Q9D9D8 (DUS21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity phosphatase 21
EC=3.1.3.16
EC=3.1.3.48

Gene names

Name:

Dusp21

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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 component	Cytoplasm Membrane Mitochondrion Mitochondrion inner membrane Nucleus
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from Biological aspect of Ancestor. Source: RefGenome 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_component	extrinsic to membrane Inferred from sequence or structural similarity Ref.5. Source: MGI 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 nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 189	189	Dual specificity phosphatase 21		PRO_0000411986
Regions
	Domain	21 – 161	141	Tyrosine-protein phosphatase
	Region	43 – 128	86	Sufficient for mitochondrial localization
Sites
	Active site	105	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9D9D8 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8EE2F7151BB5CBFA	FASTA	189	21,509
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00112564.
RefSeq	NP_082844.1. NM_028568.1.
UniGene	Mm.159027.
3D structure databases
HSSP	HSSP built from PDB template 1M3G based on UniProtKB Q05923.
ProteinModelPortal	Q9D9D8.
SMR	Q9D9D8. Positions 20-180.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000026018.
Proteomic databases
PRIDE	Q9D9D8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026018; ENSMUSP00000026018; ENSMUSG00000025043.
GeneID	73547.
KEGG	mmu:73547.
UCSC	uc009ssi.1. mouse.
Organism-specific databases
CTD	63904.
MGI	MGI:1920797. Dusp21.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104026.
HOGENOM	HOG000233766.
HOVERGEN	HBG051422.
InParanoid	Q9D9D8.
KO	K14165.
OrthoDB	EOG4VQ9QB.
Gene expression databases
Bgee	Q9D9D8.
Genevestigator	Q9D9D8.
Family and domain databases
InterPro	IPR020417. Atypical_DUSP. IPR020420. Atypical_DUSP_famB. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PRINTS	PR01908. ADSPHPHTASE. PR01910. ADSPHPHTASEB.
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	338510.
SOURCE	Search...

Entry information

Entry name

DUS21_MOUSE

Accession

Primary (citable) accession number: Q9D9D8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 27, 2011
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program