ID   DUS22_HUMAN             Reviewed;         184 AA.
AC   Q9NRW4; B4DK56; Q59GW2; Q5VWR2; Q96AR1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Dual specificity protein phosphatase 22;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=JNK-stimulatory phosphatase-1;
DE            Short=JSP-1;
DE   AltName: Full=Low molecular weight dual specificity phosphatase 2;
DE            Short=LMW-DSP2;
DE   AltName: Full=Mitogen-activated protein kinase phosphatase x;
DE            Short=MAP kinase phosphatase x;
DE            Short=MKP-x;
GN   Name=DUSP22; Synonyms=JSP1, LMWDSP2, MKPX;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION (ISOFORM 2),
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11717427; DOI=10.1073/pnas.231499098;
RA   Shen Y., Luche R., Wei B., Gordon M.L., Diltz C.D., Tonks N.K.;
RT   "Activation of the Jnk signaling pathway by a dual-specificity phosphatase,
RT   JSP-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:13613-13618(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hematopoietic stem cell;
RA   Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y.,
RA   Gu W., Fu G., Huang C.;
RT   "Novel genes expressed in hematopoietic stem/progenitor cells from
RT   myelodysplastic syndromes patient.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Mao Y., Xie Y., Cheng H.;
RT   "Cloning and characterization of human LMW-DSP2 gene.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Pancreas;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-184 (ISOFORM 2).
RC   TISSUE=Myeloid;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   SUBCELLULAR LOCATION, AND MYRISTOYLATION AT GLY-2.
RX   PubMed=20553486; DOI=10.1111/j.1742-4658.2010.07661.x;
RA   Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W.,
RA   Neubert T.A., Tonks N.K.;
RT   "Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase
RT   (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK
RT   signaling and apoptosis.";
RL   FEBS J. 277:2463-2473(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-163, SUBUNIT, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=17068812; DOI=10.1002/prot.21152;
RA   Yokota T., Nara Y., Kashima A., Matsubara K., Misawa S., Kato R., Sugio S.;
RT   "Crystal structure of human dual specificity phosphatase, JNK stimulatory
RT   phosphatase-1, at 1.5 A resolution.";
RL   Proteins 66:272-278(2007).
CC   -!- FUNCTION: Activates the Jnk signaling pathway.
CC       {ECO:0000269|PubMed:11717427}.
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:0000269|PubMed:17068812}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20553486}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NRW4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NRW4-2; Sequence=VSP_019614;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression seen in heart,
CC       placenta, lung, liver, kidney and pancreas.
CC       {ECO:0000269|PubMed:11717427}.
CC   -!- PTM: Myristoylation regulates subcellular location, and is necessary
CC       for activation of JNK. {ECO:0000269|PubMed:20553486}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16844.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF424702; AAL18850.1; -; mRNA.
DR   EMBL; AF165519; AAF86649.1; -; mRNA.
DR   EMBL; AY249859; AAP76376.1; -; mRNA.
DR   EMBL; AK296402; BAG59068.1; -; mRNA.
DR   EMBL; AL365272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016844; AAH16844.1; ALT_INIT; mRNA.
DR   EMBL; BC022847; AAH22847.1; -; mRNA.
DR   EMBL; AB208997; BAD92234.1; -; mRNA.
DR   CCDS; CCDS4468.1; -. [Q9NRW4-1]
DR   CCDS; CCDS69035.1; -. [Q9NRW4-2]
DR   RefSeq; NP_001273484.1; NM_001286555.1. [Q9NRW4-2]
DR   RefSeq; NP_064570.1; NM_020185.4. [Q9NRW4-1]
DR   PDB; 1WRM; X-ray; 1.50 A; A=1-163.
DR   PDB; 4WOH; X-ray; 1.34 A; A=1-163.
DR   PDB; 6L1S; X-ray; 1.36 A; A=1-155.
DR   PDB; 6LMY; X-ray; 1.50 A; A=1-155.
DR   PDB; 6LOT; X-ray; 1.69 A; A=1-155.
DR   PDB; 6LOU; X-ray; 1.53 A; A=1-155.
DR   PDB; 6LVQ; X-ray; 1.38 A; A=1-155.
DR   PDB; 7C8S; X-ray; 1.31 A; A=1-155.
DR   PDBsum; 1WRM; -.
DR   PDBsum; 4WOH; -.
DR   PDBsum; 6L1S; -.
DR   PDBsum; 6LMY; -.
DR   PDBsum; 6LOT; -.
DR   PDBsum; 6LOU; -.
DR   PDBsum; 6LVQ; -.
DR   PDBsum; 7C8S; -.
DR   AlphaFoldDB; Q9NRW4; -.
DR   SMR; Q9NRW4; -.
DR   BioGRID; 121264; 139.
DR   IntAct; Q9NRW4; 46.
DR   MINT; Q9NRW4; -.
DR   STRING; 9606.ENSP00000397459; -.
DR   BindingDB; Q9NRW4; -.
DR   ChEMBL; CHEMBL3924; -.
DR   DEPOD; DUSP22; -.
DR   iPTMnet; Q9NRW4; -.
DR   PhosphoSitePlus; Q9NRW4; -.
