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Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (JNK-stimulatory phosphatase-1) (JSP-1) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2) (Mitogen-activated protein kinase phosphatase x) (MAP kinase phosphatase x) (MKP-x)

 DUS22_HUMAN             Reviewed;         184 AA.
Q9NRW4; B4DK56; Q59GW2; Q5VWR2; Q96AR1;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 147.
RecName: Full=Dual specificity protein phosphatase 22;
EC=3.1.3.16;
EC=3.1.3.48;
AltName: Full=JNK-stimulatory phosphatase-1;
Short=JSP-1;
AltName: Full=Low molecular weight dual specificity phosphatase 2;
Short=LMW-DSP2;
AltName: Full=Mitogen-activated protein kinase phosphatase x;
Short=MAP kinase phosphatase x;
Short=MKP-x;
Name=DUSP22; Synonyms=JSP1, LMWDSP2, MKPX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION (ISOFORM 2),
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11717427; DOI=10.1073/pnas.231499098;
Shen Y., Luche R., Wei B., Gordon M.L., Diltz C.D., Tonks N.K.;
"Activation of the Jnk signaling pathway by a dual-specificity
phosphatase, JSP-1.";
Proc. Natl. Acad. Sci. U.S.A. 98:13613-13618(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hematopoietic stem cell;
Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J.,
Tu Y., Gu W., Fu G., Huang C.;
"Novel genes expressed in hematopoietic stem/progenitor cells from
myelodysplastic syndromes patient.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Mao Y., Xie Y., Cheng H.;
"Cloning and characterization of human LMW-DSP2 gene.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Pancreas;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-184 (ISOFORM 2).
TISSUE=Myeloid;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
MYRISTOYLATION AT GLY-2.
PubMed=20553486; DOI=10.1111/j.1742-4658.2010.07661.x;
Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W.,
Neubert T.A., Tonks N.K.;
"Myristoylation of the dual-specificity phosphatase c-JUN N-terminal
kinase (JNK) stimulatory phosphatase 1 is necessary for its activation
of JNK signaling and apoptosis.";
FEBS J. 277:2463-2473(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-163, SUBUNIT, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17068812; DOI=10.1002/prot.21152;
Yokota T., Nara Y., Kashima A., Matsubara K., Misawa S., Kato R.,
Sugio S.;
"Crystal structure of human dual specificity phosphatase, JNK
stimulatory phosphatase-1, at 1.5 A resolution.";
Proteins 66:272-278(2007).
-!- FUNCTION: Activates the Jnk signaling pathway. Dephosphorylates
and deactivates p38 and stress-activated protein kinase/c-Jun N-
terminal kinase (SAPK/JNK) (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11717427}.
-!- 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:0000269|PubMed:17068812}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NRW4-1; Sequence=Displayed;
Name=2;
IsoId=Q9NRW4-2; Sequence=VSP_019614;
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression seen in heart,
placenta, lung, liver, kidney and pancreas.
{ECO:0000269|PubMed:11717427}.
-!- PTM: Myristoylation regulates subcellular location, and is
necessary for activation of JNK. {ECO:0000269|PubMed:20553486}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class dual specificity subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH16844.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF424702; AAL18850.1; -; mRNA.
EMBL; AF165519; AAF86649.1; -; mRNA.
EMBL; AY249859; AAP76376.1; -; mRNA.
EMBL; AK296402; BAG59068.1; -; mRNA.
EMBL; AL365272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016844; AAH16844.1; ALT_INIT; mRNA.
EMBL; BC022847; AAH22847.1; -; mRNA.
EMBL; AB208997; BAD92234.1; -; mRNA.
CCDS; CCDS4468.1; -. [Q9NRW4-1]
CCDS; CCDS69035.1; -. [Q9NRW4-2]
RefSeq; NP_001273484.1; NM_001286555.1. [Q9NRW4-2]
RefSeq; NP_064570.1; NM_020185.4. [Q9NRW4-1]
UniGene; Hs.29106; -.
PDB; 1WRM; X-ray; 1.50 A; A=1-163.
PDB; 4WOH; X-ray; 1.34 A; A=1-163.
PDBsum; 1WRM; -.
PDBsum; 4WOH; -.
ProteinModelPortal; Q9NRW4; -.
