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

 PTN22_HUMAN             Reviewed;         807 AA.
Q9Y2R2; A0N0K6; B1ALC8; D4NZ71; E9PLD8; E9PPI1; O95063; O95064;
Q6IPX8; Q8WVM1;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
25-OCT-2017, entry version 159.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 22;
EC=3.1.3.48 {ECO:0000269|PubMed:21719704};
AltName: Full=Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP;
AltName: Full=Lymphoid phosphatase;
Short=LyP;
AltName: Full=PEST-domain phosphatase;
Short=PEP;
Name=PTPN22; Synonyms=PTPN8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH
CBL.
PubMed=10068674;
Cohen S., Dadi H., Shaoul E., Sharfe N., Roifman C.M.;
"Cloning and characterization of a lymphoid-specific, inducible human
protein tyrosine phosphatase, Lyp.";
Blood 93:2013-2024(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT TRP-620.
PubMed=21044313; DOI=10.1186/1471-2199-11-78;
Wang S., Dong H., Han J., Ho W.T., Fu X., Zhao Z.J.;
"Identification of a variant form of tyrosine phosphatase LYP.";
BMC Mol. Biol. 11:78-78(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TRP-620.
Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y.,
Yu M., Chen S., Mao M., Chen Z.;
"Human protein tyrosine phosphatase (70zpep) homolog.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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 [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-620.
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-620.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
TISSUE=Lymph;
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).
[9]
FUNCTION.
PubMed=16461343; DOI=10.1074/jbc.M600498200;
Wu J., Katrekar A., Honigberg L.A., Smith A.M., Conn M.T., Tang J.,
Jeffery D., Mortara K., Sampang J., Williams S.R., Buggy J.,
Clark J.M.;
"Identification of substrates of human protein-tyrosine phosphatase
PTPN22.";
J. Biol. Chem. 281:11002-11010(2006).
[10]
REVIEW ON FUNCTION.
PubMed=17729039; DOI=10.1080/08916930701464897;
Vang T., Miletic A.V., Bottini N., Mustelin T.;
"Protein tyrosine phosphatase PTPN22 in human autoimmunity.";
Autoimmunity 40:453-461(2007).
[11]
ALTERNATIVE SPLICING (ISOFORM 6).
PubMed=22427951; DOI=10.1371/journal.pone.0033067;
Chang H.H., Tai T.S., Lu B., Iannaccone C., Cernadas M., Weinblatt M.,
Shadick N., Miaw S.C., Ho I.C.;
"PTPN22.6, a dominant negative isoform of PTPN22 and potential
biomarker of rheumatoid arthritis.";
PLoS ONE 7:E33067-E33067(2012).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, 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).
[14]
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).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH
INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, AND MUTAGENESIS OF
SER-35 AND THR-36.
PubMed=18056643; DOI=10.1073/pnas.0706233104;
Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A.,
Zhang Z.Y.;
"Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-
specific tyrosine phosphatase implicated in autoimmune diseases.";
Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-302, DISULFIDE BOND, AND
MUTAGENESIS OF CYS-129 AND CYS-231.
PubMed=19371084; DOI=10.1021/bi900166y;
Tsai S.J., Sen U., Zhao L., Greenleaf W.B., Dasgupta J., Fiorillo E.,
Orru V., Bottini N., Chen X.S.;
"Crystal structure of the human lymphoid tyrosine phosphatase
catalytic domain: insights into redox regulation.";
Biochemistry 48:4838-4845(2009).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-302, AND FUNCTION.
PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
"Large-scale structural analysis of the classical human protein
tyrosine phosphatome.";
Cell 136:352-363(2009).
[18]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 2-309 OF WILD TYPE AND
VARIANT GLN-263, VARIANT GLN-263, CATALYTIC ACTIVITY, AND
CHARACTERIZATION OF VARIANT GLN-263.
