphatase

Sites

Active site2811Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue3871Phosphoserine; by MAPK By similarity
Modified residue3921Phosphoserine; by MAPK By similarity

Sequences

Sequence LengthMass (Da)Tools
Q62767 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A90EFFD378A050FD

FASTA39543,187
        10         20         30         40         50         60 
MVTMEELREM DCSVLKRLMN RDENGGTAGS SGGSHGALGL LSGGKCLLLD CRPFLAHSAG 

        70         80         90        100        110        120 
YIRGSVNVRC NTIVRRRAKG SVSLEQILPA EEEVRARLRS GLYSAVIVYD ERSPRAESLR 

       130        140        150        160        170        180 
EDSTVSLVVQ ALRRNAERTD ICLLKGGYER FSSEYPEFCS KTKALAAIPP PVPPSTNESL 

       190        200        210        220        230        240 
DLGCSSCGTP LHDQGGPVEI LPFLYLGSAY HAARRDMLDA LGITALLNVS SDCPNHFEGH 

       250        260        270        280        290        300 
YQYKCIPVED NHKADISSWF MEAIEYIDAV KDCRGRVLVH CQAGISRSAT ICLAYLMMKK 

       310        320        330        340        350        360 
RVRLEEAFEF VKQRRSIISP NFSFMGQLLQ FESQVLTTSC AAEAASPSGP LRERGKATPT 

       370        380        390 
PTSQFVFSFP VSVGVHAAPS NLPYLHSPIT TSPSC 

« Hide

References

[1]"A novel mitogen-activated protein kinase phosphatase. Structure, expression, and regulation."
Misra-Press A., Rim C.S., Yao H., Roberson M.S., Stork P.J.S.
J. Biol. Chem. 270:14587-14596(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pheochromocytoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23438 mRNA. Translation: AAC52493.1.
RefSeqNP_071535.1. NM_022199.1.
UniGeneRn.44407.

3D structure databases

ProteinModelPortalQ62767.
SMRQ62767. Positions 194-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000016328.

PTM databases

PhosphoSiteQ62767.

Proteomic databases

PaxDbQ62767.
PRIDEQ62767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID60587.
KEGGrno:60587.

Organism-specific databases

CTD1846.
RGD620625. Dusp4.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidQ62767.
KOK04459.
PhylomeDBQ62767.

Gene expression databases

GenevestigatorQ62767.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 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]
SUPFAMSSF52821. SSF52821. 1 hit.
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

NextBio612322.
PROQ62767.

Entry information

Entry nameDUS4_RAT
AccessionPrimary (citable) accession number: Q62767
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families