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Protein

Dual specificity protein phosphatase 6

Gene

Dusp6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei293 – 2931Phosphocysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_299247. ERKs are inactivated.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Dusp6
Synonyms:Mkp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1914853. Dusp6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Dual specificity protein phosphatase 6PRO_0000094805Add
BLAST

Proteomic databases

MaxQBiQ9DBB1.
PaxDbiQ9DBB1.
PRIDEiQ9DBB1.

PTM databases

PhosphoSiteiQ9DBB1.

Expressioni

Gene expression databases

BgeeiQ9DBB1.
CleanExiMM_DUSP6.
GenevestigatoriQ9DBB1.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk1P630852EBI-7812384,EBI-397697

Protein-protein interaction databases

BioGridi212304. 1 interaction.
IntActiQ9DBB1. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9DBB1.
SMRiQ9DBB1. Positions 1-154, 205-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 148119RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini206 – 381176Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ9DBB1.
KOiK04459.
OMAiRDWNENT.
OrthoDBiEOG793B7W.
PhylomeDBiQ9DBB1.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDTLRPVPF ASEMAICKTV SWLNEQLELG NERLLLMDCR PQELYESSHI
60 70 80 90 100
ESAINVAIPG IMLRRLQKGN LPVRALFTRC EDRDRFTRRC GTDTVVLYDE
110 120 130 140 150
NSSDWNENTG GESVLGLLLK KLKDEGCRAF YLEGGFSKFQ AEFALHCETN
160 170 180 190 200
LDGSCSSSSP PLPVLGLGGL RISSDSSSDI ESDLDRDPNS ATDSDGSPLS
210 220 230 240 250
NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT PNLPNLFENA
260 270 280 290 300
GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS
310 320 330 340 350
VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS
360 370 380
SPCDNRVPTP QLYFTTPSNQ NVYQVDSLQS T
Length:381
Mass (Da):42,408
Last modified:June 1, 2001 - v1
Checksum:i7EA1FB154F4AD2DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221W → G in BAB26093 (PubMed:16141072).Curated
Sequence conflicti34 – 341L → F in BAB26093 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24147.1.
RefSeqiNP_080544.1. NM_026268.3.
UniGeneiMm.1791.

Genome annotation databases

EnsembliENSMUST00000020118; ENSMUSP00000020118; ENSMUSG00000019960.
GeneIDi67603.
KEGGimmu:67603.
UCSCiuc007gxk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24147.1.
RefSeqiNP_080544.1. NM_026268.3.
UniGeneiMm.1791.

3D structure databases

ProteinModelPortaliQ9DBB1.
SMRiQ9DBB1. Positions 1-154, 205-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212304. 1 interaction.
IntActiQ9DBB1. 1 interaction.

PTM databases

PhosphoSiteiQ9DBB1.

Proteomic databases

MaxQBiQ9DBB1.
PaxDbiQ9DBB1.
PRIDEiQ9DBB1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020118; ENSMUSP00000020118; ENSMUSG00000019960.
GeneIDi67603.
KEGGimmu:67603.
UCSCiuc007gxk.2. mouse.

Organism-specific databases

CTDi1848.
MGIiMGI:1914853. Dusp6.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOVERGENiHBG007347.
InParanoidiQ9DBB1.
KOiK04459.
OMAiRDWNENT.
OrthoDBiEOG793B7W.
PhylomeDBiQ9DBB1.
TreeFamiTF105122.

Enzyme and pathway databases

ReactomeiREACT_299247. ERKs are inactivated.

Miscellaneous databases

ChiTaRSiDusp6. mouse.
NextBioi325017.
PROiQ9DBB1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBB1.
CleanExiMM_DUSP6.
GenevestigatoriQ9DBB1.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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].

Entry informationi

Entry nameiDUS6_MOUSE
AccessioniPrimary (citable) accession number: Q9DBB1
Secondary accession number(s): Q542I5, Q9D7L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.