PubMed=18981062; DOI=10.1093/hmg/ddn363;
Orru V., Tsai S.J., Rueda B., Fiorillo E., Stanford S.M., Dasgupta J.,
Hartiala J., Zhao L., Ortego-Centeno N., D'Alfonso S., Arnett F.C.,
Wu H., Gonzalez-Gay M.A., Tsao B.P., Pons-Estel B.,
Alarcon-Riquelme M.E., He Y., Zhang Z.Y., Allayee H., Chen X.S.,
Martin J., Bottini N., Danieli M.G., Galeazzi M., Sabbadini M.G.,
Migliaresi S., Sebastiani G.D.;
"A loss-of-function variant of PTPN22 is associated with reduced risk
of systemic lupus erythematosus.";
Hum. Mol. Genet. 18:569-579(2009).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH
SUBSTRATE.
Seidel R.D., Love J., Piserchio A., Cowburn D.;
"Lyp/PTPN22 phosphatase domain: substrate recognition and specificity
for Src family kinases.";
Submitted (DEC-2009) to the PDB data bank.
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE
AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, AND
FUNCTION.
PubMed=21719704; DOI=10.1074/jbc.M111.254722;
Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S.,
Imasaki T., Takagi Y., Zhang Z.Y.;
"Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp)
and identification of Src kinase-associated protein of 55 kDa homolog
(SKAP-HOM) as a Lyp substrate.";
J. Biol. Chem. 286:30526-30534(2011).
[21]
VARIANT RA TRP-620, INTERACTION WITH CSK, AND TISSUE SPECIFICITY.
PubMed=15208781; DOI=10.1086/422827;
Begovich A.B., Carlton V.E., Honigberg L.A., Schrodi S.J.,
Chokkalingam A.P., Alexander H.C., Ardlie K.G., Huang Q., Smith A.M.,
Spoerke J.M., Conn M.T., Chang M., Chang S.Y., Saiki R.K.,
Catanese J.J., Leong D.U., Garcia V.E., McAllister L.B., Jeffery D.A.,
Lee A.T., Batliwalla F., Remmers E., Criswell L.A., Seldin M.F.,
Kastner D.L., Amos C.I., Sninsky J.J., Gregersen P.K.;
"A missense single-nucleotide polymorphism in a gene encoding a
protein tyrosine phosphatase (PTPN22) is associated with rheumatoid
arthritis.";
Am. J. Hum. Genet. 75:330-337(2004).
[22]
VARIANT SLE TRP-620.
PubMed=15273934; DOI=10.1086/423790;
Kyogoku C., Langefeld C.D., Ortmann W.A., Lee A., Selby S.,
Carlton V.E.H., Chang M., Ramos P., Baechler E.C., Batliwalla F.M.,
Novitzke J., Williams A.H., Gillett C., Rodine P., Graham R.R.,
Ardlie K.G., Gaffney P.M., Moser K.L., Petri M., Begovich A.B.,
Gregersen P.K., Behrens T.W.;
"Genetic association of the R620W polymorphism of protein tyrosine
phosphatase PTPN22 with human SLE.";
Am. J. Hum. Genet. 75:504-507(2004).
[23]
VARIANT IDDM TRP-620, AND CHARACTERIZATION OF VARIANT IDDM TRP-620.
PubMed=15004560; DOI=10.1038/ng1323;
Bottini N., Musumeci L., Alonso A., Rahmouni S., Nika K.,
Rostamkhani M., MacMurray J., Meloni G.F., Lucarelli P.,
Pellecchia M., Eisenbarth G.S., Comings D., Mustelin T.;
"A functional variant of lymphoid tyrosine phosphatase is associated
with type I diabetes.";
Nat. Genet. 36:337-338(2004).
[24]
INVOLVEMENT IN GRAVES DISEASE, INVOLVEMENT IN ADDISON DISEASE, AND
VARIANT TRP-620.
PubMed=15531553; DOI=10.1210/jc.2004-1108;
Velaga M.R., Wilson V., Jennings C.E., Owen C.J., Herington S.,
Donaldson P.T., Ball S.G., James R.A., Quinton R., Perros P.,
Pearce S.H.;
"The codon 620 tryptophan allele of the lymphoid tyrosine phosphatase
(LYP) gene is a major determinant of Graves' disease.";
J. Clin. Endocrinol. Metab. 89:5862-5865(2004).
[25]
INVOLVEMENT IN HASHIMOTO THYROIDITIS, AND VARIANT TRP-620.
