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Q9DBB1 (DUS6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inactivates MAP kinases. Has a specificity for the ERK family By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Subcellular location

Cytoplasm 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.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: Compara

dorsal/ventral pattern formation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of ERK1 and ERK2 cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein dephosphorylation

Inferred from direct assay PubMed 15284227. Source: MGI

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 mutant phenotype PubMed 18753132. Source: MGI

response to drug

Inferred from electronic annotation. Source: Compara

response to growth factor stimulus

Inferred from electronic annotation. Source: Compara

response to nitrosative stress

Inferred from electronic annotation. Source: Compara

response to organic cyclic compound

Inferred from electronic annotation. Source: Compara

   Cellular_componentcytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionMAP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Dual specificity protein phosphatase 6
PRO_0000094805

Regions

Domain30 – 148119Rhodanese
Domain206 – 381176Tyrosine-protein phosphatase

Sites

Active site2931Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue3311Phosphoserine Ref.3

Experimental info

Sequence conflict221W → G in BAB26093. Ref.1
Sequence conflict341L → F in BAB26093. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9DBB1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7EA1FB154F4AD2DA

FASTA38142,408
        10         20         30         40         50         60 
MIDTLRPVPF ASEMAICKTV SWLNEQLELG NERLLLMDCR 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 SPCDNRVPTP 

       370        380 
QLYFTTPSNQ NVYQVDSLQS T

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Liver, Thymus and Tongue.
[2]"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].
[3]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK005062 mRNA. Translation: BAB23786.1.
AK009131 mRNA. Translation: BAB26093.1.
AK088468 mRNA. Translation: BAC40372.1.
AK088665 mRNA. Translation: BAC40489.1.
AK159146 mRNA. Translation: BAE34853.1.
AK159502 mRNA. Translation: BAE35135.1.
AK159900 mRNA. Translation: BAE35465.1.
BC003869 mRNA. Translation: AAH03869.1.
IPIIPI00986290.
RefSeqNP_080544.1. NM_026268.3.
UniGeneMm.1791.

3D structure databases

ProteinModelPortalQ9DBB1.
SMRQ9DBB1. Positions 1-154, 205-347.
ModBaseSearch...

PTM databases

PhosphoSiteQ9DBB1.

Proteomic databases

PaxDbQ9DBB1.
PRIDEQ9DBB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020118; ENSMUSP00000020118; ENSMUSG00000019960.
GeneID67603.
KEGGmmu:67603.
UCSCuc007gxk.2. mouse.

Organism-specific databases

CTD1848.
MGIMGI:1914853. Dusp6.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00700000104093.
HOVERGENHBG007347.
InParanoidQ9DBB1.
KOK04459.
OMAVFQLDPL.
OrthoDBEOG4GB76F.

Gene expression databases

BgeeQ9DBB1.
CleanExMM_DUSP6.
GenevestigatorQ9DBB1.
GermOnlineENSMUSG00000019960. Mus musculus.

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.
[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. Rhodanese-like. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP6. mouse.
NextBio325017.
SOURCESearch...

Entry information

Entry nameDUS6_MOUSE
AccessionPrimary (citable) accession number: Q9DBB1
Secondary accession number(s): Q542I5, Q9D7L4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents