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Tyrosine-protein phosphatase non-receptor type 22 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP) (PEST-domain phosphatase) (PEP)

 PTN22_MOUSE             Reviewed;         802 AA.
P29352; Q7TMP9;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
12-SEP-2018, entry version 157.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 22;
EC=3.1.3.48;
AltName: Full=Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP;
AltName: Full=PEST-domain phosphatase;
Short=PEP;
Name=Ptpn22; Synonyms=Ptpn8;
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].
PubMed=1373816; DOI=10.1128/MCB.12.5.2396;
Matthews R.J., Bowne D.B., Flores E., Thomas M.L.;
"Characterization of hematopoietic intracellular protein tyrosine
phosphatases: description of a phosphatase containing an SH2 domain
and another enriched in proline-, glutamic acid-, serine-, and
threonine-rich sequences.";
Mol. Cell. Biol. 12:2396-2405(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 495-789, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH CSK.
TISSUE=Splenocyte;
PubMed=8890164;
Cloutier J.-F., Veillette A.;
"Association of inhibitory tyrosine protein kinase p50csk with protein
tyrosine phosphatase PEP in T cells and other hemopoietic cells.";
EMBO J. 15:4909-4918(1996).
[4]
INTERACTION WITH LPXN.
PubMed=15786712; DOI=10.1007/s11010-005-2149-6;
Watanabe N., Amano N., Ishizuka H., Mashima K.;
"Leupaxin binds to PEST domain tyrosine phosphatase PEP.";
Mol. Cell. Biochem. 269:13-17(2005).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; SER-680 AND
SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-687, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
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).
[7]
FUNCTION, AND INTERACTION WITH TRAF3.
PubMed=23871208; DOI=10.1016/j.immuni.2013.06.013;
Wang Y., Shaked I., Stanford S.M., Zhou W., Curtsinger J.M.,
Mikulski Z., Shaheen Z.R., Cheng G., Sawatzke K., Campbell A.M.,
Auger J.L., Bilgic H., Shoyama F.M., Schmeling D.O., Balfour H.H. Jr.,
Hasegawa K., Chan A.C., Corbett J.A., Binstadt B.A., Mescher M.F.,
Ley K., Bottini N., Peterson E.J.;
"The autoimmunity-associated gene PTPN22 potentiates toll-like
receptor-driven, type 1 interferon-dependent immunity.";
Immunity 39:111-122(2013).
[8]
FUNCTION.
PubMed=23991106; DOI=10.1371/journal.pone.0072384;
Spalinger M.R., Lang S., Vavricka S.R., Fried M., Rogler G.,
Scharl M.;
"Protein tyrosine phosphatase non-receptor type 22 modulates NOD2-
induced cytokine release and autophagy.";
PLoS ONE 8:E72384-E72384(2013).
[9]
STRUCTURE BY NMR OF 612-629 IN COMPLEX WITH CSK.
PubMed=11685249; DOI=10.1038/nsb1101-998;
Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.;
"A novel, specific interaction involving the Csk SH3 domain and its
natural ligand.";
Nat. Struct. Biol. 8:998-1004(2001).
-!- FUNCTION: Acts as negative regulator of T-cell receptor (TCR)
signaling by direct dephosphorylation of the Src family kinases
LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV,
VCP and other key signaling molecules (By similarity). Associates
with and probably dephosphorylates CBL (By similarity).
Dephosphorylates LCK at its activating 'Tyr-394' residue (By
similarity). Dephosphorylates ZAP70 at its activating 'Tyr-492'
residue (By similarity). Dephosphorylates the immune system
activator SKAP2 (By similarity). Positively regulates toll-like
receptor (TLR)-induced type 1 interferon production
(PubMed:23871208). Promotes host antiviral responses mediated by
type 1 interferon (PubMed:23871208). Regulates NOD2-induced pro-
inflammatory cytokine secretion and autophagy (PubMed:23991106).
{ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:23871208,
ECO:0000269|PubMed:23991106}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Interacts with CBL (By similarity). Interacts with CSK
(PubMed:8890164, PubMed:11685249). Interacts with LPXN
(PubMed:15786712). Interacts with TRAF3 (via MATH domain); the
interaction promotes TRAF3 polyubiquitination (PubMed:23871208).
{ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:11685249,
ECO:0000269|PubMed:15786712, ECO:0000269|PubMed:23871208,
ECO:0000269|PubMed:8890164}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8890164}.
-!- TISSUE SPECIFICITY: Spleen, thymus, lymph node and bone marrow.
-!- PTM: Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability
to dephosphorylate and inactivate the SRC family kinases.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M90388; AAA39994.1; -; mRNA.
EMBL; BC055377; AAH55377.1; -; mRNA.
CCDS; CCDS38577.1; -.
PIR; B44390; B44390.
RefSeq; NP_033005.1; NM_008979.2.
RefSeq; XP_006501211.1; XM_006501148.3.
RefSeq; XP_006501212.1; XM_006501149.3.
RefSeq; XP_006501213.1; XM_006501150.2.
RefSeq; XP_011238343.1; XM_011240041.2.
RefSeq; XP_011238344.1; XM_011240042.2.
UniGene; Mm.395; -.
PDB; 1JEG; NMR; -; B=605-629.
PDBsum; 1JEG; -.
ProteinModelPortal; P29352; -.
SMR; P29352; -.
ELM; P29352; -.
IntAct; P29352; 3.
MINT; P29352; -.
STRING; 10090.ENSMUSP00000029433; -.
ChEMBL; CHEMBL2157855; -.
SwissLipids; SLP:000001911; -.
iPTMnet; P29352; -.
PhosphoSitePlus; P29352; -.
EPD; P29352; -.
MaxQB; P29352; -.
PaxDb; P29352; -.
PRIDE; P29352; -.
Ensembl; ENSMUST00000029433; ENSMUSP00000029433; ENSMUSG00000027843.
GeneID; 19260; -.
KEGG; mmu:19260; -.
UCSC; uc008qtv.2; mouse.
CTD; 26191; -.
MGI; MGI:107170; Ptpn22.
eggNOG; KOG0789; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00900000140785; -.
HOGENOM; HOG000252955; -.
HOVERGEN; HBG103877; -.
InParanoid; P29352; -.
KO; K18024; -.
OMA; PLQKHQS; -.
OrthoDB; EOG091G0B5O; -.
PhylomeDB; P29352; -.
TreeFam; TF351977; -.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
ChiTaRS; Ptpn22; mouse.
EvolutionaryTrace; P29352; -.
PRO; PR:P29352; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027843; Expressed in 96 organ(s), highest expression level in spleen.
ExpressionAtlas; P29352; baseline and differential.
Genevisible; P29352; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
GO; GO:0016791; F:phosphatase activity; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0071225; P:cellular response to muramyl dipeptide; IDA:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI.
GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0043508; P:negative regulation of JUN kinase activity; ISO:MGI.
GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB.
GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:BHF-UCL.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0035644; P:phosphoanandamide dephosphorylation; IDA:BHF-UCL.
GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0071663; P:positive regulation of granzyme B production; IMP:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; ISO:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; IMP:UniProtKB.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
GO; GO:0032481; P:positive regulation of type I interferon production; ISO:MGI.
GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
GO; GO:1903169; P:regulation of calcium ion transmembrane transport; ISO:MGI.
GO; GO:0002685; P:regulation of leukocyte migration; IMP:UniProtKB.
GO; GO:0032817; P:regulation of natural killer cell proliferation; ISS:BHF-UCL.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016276; PTPN22.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000930; PTPN8_PTPN22; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
3D-structure; Autophagy; Complete proteome; Cytoplasm; Hydrolase;
Immunity; Phosphoprotein; Protein phosphatase; Reference proteome.
CHAIN 1 802 Tyrosine-protein phosphatase non-receptor
type 22.
/FTId=PRO_0000094776.
DOMAIN 24 289 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 227 233 Substrate binding. {ECO:0000250}.
REGION 613 621 Interaction with CSK.
{ECO:0000269|PubMed:8890164}.
ACT_SITE 227 227 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 195 195 Substrate. {ECO:0000250}.
BINDING 274 274 Substrate. {ECO:0000250}.
MOD_RES 35 35 Phosphoserine; by PKC/PRKCD.
{ECO:0000250|UniProtKB:Q9Y2R2}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CONFLICT 91 91 K -> Q (in Ref. 2; AAH55377).
{ECO:0000305}.
CONFLICT 141 141 R -> H (in Ref. 2; AAH55377).
{ECO:0000305}.
HELIX 621 624 {ECO:0000244|PDB:1JEG}.
SEQUENCE 802 AA; 89714 MW; 0F1E45339BD4613E CRC64;
MDQREILQQL LKEAQKKKLN SEEFASEFLK LKRQSTKYKA DKIYPTTVAQ RPKNIKKNRY
KDILPYDHSL VELSLLTSDE DSSYINASFI KGVYGPKAYI ATQGPLSTTL LDFWRMIWEY
RILVIVMACM EFEMGKKKCE RYWAEPGETQ LQFGPFSISC EAEKKKSDYK IRTLKAKFNN
ETRIIYQFHY KNWPDHDVPS SIDPILQLIW DMRCYQEDDC VPICIHCSAG CGRTGVICAV
DYTWMLLKDG IIPKNFSVFN LIQEMRTQRP SLVQTQEQYE LVYSAVLELF KRHMDVISDN
HLGREIQAQC SIPEQSLTVE ADSCPLDLPK NAMRDVKTTN QHSKQGAEAE STGGSSLGLR
TSTMNAEEEL VLHSAKSSPS FNCLELNCGC NNKAVITRNG QARASPVVGE PLQKYQSLDF
GSMLFGSCPS ALPINTADRY HNSKGPVKRT KSTPFELIQQ RKTNDLAVGD GFSCLESQLH
EHYSLRELQV QRVAHVSSEE LNYSLPGACD ASCVPRHSPG ALRVHLYTSL AEDPYFSSSP
PNSADSKMSF DLPEKQDGAT SPGALLPASS TTSFFYSNPH DSLVMNTLTS FSPPLNQETA
VEAPSRRTDD EIPPPLPERT PESFIVVEEA GEPSPRVTES LPLVVTFGAS PECSGTSEMK
SHDSVGFTPS KNVKLRSPKS DRHQDGSPPP PLPERTLESF FLADEDCIQA QAVQTSSTSY
PETTENSTSS KQTLRTPGKS FTRSKSLKIF RNMKKSVCNS SSPSKPTERV QPKNSSSFLN
FGFGNRFSKP KGPRNPPSAW NM


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