PubMed=15719322; DOI=10.1086/429096;
Criswell L.A., Pfeiffer K.A., Lum R.F., Gonzales B., Novitzke J.,
Kern M., Moser K.L., Begovich A.B., Carlton V.E., Li W., Lee A.T.,
Ortmann W., Behrens T.W., Gregersen P.K.;
"Analysis of families in the multiple autoimmune disease genetics
consortium (MADGC) collection: the PTPN22 620W allele associates with
multiple autoimmune phenotypes.";
Am. J. Hum. Genet. 76:561-571(2005).
[26]
VARIANT VTLG TRP-620.
PubMed=16015369; DOI=10.1038/sj.gene.6364243;
Canton I., Akhtar S., Gavalas N.G., Gawkrodger D.J., Blomhoff A.,
Watson P.F., Weetman A.P., Kemp E.H.;
"A single-nucleotide polymorphism in the gene encoding lymphoid
protein tyrosine phosphatase (PTPN22) confers susceptibility to
generalised vitiligo.";
Genes Immun. 6:584-587(2005).
[27]
VARIANT TRP-620, AND CHARACTERIZATION OF VARIANT TRP-620.
PubMed=19265110; DOI=10.4049/jimmunol.0713370;
Arechiga A.F., Habib T., He Y., Zhang X., Zhang Z.Y., Funk A.,
Buckner J.H.;
"Cutting edge: the PTPN22 allelic variant associated with autoimmunity
impairs B cell signaling.";
J. Immunol. 182:3343-3347(2009).
[28]
VARIANTS GLN-263 AND TRP-620, AND CHARACTERIZATION OF VARIANTS GLN-263
AND TRP-620.
PubMed=21287672; DOI=10.1002/ibd.21630;
Diaz-Gallo L.M., Espino-Paisan L., Fransen K., Gomez-Garcia M.,
van Sommeren S., Cardena C., Rodrigo L., Mendoza J.L., Taxonera C.,
Nieto A., Alcain G., Cueto I., Lopez-Nevot M.A., Bottini N.,
Barclay M.L., Crusius J.B., van Bodegraven A.A., Wijmenga C.,
Ponsioen C.Y., Gearry R.B., Roberts R.L., Weersma R.K., Urcelay E.,
Merriman T.R., Alizadeh B.Z., Martin J.;
"Differential association of two PTPN22 coding variants with Crohn's
disease and ulcerative colitis.";
Inflamm. Bowel Dis. 17:2287-2294(2011).
[29]
VARIANTS PHE-201; GLN-263 AND TRP-266, AND CHARACTERIZATION OF
VARIANTS PHE-201; GLN-263 AND TRP-266.
PubMed=22952725; DOI=10.1371/journal.pone.0043631;
Liu J., Chen M., Li R., Yang F., Shi X., Zhu L., Wang H.M., Yao W.,
Liu Q., Meng F.G., Sun J.P., Pang Q., Yu X.;
"Biochemical and functional studies of lymphoid-specific tyrosine
phosphatase (Lyp) variants S201F and R266W.";
PLoS ONE 7:E43631-E43631(2012).
-!- 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 (PubMed:16461343,
PubMed:18056643). Associates with and probably dephosphorylates
CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue
(PubMed:21719704). Dephosphorylates ZAP70 at its activating 'Tyr-
493' residue (PubMed:16461343). Dephosphorylates the immune system
activator SKAP2 (PubMed:21719704). Positively regulates toll-like
receptor (TLR)-induced type 1 interferon production
(PubMed:23871208). Promotes host antiviral responses mediated by
type 1 interferon (By similarity). Regulates NOD2-induced pro-
inflammatory cytokine secretion and autophagy (PubMed:23991106).
