Dual specificity protein phosphatase 6 - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

Q64346 (DUS6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 6
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Mitogen-activated protein kinase phosphatase 3
Short name=MAP kinase phosphatase 3
Short name=MKP-3

Gene names

Name:	Dusp6
Synonyms:	Mkp3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inactivates MAP kinases. Has a specificity for the ERK family. Implicated in muscle and neuronal differentiation.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate. A phosphoprotein + H₂O = a protein + phosphate.
Subcellular location	Cytoplasm.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from expression pattern Ref.2. Source: RGD dorsal/ventral pattern formation Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of ERK1 and ERK2 cascade Inferred from direct assay Ref.1. Source: RGD positive regulation of apoptotic process Inferred from Biological aspect of Ancestor. Source: RefGenome protein dephosphorylation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of endodermal cell fate specification Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of fibroblast growth factor receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of heart growth Inferred from Biological aspect of Ancestor. Source: RefGenome response to drug Inferred from expression pattern PubMed 11701771 PubMed 16799812 PubMed 18958736. Source: RGD response to growth factor stimulus Inferred from expression pattern PubMed 9559664. Source: RGD response to nitrosative stress Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from expression pattern PubMed 17881770. Source: RGD
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 381

381

Dual specificity protein phosphatase 6

PRO_0000094806

Regions

Domain

30 – 148

119

Rhodanese

Domain

206 – 381

176

Tyrosine-protein phosphatase

Sites

Active site

293

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

331

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q64346 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C511E00CB68F2888
Show »

FASTA

381

42,319

        10         20         30         40         50         60 
MIDTLRPVPF ASEMAISKTV AWLNEQLELG NEQLLLMDCR PQELYESSHI ESAINVAIPG 

        70         80         90        100        110        120 
IMLRRLQKGN LPVRALFTRC EDRDRFTRRC GTDTVVLYDE NSSDWNENTG GESVLGLLLK 

       130        140        150        160        170        180 
KLKDEGCRAF YLEGGFSKFQ AEFALHCETN LDGSCSSSSP PLPVLGLGGL RISSDSSSDI 

       190        200        210        220        230        240 
ESDLDRDPNS ATDSDGSPLS NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT 

       250        260        270        280        290        300 
PNLPNLFENA GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS 

       310        320        330        340        350        360 
VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS SPCDNRVPAQ 

       370        380 
QLYFTAPSNQ NVYQVDSLQS T

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase." Muda M., Boschert U., Dickinson R., Martinou J.-C., Martinou I., Camps M., Schlegel W., Arkinstall S. J. Biol. Chem. 271:4319-4326(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Neuron.
[2]	"A novel cytoplasmic dual specificity protein tyrosine phosphatase implicated in muscle and neuronal differentiation." Mourey R.J., Vega Q.C., Campbell J.S., Wenderoth M.P., Hauschka S.D., Krebs E.G., Dixon J.E. J. Biol. Chem. 271:3795-3802(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X94185 mRNA. Translation: CAA63895.1.
U42627 mRNA. Translation: AAB06202.1.
BC087003 mRNA. Translation: AAH87003.1.

IPI

IPI00211712.

RefSeq

NP_446335.1. NM_053883.2.

UniGene

Rn.4313.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FYS	X-ray	2.50	C/D	60-76	[»]

ProteinModelPortal

Q64346.

SMR

Q64346. Positions 1-154, 205-347.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000032969.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000037844; ENSRNOP00000032969; ENSRNOG00000023896.

GeneID

116663.

KEGG

rno:116663.

UCSC

RGD:70978. rat.

Organism-specific databases

CTD

1848.

RGD

70978. Dusp6.

Phylogenomic databases

eggNOG

COG2453.

GeneTree

ENSGT00700000104093.

HOGENOM

HOG000294079.

HOVERGEN

HBG007347.

K04459.

OrthoDB

EOG4GB76F.

Gene expression databases

Genevestigator

Q64346.

GermOnline

ENSRNOG00000023896. Rattus norvegicus.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PIRSF

PIRSF000939. MAPK_Ptase. 1 hit.

PRINTS

PR01764. MAPKPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q64346.

ChEMBL

CHEMBL5511.

EvolutionaryTrace

Q64346.

NextBio

619455.

Entry information

Entry name

DUS6_RAT

Accession

Primary (citable) accession number: Q64346

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents