Q99N11 (DUS22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	184 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
PTM	Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC positive regulation of JNK cascade Inferred from direct assay PubMed 12138158. Source: MGI regulation of cell proliferation Inferred from mutant phenotype PubMed 12138158. Source: MGI transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype PubMed 12138158. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from sequence orthology PubMed 12138158. Source: MGI
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 184	183	Dual specificity protein phosphatase 22		PRO_0000244752
Regions
	Domain	65 – 133	69	Tyrosine-protein phosphatase
Sites
	Active site	88	1	Phosphocysteine intermediate
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Alternative sequence	170 – 184	15	AAPGI…FLRRL → GKYKEQGRMEPRPSSRRWSS FSTLPPLTYNNYTTET in isoform 2.		VSP_019615
Experimental info
	Mutagenesis	57	1	D → A: Great decrease in activity. Ref.1
	Mutagenesis	88	1	C → S: Complete loss of activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 64953325E88AB577	FASTA	184	20,997
	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
	Isoform 2 [UniParc]. Checksum: 643BD84636335A75	FASTA	205	23,489
	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 DAEEAKNILG KYKEQGRMEP 190 200 RPSSRRWSSF STLPPLTYNN YTTET

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00117982. IPI00515139.
RefSeq	NP_001033044.1. NM_001037955.3. NP_598829.1. NM_134068.2.
UniGene	Mm.289646.
3D structure databases
ProteinModelPortal	Q99N11.
SMR	Q99N11. Positions 1-154.
ModBase	Search...
Proteomic databases
PaxDb	Q99N11.
PRIDE	Q99N11.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255.
GeneID	105352.
KEGG	mmu:105352.
UCSC	uc007pyx.1. mouse. uc007pyy.1. mouse.
Organism-specific databases
CTD	56940.
MGI	MGI:1915926. Dusp22.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00680000099678.
HOGENOM	HOG000007880.
HOVERGEN	HBG054344.
KO	K04459.
OMA	WLREEYG.
OrthoDB	EOG4RFKT3.
Gene expression databases
Bgee	Q99N11.
CleanEx	MM_DUSP22.
Genevestigator	Q99N11.
GermOnline	ENSMUSG00000069255. Mus musculus.
Family and domain databases
InterPro	IPR020417. Atypical_DUSP. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PRINTS	PR01908. ADSPHPHTASE.
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
NextBio	357626.
SOURCE	Search...

Entry information

Entry name

DUS22_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program