{ECO:0000250|UniProtKB:P29352, ECO:0000269|PubMed:16461343,
ECO:0000269|PubMed:18056643, ECO:0000269|PubMed:19167335,
ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:23871208,
ECO:0000269|PubMed:23991106}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:21719704}.
-!- ENZYME REGULATION: Down-regulated by phosphorylation.
-!- SUBUNIT: Interacts with CSK (PubMed:15208781). Interacts with LPXN
(By similarity). Interacts with CBL (PubMed:10068674). Interacts
with TRAF3 (via MATH domain); the interaction promotes TRAF3
polyubiquitination (PubMed:23871208).
{ECO:0000250|UniProtKB:P29352, ECO:0000269|PubMed:10068674,
ECO:0000269|PubMed:15208781, ECO:0000269|PubMed:18056643,
ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:23871208,
ECO:0000269|Ref.19}.
-!- INTERACTION:
P20963:CD247; NbExp=4; IntAct=EBI-1211241, EBI-1165705;
P00533:EGFR; NbExp=2; IntAct=EBI-1211241, EBI-297353;
P62993:GRB2; NbExp=2; IntAct=EBI-1211241, EBI-401755;
P06239:LCK; NbExp=6; IntAct=EBI-1211241, EBI-1348;
O43586:PSTPIP1; NbExp=6; IntAct=EBI-1211241, EBI-1050964;
O75563:SKAP2; NbExp=3; IntAct=EBI-1211241, EBI-2483161;
Q3UND0:Skap2 (xeno); NbExp=2; IntAct=EBI-1211241, EBI-642769;
Q13114:TRAF3; NbExp=2; IntAct=EBI-1211241, EBI-357631;
Q60803:Traf3 (xeno); NbExp=5; IntAct=EBI-1211241, EBI-520135;
P43403:ZAP70; NbExp=4; IntAct=EBI-1211241, EBI-1211276;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=LyP1;
IsoId=Q9Y2R2-1; Sequence=Displayed;
Name=2; Synonyms=LyP2;
IsoId=Q9Y2R2-2; Sequence=VSP_005134;
Note=Due to intron retention.;
Name=3;
IsoId=Q9Y2R2-3; Sequence=VSP_039728;
Note=No experimental confirmation available.;
Name=4; Synonyms=LYP3;
IsoId=Q9Y2R2-4; Sequence=VSP_039729;
Name=5;
IsoId=Q9Y2R2-5; Sequence=VSP_039725, VSP_039726, VSP_039727;
Note=No experimental confirmation available.;
Name=6; Synonyms=PTPN22.6;
IsoId=Q9Y2R2-6; Sequence=VSP_044428, VSP_044429;
Note=Lacks most of the phosphatase domain and functions as a
dominant negative isoform of the full length PTPN22.;
-!- TISSUE SPECIFICITY: Expressed in bone marrow, B and T-cells,
PBMCs, natural killer cells, monocytes, dendritic cells and
neutrophils (PubMed:15208781). Both isoform 1 and 4 are
predominantly expressed in lymphoid tissues and cells. Isoform 1
is expressed in thymocytes and both mature B and T-cells.
{ECO:0000269|PubMed:15208781}.
-!- INDUCTION: By muramyl-dipeptide and lipopolysaccharide.
{ECO:0000269|PubMed:23991106}.
-!- PTM: Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability
to dephosphorylate and inactivate the SRC family kinases.
{ECO:0000269|PubMed:18056643}.
-!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A
chronic, relapsing, inflammatory, and often febrile multisystemic
disorder of connective tissue, characterized principally by
involvement of the skin, joints, kidneys and serosal membranes. It
is of unknown etiology, but is thought to represent a failure of
the regulatory mechanisms of the autoimmune system. The disease is
marked by a wide range of system dysfunctions, an elevated
erythrocyte sedimentation rate, and the formation of LE cells in
the blood or bone marrow. {ECO:0000269|PubMed:15273934}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, insulin-dependent (IDDM) [MIM:222100]:
A multifactorial disorder of glucose homeostasis that is
characterized by susceptibility to ketoacidosis in the absence of
insulin therapy. Clinical features are polydipsia, polyphagia and
polyuria which result from hyperglycemia-induced osmotic diuresis
and secondary thirst. These derangements result in long-term
complications that affect the eyes, kidneys, nerves, and blood
vessels. {ECO:0000269|PubMed:15004560}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Rheumatoid arthritis (RA) [MIM:180300]: An inflammatory
disease with autoimmune features and a complex genetic component.
