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Q99N11 (DUS22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 22

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
Low molecular weight dual specificity phosphatase 2
Short name=LMW-DSP2
Gene names
Name:Dusp22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK). Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

Specifically expressed in the testis. Ref.1

Post-translational modification

Myristoylation regulates subcellular location, and is necessary for activation of JNK By similarity.

Sequence similarities

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

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence CAI24592.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99N11-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99N11-2)

The sequence of this isoform differs from the canonical sequence as follows:
     170-184: AAPGILKYWAFLRRL → GKYKEQGRMEPRPSSRRWSSFSTLPPLTYNNYTTET

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 184183Dual specificity protein phosphatase 22
PRO_0000244752

Regions

Domain65 – 13369Tyrosine-protein phosphatase

Sites

Active site881Phosphocysteine intermediate

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity

Natural variations

Alternative sequence170 – 18415AAPGI…FLRRL → GKYKEQGRMEPRPSSRRWSS FSTLPPLTYNNYTTET in isoform 2.
VSP_019615

Experimental info

Mutagenesis571D → A: Great decrease in activity. Ref.1
Mutagenesis881C → S: Complete loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 64953325E88AB577

FASTA18420,997
        10         20         30         40         50         60 
MGSGMSQILP GLYIGNFKDA RDAEQLSRNK VTHILSVHDT ARPMLEGVKY LCIPAADTPS 

        70         80         90        100        110        120 
QNLTRHFKES IKFIHECRLQ GESCLVHCLA GVSRSVTLVI AYIMTVTDFG WEDALHTVRA 

       130        140        150        160        170        180 
GRSCANPNLG FQRQLQEFEK HEVHQYRQWL REEYGENPLR DAEEAKNILA APGILKYWAF 


LRRL 

« Hide

Isoform 2 [UniParc].

Checksum: 643BD84636335A75
Show »

FASTA20523,489

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel dual specificity phosphatase, LMW-DSP2, that lacks the cdc25 homology domain."
Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.
J. Biol. Chem. 276:27575-27583(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-57 AND CYS-88.
Tissue: Testis.
[2]"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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Retina.
[3]"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.
[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] (ISOFORM 2).
Strain: NMRI.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237619 mRNA. Translation: AAK15038.1.
AK149363 mRNA. Translation: BAE28836.1.
AL731659 Genomic DNA. Translation: CAI24592.1. Sequence problems.
AL731659 Genomic DNA. Translation: CAI24593.1.
AL731659 Genomic DNA. Translation: CAI24594.1.
BC108362 mRNA. Translation: AAI08363.1.
CCDSCCDS26417.1. [Q99N11-1]
CCDS26418.1. [Q99N11-2]
RefSeqNP_001033044.1. NM_001037955.4. [Q99N11-2]
NP_598829.1. NM_134068.3. [Q99N11-1]
UniGeneMm.289646.

3D structure databases

ProteinModelPortalQ99N11.
SMRQ99N11. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222825. 2 interactions.

Proteomic databases

PaxDbQ99N11.
PRIDEQ99N11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
GeneID105352.
KEGGmmu:105352.
UCSCuc007pyx.1. mouse. [Q99N11-2]
uc007pyy.1. mouse. [Q99N11-1]

Organism-specific databases

CTD56940.
MGIMGI:1915926. Dusp22.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00730000110377.
HOGENOMHOG000007880.
HOVERGENHBG054344.
KOK14165.
OMALFIGNFK.
OrthoDBEOG7966HM.
PhylomeDBQ99N11.
TreeFamTF105126.

Gene expression databases

BgeeQ99N11.
CleanExMM_DUSP22.
GenevestigatorQ99N11.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR020417. Atypical_DUSP.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio357626.
PROQ99N11.
SOURCESearch...

Entry information

Entry nameDUS22_MOUSE
AccessionPrimary (citable) accession number: Q99N11
Secondary accession number(s): Q5SQN9, Q5SQP0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 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