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Protein

Dual specificity protein phosphatase 26

Gene

Dusp26

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

Functioni

Inactivates MAPK1 and MAPK3 which leads to dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 26 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase SKRP3
Gene namesi
Name:Dusp26
Synonyms:Skrp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1914209. Dusp26.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Dual specificity protein phosphatase 26PRO_0000292220Add
BLAST

Proteomic databases

PRIDEiQ9D700.

Expressioni

Tissue specificityi

Brain and skeletal muscle. In the brain it is expressed ubiquitously except in the hippocampus.2 Publications

Gene expression databases

BgeeiQ9D700.
CleanExiMM_DUSP26.
GenevestigatoriQ9D700.

Interactioni

Subunit structurei

Interacts with HSF4.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9D700.
SMRiQ9D700. Positions 61-210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 206146Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233767.
HOVERGENiHBG001524.
InParanoidiQ9D700.
KOiK14165.
OMAiMAFMSRF.
OrthoDBiEOG7CZK7N.
PhylomeDBiQ9D700.
TreeFamiTF105128.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCPGNWLWAS MTFMARFSRG SSRSPVRTRG SLEEMPSVHH PFLNVFELER
60 70 80 90 100
LLYTGKTACN HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHNRWR
110 120 130 140 150
GTPEAYEGLG IRYLGVEAHD SPAFDMSIHF QTAADFIHRA LSQPGGKILV
160 170 180 190 200
HCAVGVSRSA TLVLAYLMLY HHFTLVEAIK KVKDHRGITP NRGFLRQLLA
210
LDRRLRQGLE A
Length:211
Mass (Da):23,946
Last modified:March 1, 2003 - v2
Checksum:i952A6C7561E9B046
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB104416 mRNA. Translation: BAD91016.1.
AK009781 mRNA. Translation: BAB26501.2.
BC018204 mRNA. Translation: AAH18204.1.
CCDSiCCDS22219.1.
RefSeqiNP_080145.1. NM_025869.3.
UniGeneiMm.23916.

Genome annotation databases

EnsembliENSMUST00000036631; ENSMUSP00000046794; ENSMUSG00000039661.
ENSMUST00000161713; ENSMUSP00000124949; ENSMUSG00000039661.
ENSMUST00000170204; ENSMUSP00000126397; ENSMUSG00000039661.
GeneIDi66959.
KEGGimmu:66959.
UCSCiuc009ljb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB104416 mRNA. Translation: BAD91016.1.
AK009781 mRNA. Translation: BAB26501.2.
BC018204 mRNA. Translation: AAH18204.1.
CCDSiCCDS22219.1.
RefSeqiNP_080145.1. NM_025869.3.
UniGeneiMm.23916.

3D structure databases

ProteinModelPortaliQ9D700.
SMRiQ9D700. Positions 61-210.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9D700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036631; ENSMUSP00000046794; ENSMUSG00000039661.
ENSMUST00000161713; ENSMUSP00000124949; ENSMUSG00000039661.
ENSMUST00000170204; ENSMUSP00000126397; ENSMUSG00000039661.
GeneIDi66959.
KEGGimmu:66959.
UCSCiuc009ljb.1. mouse.

Organism-specific databases

CTDi78986.
MGIiMGI:1914209. Dusp26.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233767.
HOVERGENiHBG001524.
InParanoidiQ9D700.
KOiK14165.
OMAiMAFMSRF.
OrthoDBiEOG7CZK7N.
PhylomeDBiQ9D700.
TreeFamiTF105128.

Miscellaneous databases

NextBioi323124.
PROiQ9D700.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D700.
CleanExiMM_DUSP26.
GenevestigatoriQ9D700.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020405. Atypical_DUSP_famA.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01909. ADSPHPHTASEA.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel dual specificity phosphatase, SKRP3."
    Zama T., Aoki R., Murata M., Ikeda Y.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.
    Tissue: Tongue.
  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: Mammary tumor.
  4. "Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
    Hu Y., Mivechi N.F.
    Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Characterization of a novel low-molecular-mass dual specificity phosphatase-4 (LDP-4) expressed in brain."
    Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M., Kikuchi K.
    Mol. Cell. Biochem. 296:177-184(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiDUS26_MOUSE
AccessioniPrimary (citable) accession number: Q9D700
Secondary accession number(s): Q8VCZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 1, 2003
Last modified: May 27, 2015
This is version 100 of the entry and version 2 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.