It primarily affects the joints and is characterized by
inflammatory changes in the synovial membranes and articular
structures, widespread fibrinoid degeneration of the collagen
fibers in mesenchymal tissues, and by atrophy and rarefaction of
bony structures. {ECO:0000269|PubMed:15208781}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Vitiligo (VTLG) [MIM:193200]: A pigmentary disorder of
the skin and mucous membranes. It is characterized by
circumscribed depigmented macules and patches, commonly on
extensor aspects of extremities, on the face or neck and in skin
folds. Vitiligo is a progressive disorder in which some or all of
the melanocytes in the affected skin are selectively destroyed. It
is a multifactorial disorder with a complex etiology probably
including autoimmune mechanisms, and is associated with an
elevated risk of other autoimmune diseases.
{ECO:0000269|PubMed:16015369}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF001846; AAD00904.1; -; mRNA.
EMBL; AF001847; AAD00905.1; -; mRNA.
EMBL; GU479452; ADD59979.1; -; mRNA.
EMBL; AF077031; AAD27764.1; -; mRNA.
EMBL; AK310570; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; EF064714; ABK41897.1; -; Genomic_DNA.
EMBL; AL137856; CAI19068.1; -; Genomic_DNA.
EMBL; CH471122; EAW56575.1; -; Genomic_DNA.
EMBL; CH471122; EAW56576.1; -; Genomic_DNA.
EMBL; BC017785; AAH17785.1; -; mRNA.
EMBL; BC071670; AAH71670.1; -; mRNA.
CCDS; CCDS863.1; -. [Q9Y2R2-1]
CCDS; CCDS864.2; -. [Q9Y2R2-3]
RefSeq; NP_001180360.1; NM_001193431.2. [Q9Y2R2-4]
RefSeq; NP_001295226.1; NM_001308297.1.
RefSeq; NP_036543.4; NM_012411.5. [Q9Y2R2-3]
RefSeq; NP_057051.3; NM_015967.6. [Q9Y2R2-1]
UniGene; Hs.535276; -.
PDB; 2P6X; X-ray; 1.90 A; A/B=1-302.
PDB; 2QCJ; X-ray; 3.00 A; A/B=1-294.
PDB; 2QCT; X-ray; 2.80 A; A/B=1-294.
PDB; 3BRH; X-ray; 2.20 A; A/B=1-310.
PDB; 3H2X; X-ray; 2.20 A; A=1-302.
PDB; 3OLR; X-ray; 2.50 A; A/B/C/D=1-294.
PDB; 3OMH; X-ray; 2.90 A; A/B/C/D=1-294.
PDB; 4J51; X-ray; 2.30 A; A/B=1-303.
PDBsum; 2P6X; -.
PDBsum; 2QCJ; -.
PDBsum; 2QCT; -.
PDBsum; 3BRH; -.
PDBsum; 3H2X; -.
PDBsum; 3OLR; -.
PDBsum; 3OMH; -.
PDBsum; 4J51; -.
ProteinModelPortal; Q9Y2R2; -.
SMR; Q9Y2R2; -.
BioGrid; 117604; 46.
DIP; DIP-29953N; -.
IntAct; Q9Y2R2; 24.
STRING; 9606.ENSP00000352833; -.
BindingDB; Q9Y2R2; -.
ChEMBL; CHEMBL2889; -.
DEPOD; Q9Y2R2; -.
iPTMnet; Q9Y2R2; -.
PhosphoSitePlus; Q9Y2R2; -.
BioMuta; PTPN22; -.
DMDM; 20139861; -.
PaxDb; Q9Y2R2; -.
PeptideAtlas; Q9Y2R2; -.
PRIDE; Q9Y2R2; -.
DNASU; 26191; -.
Ensembl; ENST00000460620; ENSP00000433141; ENSG00000134242. [Q9Y2R2-5]
GeneID; 26191; -.
KEGG; hsa:26191; -.
UCSC; uc001edt.4; human. [Q9Y2R2-1]
CTD; 26191; -.
DisGeNET; 26191; -.
EuPathDB; HostDB:ENSG00000134242.15; -.
GeneCards; PTPN22; -.
HGNC; HGNC:9652; PTPN22.
HPA; CAB012209; -.
HPA; HPA004912; -.
HPA; HPA013350; -.
MalaCards; PTPN22; -.
MIM; 152700; phenotype.
MIM; 180300; phenotype.
MIM; 193200; phenotype.
MIM; 222100; phenotype.
MIM; 600716; gene.
neXtProt; NX_Q9Y2R2; -.
OpenTargets; ENSG00000134242; -.
Orphanet; 397; Giant cell arteritis.
Orphanet; 900; Granulomatosis with polyangiitis.
Orphanet; 85408; Juvenile rheumatoid factor-negative polyarthritis.
Orphanet; 85410; Oligoarticular juvenile arthritis.
Orphanet; 93552; Pediatric systemic lupus erythematosus.
Orphanet; 536; Systemic lupus erythematosus.
Orphanet; 3437; Vogt-Koyanagi-Harada disease.
PharmGKB; PA33995; -.
eggNOG; KOG0789; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00900000140780; -.
HOVERGEN; HBG103877; -.
InParanoid; Q9Y2R2; -.
KO; K18024; -.
PhylomeDB; Q9Y2R2; -.
TreeFam; TF351977; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
SignaLink; Q9Y2R2; -.
SIGNOR; Q9Y2R2; -.
ChiTaRS; PTPN22; human.
EvolutionaryTrace; Q9Y2R2; -.
GeneWiki; PTPN22; -.
GenomeRNAi; 26191; -.
PRO; PR:Q9Y2R2; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134242; -.
CleanEx; HS_PTPN22; -.
ExpressionAtlas; Q9Y2R2; baseline and differential.
Genevisible; Q9Y2R2; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0019900; F:kinase binding; ISS:BHF-UCL.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
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; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
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; IMP:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0035644; P:phosphoanandamide dephosphorylation; ISS:BHF-UCL.
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:1902715; P:positive regulation of interferon-gamma secretion; 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:0032481; P:positive regulation of type I interferon production; IMP:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; NAS:BHF-UCL.
GO; GO:0045088; P:regulation of innate immune response; IC:BHF-UCL.
GO; GO:0032817; P:regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:BHF-UCL.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
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; Alternative splicing; Autophagy; Complete proteome;
Cytoplasm; Diabetes mellitus; Disease mutation; Disulfide bond;
Hydrolase; Immunity; Phosphoprotein; Polymorphism;
Protein phosphatase; Reference proteome; Systemic lupus erythematosus.
CHAIN 1 807 Tyrosine-protein phosphatase non-receptor
type 22.
/FTId=PRO_0000094775.
DOMAIN 24 289 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 227 233 Substrate binding.
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:0000269|Ref.19}.
MOD_RES 35 35 Phosphoserine; by PKC/PRKCD.
{ECO:0000269|PubMed:18056643}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000250|UniProtKB:P29352}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:P29352}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000250|UniProtKB:P29352}.
DISULFID 129 227 {ECO:0000269|PubMed:19371084}.
VAR_SEQ 124 250 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044428.
VAR_SEQ 137 160 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039725.
VAR_SEQ 181 203 ETRTIYQFHYKNWPDHDVPSSID -> VSVILAHQTSLQNL
FSQITPAHF (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039726.
VAR_SEQ 204 807 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039727.
VAR_SEQ 251 305 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039728.
VAR_SEQ 647 674 Missing (in isoform 4).
{ECO:0000303|PubMed:21044313}.
/FTId=VSP_039729.
