DUS22_MOUSE
ID DUS22_MOUSE Reviewed; 184 AA.
AC Q99N11; Q5SQN9; Q5SQP0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Dual specificity protein phosphatase 22;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Low molecular weight dual specificity phosphatase 2;
DE Short=LMW-DSP2;
GN Name=Dusp22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NMRI; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP RETRACTED PAPER.
RC TISSUE=Testis;
RX PubMed=11346645; DOI=10.1074/jbc.m100408200;
RA Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.;
RT "Molecular cloning and characterization of a novel dual specificity
RT phosphatase, LMW-DSP2, that lacks the cdc25 homology domain.";
RL J. Biol. Chem. 276:27575-27583(2001).
RN [5]
RP RETRACTION NOTICE OF PUBMED:11346645.
RX PubMed=23997090; DOI=10.1074/jbc.a113.100408;
RA Aoyama K., Nagata M., Oshima K., Matsuda T., Aoki N.;
RL J. Biol. Chem. 288:25658-25658(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Activates the Jnk signaling pathway.
CC {ECO:0000250|UniProtKB:Q9NRW4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NRW4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NRW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99N11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99N11-2; Sequence=VSP_019615;
CC -!- PTM: Myristoylation regulates subcellular location, and is necessary
CC for activation of JNK. {ECO:0000250|UniProtKB:Q9NRW4}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: The publication has been retracted as they duplicated images.
CC {ECO:0000305|PubMed:11346645, ECO:0000305|PubMed:23997090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI24592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF237619; AAK15038.1; -; mRNA.
DR EMBL; AK149363; BAE28836.1; -; mRNA.
DR EMBL; AL731659; CAI24592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL731659; CAI24593.1; -; Genomic_DNA.
DR EMBL; AL731659; CAI24594.1; -; Genomic_DNA.
DR EMBL; BC108362; AAI08363.1; -; mRNA.
DR CCDS; CCDS26417.1; -. [Q99N11-1]
DR CCDS; CCDS26418.1; -. [Q99N11-2]
DR RefSeq; NP_001033044.1; NM_001037955.4. [Q99N11-2]
DR RefSeq; NP_598829.1; NM_134068.3. [Q99N11-1]
DR AlphaFoldDB; Q99N11; -.
DR SMR; Q99N11; -.
DR BioGRID; 222825; 2.
DR STRING; 10090.ENSMUSP00000093603; -.
DR PhosphoSitePlus; Q99N11; -.
DR EPD; Q99N11; -.
DR MaxQB; Q99N11; -.
DR PaxDb; Q99N11; -.
DR PeptideAtlas; Q99N11; -.
DR PRIDE; Q99N11; -.
DR ProteomicsDB; 277530; -. [Q99N11-1]
DR ProteomicsDB; 277531; -. [Q99N11-2]
DR Antibodypedia; 9106; 320 antibodies from 32 providers.
DR DNASU; 105352; -.
DR Ensembl; ENSMUST00000091672; ENSMUSP00000089260; ENSMUSG00000069255. [Q99N11-1]
DR Ensembl; ENSMUST00000095914; ENSMUSP00000093603; ENSMUSG00000069255. [Q99N11-2]
DR GeneID; 105352; -.
DR KEGG; mmu:105352; -.
DR UCSC; uc007pyx.2; mouse. [Q99N11-2]
DR UCSC; uc007pyy.2; mouse. [Q99N11-1]
DR CTD; 56940; -.
DR MGI; MGI:1915926; Dusp22.
DR VEuPathDB; HostDB:ENSMUSG00000069255; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157153; -.
DR HOGENOM; CLU_027074_5_1_1; -.
DR InParanoid; Q99N11; -.
DR OMA; CAYLMWK; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q99N11; -.
DR TreeFam; TF105126; -.
DR BioGRID-ORCS; 105352; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q99N11; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q99N11; protein.
DR Bgee; ENSMUSG00000069255; Expressed in lip and 254 other tissues.
DR ExpressionAtlas; Q99N11; baseline and differential.
DR Genevisible; Q99N11; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0061851; C:leading edge of lamellipodium; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:1903996; P:negative regulation of non-membrane spanning protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
DR GO; GO:0002710; P:negative regulation of T cell mediated immunity; IMP:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lipoprotein; Myristate;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..184
FT /note="Dual specificity protein phosphatase 22"
FT /id="PRO_0000244752"
FT DOMAIN 4..144
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 88
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 170..184
FT /note="AAPGILKYWAFLRRL -> GKYKEQGRMEPRPSSRRWSSFSTLPPLTYNNYT
FT TET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019615"
SQ 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
