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Q9D0T2 (DUS12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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 protein phosphatase 12

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase T-DSP4
Dual specificity phosphatase VH1
Gene names
Name:Dusp12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Dual specificity protein phosphatase 12
PRO_0000094819

Regions

Domain87 – 16175Tyrosine-protein phosphatase

Sites

Active site1141Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict71S → T in AAG44739. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D0T2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B6A254D319BEC98F

FASTA33937,159
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. 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: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF280810 mRNA. Translation: AAK69508.1.
AF268196 mRNA. Translation: AAG44739.1.
AK004488 mRNA. Translation: BAB23328.1.
RefSeqNP_075662.2. NM_023173.2.
UniGeneMm.34365.

3D structure databases

ProteinModelPortalQ9D0T2.
SMRQ9D0T2. Positions 26-161.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9D0T2.

Proteomic databases

PaxDbQ9D0T2.
PRIDEQ9D0T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027970; ENSMUSP00000027970; ENSMUSG00000026659.
GeneID80915.
KEGGmmu:80915.
UCSCuc007dml.1. mouse.

Organism-specific databases

CTD11266.
MGIMGI:1890614. Dusp12.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00740000115610.
HOGENOMHOG000243638.
HOVERGENHBG051421.
InParanoidQ9D0T2.
KOK14819.
OMAKITHILT.
PhylomeDBQ9D0T2.
TreeFamTF105123.

Gene expression databases

ArrayExpressQ9D0T2.
BgeeQ9D0T2.
CleanExMM_DUSP12.
GenevestigatorQ9D0T2.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR016278. DUSP12.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PIRSFPIRSF000941. DUSP12. 1 hit.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio350298.
PROQ9D0T2.
SOURCESearch...

Entry information

Entry nameDUS12_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 101 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