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Protein

Dual specificity phosphatase 21

Gene

Dusp21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • peptidyl-tyrosine dephosphorylation Source: GO_Central
  • protein localization to organelle Source: MGI
  • protein targeting to membrane Source: MGI
  • protein targeting to mitochondrion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity phosphatase 21 (EC:3.1.3.16, EC:3.1.3.48)
Gene namesi
Name:Dusp21
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1920797. Dusp21.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of membrane Source: MGI
  • extrinsic component of mitochondrial inner membrane Source: Ensembl
  • mitochondrial inner membrane Source: MGI
  • mitochondrial intermembrane space Source: MGI
  • mitochondrial matrix Source: Ensembl
  • mitochondrion Source: MGI
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Dual specificity phosphatase 21PRO_0000411986Add
BLAST

Proteomic databases

PRIDEiQ9D9D8.

Expressioni

Tissue specificityi

Selectively expressed in testis.1 Publication

Gene expression databases

BgeeiQ9D9D8.
GenevisibleiQ9D9D8. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026018.

Structurei

3D structure databases

ProteinModelPortaliQ9D9D8.
SMRiQ9D9D8. Positions 20-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 161141Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 12886Sufficient for mitochondrial localizationAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ9D9D8.
KOiK14165.
OMAiFWEQLIN.
OrthoDBiEOG7PK90H.
TreeFamiTF316009.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
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.

Q9D9D8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTASCIFPS QATQQDNIYG LSQITASLFI SNSAVANDKL TLSNNHITTI
60 70 80 90 100
INVSAEVVNT FFEDIQYVQV PVSDAPNSYL YDFFDPIADH IHGVEMRNGR
110 120 130 140 150
TLLHCAAGVS RSATLCLAYL MKYHNMTLLD AHTWTKTCRP IIRPNNGFWE
160 170 180
QLIHYEFKLF SRNTVRMIYS PIGLIPNIYE KEAYLMELM
Length:189
Mass (Da):21,509
Last modified:June 1, 2001 - v1
Checksum:i8EE2F7151BB5CBFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007061 mRNA. Translation: BAB24847.1.
AL773547 Genomic DNA. Translation: CAM18407.1.
CH466584 Genomic DNA. Translation: EDL35726.1.
BC048605 mRNA. Translation: AAH48605.1.
CCDSiCCDS30036.1.
RefSeqiNP_082844.1. NM_028568.1.
UniGeneiMm.159027.

Genome annotation databases

EnsembliENSMUST00000026018; ENSMUSP00000026018; ENSMUSG00000025043.
GeneIDi73547.
KEGGimmu:73547.
UCSCiuc009ssi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007061 mRNA. Translation: BAB24847.1.
AL773547 Genomic DNA. Translation: CAM18407.1.
CH466584 Genomic DNA. Translation: EDL35726.1.
BC048605 mRNA. Translation: AAH48605.1.
CCDSiCCDS30036.1.
RefSeqiNP_082844.1. NM_028568.1.
UniGeneiMm.159027.

3D structure databases

ProteinModelPortaliQ9D9D8.
SMRiQ9D9D8. Positions 20-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000026018.

Proteomic databases

PRIDEiQ9D9D8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026018; ENSMUSP00000026018; ENSMUSG00000025043.
GeneIDi73547.
KEGGimmu:73547.
UCSCiuc009ssi.1. mouse.

Organism-specific databases

CTDi63904.
MGIiMGI:1920797. Dusp21.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ9D9D8.
KOiK14165.
OMAiFWEQLIN.
OrthoDBiEOG7PK90H.
TreeFamiTF316009.

Miscellaneous databases

NextBioi338510.
PROiQ9D9D8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D9D8.
GenevisibleiQ9D9D8. MM.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
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. "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: Testis.
  2. 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.

Entry informationi

Entry nameiDUS21_MOUSE
AccessioniPrimary (citable) accession number: Q9D9D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 110 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.