Reviewed, UniProtKB/Swiss-Prot Q9D0T2 (DUS12_MOUSE)

Names and origin

Protein names

Recommended name:
    Dual specificity protein phosphatase 12
    EC=3.1.3.48
    EC=3.1.3.16
Alternative name(s):
    Dual specificity phosphatase T-DSP4
    Dual specificity phosphatase VH1

Gene names

Name:

Dusp12

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from direct assay. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Dual specificity protein phosphatase 12		PRO_0000094819
Regions
	Domain	87 – 161	75	Tyrosine-protein phosphatase
Sites
	Active site	114	1	Phosphocysteine intermediate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
Experimental info
	Sequence conflict	7	1	S → T in AAG44739. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9D0T2-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B6A254D319BEC98F	FASTA	339	37,159
	10 20 30 40 50 60 MLEAQGSNHG CERQAPTASP ASSAGHAVEV RPGLYLGGAA AVAEPGHLRE AGITAVLTVD 70 80 90 100 110 120 SEPAFPAGAG FEGLRSLFVP ALDKPETDLL SHLDRCVAFI GQARSEGRAV LVHCHAGVSR 130 140 150 160 170 180 SVAVVMAFIM KTDQLTFEKA YDILRTVKPE AKVNEGFEWQ LKLYEAMGYE VDTSSAFYKQ 190 200 210 220 230 240 YRLQKVTEKC PKLWNLPQEL FAVDPTTISQ GLKDDILYKC RKCRRSLFRH SSILGHSEGS 250 260 270 280 290 300 GPIAFAHKRT APSSVLTTGS QAQCTSYFIE PVQWMESTLL GVMDGQLLCP KCSAKLGSFN 310 320 330 WYGEQCSCGR WITPAFQIHK NRVDEMKMLP VLGSQTKKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of putative dual specificity phosphatase T-DSP4." Aoyama K., Matsuda T., Aoki N. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"mVH1, a dual-specificity phosphatase whose expression is cell cycle regulated." Zhang X.M., Dormady S.P., Chaung W., Basch R.S. Mamm. Genome 11:1154-1156(2000) [PubMed: 11130991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[3]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF280810 mRNA. Translation: AAK69508.1. AF268196 mRNA. Translation: AAG44739.1. AK004488 mRNA. Translation: BAB23328.1.
IPI	IPI00315689.
RefSeq	NP_075662.2.
UniGene	Mm.34365
3D structure databases
SMR	Q9D0T2. Positions 26-167, 73-201.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9D0T2.
Proteomic databases
PRIDE	Q9D0T2.
Genome annotation databases
Ensembl	ENSMUST00000027970; ENSMUSP00000027970; ENSMUSG00000026659; Mus musculus. [Genome view]
GeneID	80915.
KEGG	mmu:80915.
UCSC	uc007dml.1. mouse.
Organism-specific databases
CTD	80915.
MGI	MGI:1890614. Dusp12.
Phylogenomic databases
HOGENOM	HBG588460.
HOVERGEN	Q9D0T2.
InParanoid	Q9D0T2.
OMA	VTAYLMK.
OrthoDB	EOG9KPWX9.
PhylomeDB	Q9D0T2.
Enzyme and pathway databases
BRENDA	3.1.3.16. 244. 3.1.3.48. 244.
Gene expression databases
ArrayExpress	Q9D0T2.
Bgee	Q9D0T2.
CleanEx	MM_DUSP12.
Genevestigator	Q9D0T2.
GermOnline	ENSMUSG00000026659. Mus musculus.
Family and domain databases
InterPro	IPR000387. Dual-sp/Tyr_phosphatase. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR016278. Tyr_Pase_dual_specific_12. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PIRSF	PIRSF000941. DUSP12. 1 hit.
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. False negative. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	350298.
SOURCE	Search...

Entry information

Entry name

DUS12_MOUSE

Accession

Primary (citable) accession number: Q9D0T2
Secondary accession number(s): Q9EQD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	June 1, 2001
Last modified:	January 19, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)