VAR_SEQ 685 807 ELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIETYSTSY
PDTMENSTSSKQTLKTPGKSFTRSKSLKILRNMKKSICNSC
PPNKPAESVQSNNSSSFLNFGFANRFSKPKGPRNPPPTWNI
-> GKNFSWL (in isoform 2).
{ECO:0000303|PubMed:10068674}.
/FTId=VSP_005134.
VAR_SEQ 788 807 FANRFSKPKGPRNPPPTWNI -> MCVILLKS (in
isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044429.
VARIANT 201 201 S -> F (polymorphism; moderately reduces
phosphatase activity; dbSNP:rs7416347).
{ECO:0000269|PubMed:22952725}.
/FTId=VAR_072629.
VARIANT 263 263 R -> Q (polymorphism; reduces risk of SLE
and RA but not IDDM; associated with
reduced risk of ulcerative colitis but
not of Crohn disease; severely reduces
phosphatase activity; dbSNP:rs33996649).
{ECO:0000269|PubMed:18981062,
ECO:0000269|PubMed:21287672,
ECO:0000269|PubMed:22952725}.
/FTId=VAR_072630.
VARIANT 266 266 R -> W (polymorphism; severely reduces
phosphatase activity; dbSNP:rs72650670).
{ECO:0000269|PubMed:22952725}.
/FTId=VAR_072631.
VARIANT 620 620 R -> W (in IDDM, RA, SLE and VTLG; also
found in patients with Graves disease,
Hashimoto thyroiditis and Addison
disease; associated with reduced risk of
Crohn disease but not of ulcerative
colitis; affects CSK kinase binding;
alters B cell receptor signaling and
memory B cell proliferation;
dbSNP:rs2476601).
{ECO:0000269|PubMed:15004560,
ECO:0000269|PubMed:15208781,
ECO:0000269|PubMed:15273934,
ECO:0000269|PubMed:15531553,
ECO:0000269|PubMed:15719322,
ECO:0000269|PubMed:16015369,
ECO:0000269|PubMed:16710414,
ECO:0000269|PubMed:19265110,
ECO:0000269|PubMed:21044313,
ECO:0000269|PubMed:21287672,
ECO:0000269|Ref.3, ECO:0000269|Ref.7}.
/FTId=VAR_022605.
MUTAGEN 35 35 S->E: Loss of phosphorylation by
PKC/PRKCD. {ECO:0000269|PubMed:18056643}.
MUTAGEN 36 36 T->E: No effect on phosphorylation by
PKC/PRKCD. {ECO:0000269|PubMed:18056643}.
MUTAGEN 129 129 C->S: Decreases activity 2 fold.
{ECO:0000269|PubMed:19371084}.
MUTAGEN 231 231 C->S: Decreases activity 7 fold.
{ECO:0000269|PubMed:19371084}.
CONFLICT 51 52 KP -> NA (in Ref. 1; AAD00904/AAD00905).
{ECO:0000305}.
CONFLICT 126 126 V -> G (in Ref. 2; AAD27764).
{ECO:0000305}.
CONFLICT 147 147 G -> V (in Ref. 2; AAD27764).
{ECO:0000305}.
CONFLICT 240 240 I -> IV (in Ref. 1; AAD00905).
{ECO:0000305}.
CONFLICT 372 372 A -> V (in Ref. 4; AK310570).
{ECO:0000305}.
CONFLICT 420 420 L -> P (in Ref. 2; AAD27764).
{ECO:0000305}.
CONFLICT 742 742 P -> S (in Ref. 2; AAD27764).
{ECO:0000305}.
HELIX 3 16 {ECO:0000244|PDB:2P6X}.
HELIX 21 40 {ECO:0000244|PDB:2P6X}.
HELIX 47 50 {ECO:0000244|PDB:2P6X}.
HELIX 52 55 {ECO:0000244|PDB:2P6X}.
STRAND 59 62 {ECO:0000244|PDB:3OMH}.
HELIX 67 69 {ECO:0000244|PDB:2P6X}.
STRAND 70 72 {ECO:0000244|PDB:4J51}.