DR   BioMuta; DUSP22; -.
DR   DMDM; 74752929; -.
DR   EPD; Q9NRW4; -.
DR   jPOST; Q9NRW4; -.
DR   MassIVE; Q9NRW4; -.
DR   MaxQB; Q9NRW4; -.
DR   PaxDb; 9606-ENSP00000397459; -.
DR   PeptideAtlas; Q9NRW4; -.
DR   ProteomicsDB; 82429; -. [Q9NRW4-1]
DR   ProteomicsDB; 82430; -. [Q9NRW4-2]
DR   Antibodypedia; 9106; 354 antibodies from 32 providers.
DR   DNASU; 56940; -.
DR   Ensembl; ENST00000344450.9; ENSP00000345281.5; ENSG00000112679.15. [Q9NRW4-1]
DR   Ensembl; ENST00000419235.7; ENSP00000397459.2; ENSG00000112679.15. [Q9NRW4-2]
DR   GeneID; 56940; -.
DR   KEGG; hsa:56940; -.
DR   MANE-Select; ENST00000419235.7; ENSP00000397459.2; NM_001286555.3; NP_001273484.1. [Q9NRW4-2]
DR   UCSC; uc003msx.5; human. [Q9NRW4-1]
DR   AGR; HGNC:16077; -.
DR   CTD; 56940; -.
DR   DisGeNET; 56940; -.
DR   GeneCards; DUSP22; -.
DR   HGNC; HGNC:16077; DUSP22.
DR   HPA; ENSG00000112679; Low tissue specificity.
DR   neXtProt; NX_Q9NRW4; -.
DR   OpenTargets; ENSG00000112679; -.
DR   PharmGKB; PA134991025; -.
DR   VEuPathDB; HostDB:ENSG00000112679; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000157153; -.
DR   HOGENOM; CLU_027074_5_1_1; -.
DR   InParanoid; Q9NRW4; -.
DR   OMA; CAYLMWK; -.
DR   OrthoDB; 3037246at2759; -.
DR   PhylomeDB; Q9NRW4; -.
DR   TreeFam; TF105126; -.
DR   PathwayCommons; Q9NRW4; -.
DR   SABIO-RK; Q9NRW4; -.
DR   SignaLink; Q9NRW4; -.
DR   SIGNOR; Q9NRW4; -.
DR   BioGRID-ORCS; 56940; 25 hits in 1176 CRISPR screens.
DR   ChiTaRS; DUSP22; human.
DR   EvolutionaryTrace; Q9NRW4; -.
DR   GeneWiki; DUSP22; -.
DR   GenomeRNAi; 56940; -.
DR   Pharos; Q9NRW4; Tbio.
DR   PRO; PR:Q9NRW4; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9NRW4; Protein.
DR   Bgee; ENSG00000112679; Expressed in secondary oocyte and 201 other cell types or tissues.
DR   ExpressionAtlas; Q9NRW4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0031941; C:filamentous actin; IDA:ARUK-UCL.
DR   GO; GO:0061851; C:leading edge of lamellipodium; IDA:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:ARUK-UCL.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:ARUK-UCL.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:ARUK-UCL.
DR   GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:ARUK-UCL.
DR   GO; GO:1903996; P:negative regulation of non-membrane spanning protein tyrosine kinase activity; IMP:ARUK-UCL.
DR   GO; GO:0050868; P:negative regulation of T cell activation; IEA:Ensembl.
DR   GO; GO:0002710; P:negative regulation of T cell mediated immunity; IEA:Ensembl.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:ARUK-UCL.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd14581; DUSP22; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45948:SF3; DUAL SPECIFICITY PROTEIN PHOSPHATASE 22; 1.
DR   PANTHER; PTHR45948; DUAL SPECIFICITY PROTEIN PHOSPHATASE DDB_G0269404-RELATED; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR   Genevisible; Q9NRW4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Lipoprotein;
KW   Myristate; Phosphoprotein; 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_0000244751"
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   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:20553486"
FT   VAR_SEQ         170..184
FT                   /note="AAPGILKFWAFLRRL -> GKYKEQGRTEPQPGARRWSSFPALAPLTYDNYT
FT                   TET (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT                   /id="VSP_019614"
FT   VARIANT         119
FT                   /note="R -> H (in dbSNP:rs7768224)"
FT                   /id="VAR_026912"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           23..28
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           94..106
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           111..121
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           129..141
FT                   /evidence="ECO:0007829|PDB:7C8S"
FT   HELIX           143..153
FT                   /evidence="ECO:0007829|PDB:7C8S"
SQ   SEQUENCE   184 AA;  20910 MW;  B3F962A087C2BA20 CRC64;
     MGNGMNKILP GLYIGNFKDA RDAEQLSKNK VTHILSVHDS ARPMLEGVKY LCIPAADSPS
     QNLTRHFKES IKFIHECRLR GESCLVHCLA GVSRSVTLVI AYIMTVTDFG WEDALHTVRA
     GRSCANPNVG FQRQLQEFEK HEVHQYRQWL KEEYGESPLQ DAEEAKNILA APGILKFWAF
     LRRL
//