SMR; Q9NRW4; -.
BioGrid; 121264; 112.
IntAct; Q9NRW4; 6.
STRING; 9606.ENSP00000345281; -.
BindingDB; Q9NRW4; -.
ChEMBL; CHEMBL3924; -.
DEPOD; Q9NRW4; -.
iPTMnet; Q9NRW4; -.
PhosphoSitePlus; Q9NRW4; -.
BioMuta; DUSP22; -.
DMDM; 74752929; -.
EPD; Q9NRW4; -.
MaxQB; Q9NRW4; -.
PaxDb; Q9NRW4; -.
PeptideAtlas; Q9NRW4; -.
PRIDE; Q9NRW4; -.
DNASU; 56940; -.
Ensembl; ENST00000344450; ENSP00000345281; ENSG00000112679. [Q9NRW4-1]
Ensembl; ENST00000419235; ENSP00000397459; ENSG00000112679. [Q9NRW4-2]
GeneID; 56940; -.
KEGG; hsa:56940; -.
UCSC; uc003msx.5; human. [Q9NRW4-1]
CTD; 56940; -.
DisGeNET; 56940; -.
EuPathDB; HostDB:ENSG00000112679.14; -.
GeneCards; DUSP22; -.
HGNC; HGNC:16077; DUSP22.
HPA; HPA031394; -.
neXtProt; NX_Q9NRW4; -.
OpenTargets; ENSG00000112679; -.
PharmGKB; PA134991025; -.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000118853; -.
HOGENOM; HOG000007880; -.
HOVERGEN; HBG054344; -.
InParanoid; Q9NRW4; -.
KO; K14165; -.
OMA; LFIGNFK; -.
OrthoDB; EOG091G0NE0; -.
PhylomeDB; Q9NRW4; -.
TreeFam; TF105126; -.
SABIO-RK; Q9NRW4; -.
SignaLink; Q9NRW4; -.
SIGNOR; Q9NRW4; -.
ChiTaRS; DUSP22; human.
EvolutionaryTrace; Q9NRW4; -.
GeneWiki; DUSP22; -.
GenomeRNAi; 56940; -.
PRO; PR:Q9NRW4; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112679; -.
CleanEx; HS_DUSP22; -.
ExpressionAtlas; Q9NRW4; baseline and differential.
Genevisible; Q9NRW4; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0000188; P:inactivation of MAPK activity; TAS:ProtInc.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0050868; P:negative regulation of T cell activation; IEA:Ensembl.
GO; GO:0002710; P:negative regulation of T cell mediated immunity; IEA:Ensembl.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
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; 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.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Lipoprotein; Myristate; Nucleus; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 184 Dual specificity protein phosphatase 22.
/FTId=PRO_0000244751.
DOMAIN 65 133 Tyrosine-protein phosphatase.
ACT_SITE 88 88 Phosphocysteine intermediate.
{ECO:0000250}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:20553486}.
VAR_SEQ 170 184 AAPGILKFWAFLRRL -> GKYKEQGRTEPQPGARRWSSFP
ALAPLTYDNYTTET (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.7}.
/FTId=VSP_019614.
VARIANT 119 119 R -> H (in dbSNP:rs7768224).
/FTId=VAR_026912.
STRAND 6 9 {ECO:0000244|PDB:4WOH}.
STRAND 12 15 {ECO:0000244|PDB:4WOH}.
HELIX 19 21 {ECO:0000244|PDB:4WOH}.
HELIX 23 28 {ECO:0000244|PDB:4WOH}.
STRAND 31 38 {ECO:0000244|PDB:4WOH}.
STRAND 49 54 {ECO:0000244|PDB:4WOH}.
HELIX 64 66 {ECO:0000244|PDB:4WOH}.
HELIX 67 79 {ECO:0000244|PDB:4WOH}.
STRAND 83 87 {ECO:0000244|PDB:4WOH}.
STRAND 89 93 {ECO:0000244|PDB:4WOH}.
HELIX 94 106 {ECO:0000244|PDB:4WOH}.
HELIX 111 121 {ECO:0000244|PDB:4WOH}.
HELIX 129 141 {ECO:0000244|PDB:4WOH}.
HELIX 143 154 {ECO:0000244|PDB:4WOH}.
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


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