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O54838 (DUS5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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 5

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
MAP-kinase phosphatase CPG21
Gene names
Name:Dusp5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This protein shows both activity toward tyrosine-protein phosphate as well as with serine/threonine-protein phosphate By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subcellular location

Nucleus 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 – 384384Dual specificity protein phosphatase 5
PRO_0000094803

Regions

Domain19 – 141123Rhodanese
Domain180 – 384205Tyrosine-protein phosphatase
Motif53 – 7422Nuclear localization signal Potential
Compositional bias79 – 824Poly-Gly

Sites

Active site2631Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O54838 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 5644069B8D348700

FASTA38442,094
        10         20         30         40         50         60 
MKVTSLDGRR LRKMLRKEAE ARCVVLDCRP YLAFAASSVR GSLNVNLNSV VLRRARGGAV 

        70         80         90        100        110        120 
SARYVLADEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR EESAARVVLT SLLACLSAGP 

       130        140        150        160        170        180 
RVYFLKGGYE TFYSQYPECC VDAKPISQEK LEGERGLLSQ CGKPILSVAY RPAYDQGGPV 

       190        200        210        220        230        240 
EILPFLYLGS AYHASKCEFL ANLHITALLN VSRRTSEACT THLHYKWIPV EDSHTADISS 

       250        260        270        280        290        300 
HFQEAIDFID CVREEGGKVL VHCEAGVSRS PTICMAYLMK TKQFRLKEAF EYIKQRRSVV 

       310        320        330        340        350        360 
SPNFGFMGQL LQYESEILPS TPTPQPPSCQ GEAASSTFIG HLQTLSPDMQ GAYCTFPTSV 

       370        380 
LAPVPTHATV AELHRSPVAT ATSC 

« Hide

References

[1]"Hippocampal plasticity involves extensive gene induction and multiple cellular mechanisms."
Hevroni D., Rattner A., Bundman M., Lederfein D., Gabarah A., Mangelus M., Silverman M.A., Kedar H., Naor C., Kornuc M., Hanoch T., Seger R., Theill L.E., Nedivi E., Richter-Levin G., Citri Y.
J. Mol. Neurosci. 10:75-98(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF013144 mRNA. Translation: AAB94858.1.
RefSeqNP_598262.1. NM_133578.1.
UniGeneRn.10877.

3D structure databases

ProteinModelPortalO54838.
SMRO54838. Positions 178-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000018889.

PTM databases

PhosphoSiteO54838.

Proteomic databases

PRIDEO54838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID171109.
KEGGrno:171109.

Organism-specific databases

CTD1847.
RGD620854. Dusp5.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidO54838.
KOK04459.
PhylomeDBO54838.

Gene expression databases

GenevestigatorO54838.

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

NextBio621812.
PROO54838.

Entry information

Entry nameDUS5_RAT
AccessionPrimary (citable) accession number: O54838
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 102 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