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Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2)

 DUS22_MOUSE             Reviewed;         184 AA.
Q99N11; Q5SQN9; Q5SQP0;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-MAY-2017, entry version 119.
RecName: Full=Dual specificity protein phosphatase 22;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=Low molecular weight dual specificity phosphatase 2;
Short=LMW-DSP2;
Name=Dusp22;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-57 AND CYS-88.
TISSUE=Testis;
PubMed=11346645; DOI=10.1074/jbc.M100408200;
Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.;
"Molecular cloning and characterization of a novel dual specificity
phosphatase, LMW-DSP2, that lacks the cdc25 homology domain.";
J. Biol. Chem. 276:27575-27583(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Activates the Jnk signaling pathway. Dephosphorylates
and deactivates p38 and stress-activated protein kinase/c-Jun N-
terminal kinase (SAPK/JNK). {ECO:0000269|PubMed:11346645}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11346645}.
Nucleus {ECO:0000269|PubMed:11346645}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99N11-1; Sequence=Displayed;
Name=2;
IsoId=Q99N11-2; Sequence=VSP_019615;
-!- TISSUE SPECIFICITY: Specifically expressed in the testis.
{ECO:0000269|PubMed:11346645}.
-!- PTM: Myristoylation regulates subcellular location, and is
necessary for activation of JNK. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI24592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF237619; AAK15038.1; -; mRNA.
EMBL; AK149363; BAE28836.1; -; mRNA.
EMBL; AL731659; CAI24592.1; ALT_SEQ; Genomic_DNA.
EMBL; AL731659; CAI24593.1; -; Genomic_DNA.
EMBL; AL731659; CAI24594.1; -; Genomic_DNA.
EMBL; BC108362; AAI08363.1; -; mRNA.
CCDS; CCDS26417.1; -. [Q99N11-1]
CCDS; CCDS26418.1; -. [Q99N11-2]
RefSeq; NP_001033044.1; NM_001037955.4. [Q99N11-2]
RefSeq; NP_598829.1; NM_134068.3. [Q99N11-1]
UniGene; Mm.289646; -.
ProteinModelPortal; Q99N11; -.
SMR; Q99N11; -.
BioGrid; 222825; 2.
STRING; 10090.ENSMUSP00000093603; -.
PhosphoSitePlus; Q99N11; -.
EPD; Q99N11; -.
PaxDb; Q99N11; -.
PeptideAtlas; Q99N11; -.
PRIDE; Q99N11; -.
Ensembl; ENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
Ensembl; ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
GeneID; 105352; -.
KEGG; mmu:105352; -.
UCSC; uc007pyx.2; mouse. [Q99N11-2]
UCSC; uc007pyy.2; mouse. [Q99N11-1]
CTD; 56940; -.
MGI; MGI:1915926; Dusp22.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118853; -.
HOGENOM; HOG000007880; -.
HOVERGEN; HBG054344; -.
InParanoid; Q99N11; -.
KO; K14165; -.
OMA; LFIGNFK; -.
OrthoDB; EOG091G0NE0; -.
PhylomeDB; Q99N11; -.
TreeFam; TF105126; -.
PRO; PR:Q99N11; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000069255; -.
CleanEx; MM_DUSP22; -.
ExpressionAtlas; Q99N11; baseline and differential.
Genevisible; Q99N11; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
GO; GO:0002710; P:negative regulation of T cell mediated immunity; IMP:MGI.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
CDD; cd00127; DSPc; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR020417; Atypical_DUSP.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00782; DSPc; 1.
PRINTS; PR01908; ADSPHPHTASE.
SMART; SM00195; DSPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
Lipoprotein; Myristate; Nucleus; Protein phosphatase;
Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 184 Dual specificity protein phosphatase 22.
/FTId=PRO_0000244752.
DOMAIN 65 133 Tyrosine-protein phosphatase.
ACT_SITE 88 88 Phosphocysteine intermediate.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 170 184 AAPGILKYWAFLRRL -> GKYKEQGRMEPRPSSRRWSSFS
TLPPLTYNNYTTET (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_019615.
MUTAGEN 57 57 D->A: Great decrease in activity.
{ECO:0000269|PubMed:11346645}.
MUTAGEN 88 88 C->S: Complete loss of activity.
{ECO:0000269|PubMed:11346645}.
SEQUENCE 184 AA; 20997 MW; 64953325E88AB577 CRC64;
MGSGMSQILP GLYIGNFKDA RDAEQLSRNK VTHILSVHDT ARPMLEGVKY LCIPAADTPS
QNLTRHFKES IKFIHECRLQ GESCLVHCLA GVSRSVTLVI AYIMTVTDFG WEDALHTVRA
GRSCANPNLG FQRQLQEFEK HEVHQYRQWL REEYGENPLR DAEEAKNILA APGILKYWAF
LRRL


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