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Q9D9D8 (DUS21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 phosphatase 21

EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:Dusp21
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.5

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.5

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.5.

Tissue specificity

Selectively expressed in testis. Ref.5

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-tyrosine dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein localization to organelle

Inferred from sequence or structural similarity Ref.5. Source: MGI

protein targeting to membrane

Inferred from sequence or structural similarity Ref.5. Source: MGI

protein targeting to mitochondrion

Inferred from sequence or structural similarity Ref.5. Source: MGI

   Cellular_componentextrinsic component of membrane

Inferred from sequence or structural similarity Ref.5. Source: MGI

integral component of mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from sequence or structural similarity Ref.5. Source: MGI

mitochondrial intermembrane space

Inferred from sequence or structural similarity Ref.5. Source: MGI

mitochondrion

Inferred from sequence or structural similarity Ref.5. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

phosphatase activity

Inferred from sequence or structural similarity Ref.5. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Dual specificity phosphatase 21
PRO_0000411986

Regions

Domain21 – 161141Tyrosine-protein phosphatase
Region43 – 12886Sufficient for mitochondrial localization

Sites

Active site1051Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D9D8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8EE2F7151BB5CBFA

FASTA18921,509
        10         20         30         40         50         60 
MTTASCIFPS QATQQDNIYG LSQITASLFI SNSAVANDKL TLSNNHITTI INVSAEVVNT 

        70         80         90        100        110        120 
FFEDIQYVQV PVSDAPNSYL YDFFDPIADH IHGVEMRNGR TLLHCAAGVS RSATLCLAYL 

       130        140        150        160        170        180 
MKYHNMTLLD AHTWTKTCRP IIRPNNGFWE QLIHYEFKLF SRNTVRMIYS PIGLIPNIYE 


KEAYLMELM 

« Hide

References

« Hide 'large scale' 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.
Tissue: Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Testis.
[5]"Dual specificity phosphatases 18 and 21 target to opposing sides of the mitochondrial inner membrane."
Rardin M.J., Wiley S.E., Murphy A.N., Pagliarini D.J., Dixon J.E.
J. Biol. Chem. 283:15440-15450(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK007061 mRNA. Translation: BAB24847.1.
AL773547 Genomic DNA. Translation: CAM18407.1.
CH466584 Genomic DNA. Translation: EDL35726.1.
BC048605 mRNA. Translation: AAH48605.1.
CCDSCCDS30036.1.
RefSeqNP_082844.1. NM_028568.1.
UniGeneMm.159027.

3D structure databases

ProteinModelPortalQ9D9D8.
SMRQ9D9D8. Positions 20-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000026018.

Proteomic databases

PRIDEQ9D9D8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026018; ENSMUSP00000026018; ENSMUSG00000025043.
GeneID73547.
KEGGmmu:73547.
UCSCuc009ssi.1. mouse.

Organism-specific databases

CTD63904.
MGIMGI:1920797. Dusp21.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117525.
HOGENOMHOG000233766.
HOVERGENHBG051422.
InParanoidQ9D9D8.
KOK14165.
OMAFWEQLIN.
OrthoDBEOG7PK90H.
TreeFamTF316009.

Gene expression databases

BgeeQ9D9D8.
GenevestigatorQ9D9D8.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
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]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio338510.
PROQ9D9D8.
SOURCESearch...

Entry information

Entry nameDUS21_MOUSE
AccessionPrimary (citable) accession number: Q9D9D8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 105 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

MGD cross-references

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