TURN 80 83 {ECO:0000244|PDB:4J51}.
STRAND 86 92 {ECO:0000244|PDB:2P6X}.
STRAND 95 102 {ECO:0000244|PDB:2P6X}.
HELIX 107 109 {ECO:0000244|PDB:2P6X}.
HELIX 110 119 {ECO:0000244|PDB:2P6X}.
STRAND 124 127 {ECO:0000244|PDB:2P6X}.
STRAND 131 133 {ECO:0000244|PDB:2P6X}.
STRAND 135 137 {ECO:0000244|PDB:3BRH}.
STRAND 146 148 {ECO:0000244|PDB:2QCJ}.
STRAND 151 153 {ECO:0000244|PDB:2P6X}.
STRAND 156 165 {ECO:0000244|PDB:2P6X}.
STRAND 167 178 {ECO:0000244|PDB:2P6X}.
STRAND 181 190 {ECO:0000244|PDB:2P6X}.
STRAND 195 197 {ECO:0000244|PDB:2QCJ}.
HELIX 199 202 {ECO:0000244|PDB:2P6X}.
HELIX 203 215 {ECO:0000244|PDB:2P6X}.
STRAND 218 221 {ECO:0000244|PDB:3BRH}.
STRAND 223 226 {ECO:0000244|PDB:2P6X}.
STRAND 228 232 {ECO:0000244|PDB:2P6X}.
HELIX 233 248 {ECO:0000244|PDB:2P6X}.
HELIX 258 266 {ECO:0000244|PDB:2P6X}.
HELIX 276 301 {ECO:0000244|PDB:2P6X}.
SEQUENCE 807 AA; 91705 MW; 1ABE8AE89C9D9FBF CRC64;
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE KPKNIKKNRY
KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI ATQGPLSTTL LDFWRMIWEY
SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS
ETRTIYQFHY KNWPDHDVPS SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI
DYTWMLLKDG IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK
HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE SSSFDFRTSE
ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK AFPIVGEPLQ KHQSLDLGSL
LFEGCSNSKP VNAAGRYFNS KVPITRTKST PFELIQQRET KEVDSKENFS YLESQPHDSC
FVEMQAQKVM HVSSAELNYS LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW
PPSGTSSKMS LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES
AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI GTSLEWGGTS
EPKKFDDSVI LRPSKSVKLR SPKSELHQDR SSPPPPLPER TLESFFLADE DCMQAQSIET
YSTSYPDTME NSTSSKQTLK TPGKSFTRSK SLKILRNMKK SICNSCPPNK PAESVQSNNS
SSFLNFGFAN RFSKPKGPRN PPPTWNI


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10-782-55087 Tyrosine-protein phosphatase non-receptor type 7 - EC 3.1.3.48; Protein-tyrosine phosphatase LC-PTP; Hematopoietic protein-tyrosine phosphatase; HEPTP N_A 0.02 mg
10-782-55087 Tyrosine-protein phosphatase non-receptor type 7 - EC 3.1.3.48; Protein-tyrosine phosphatase LC-PTP; Hematopoietic protein-tyrosine phosphatase; HEPTP N_A 0.01 mg
10-782-55087 Tyrosine-protein phosphatase non-receptor type 7 - EC 3.1.3.48; Protein-tyrosine phosphatase LC-PTP; Hematopoietic protein-tyrosine phosphatase; HEPTP N_A 0.005 mg
10-782-55087 Tyrosine-protein phosphatase non-receptor type 7 - EC 3.1.3.48; Protein-tyrosine phosphatase LC-PTP; Hematopoietic protein-tyrosine phosphatase; HEPTP N_A 0.001 mg
EIAAB33117 FMI,Homo sapiens,hPTP-J,Human,Pancreatic carcinoma phosphatase 2,PCP2,PCP-2,Protein-tyrosine phosphatase J,Protein-tyrosine phosphatase pi,Protein-tyrosine phosphatase receptor omicron,PTP pi,PTP-J,PT
EIAAB33023 Homo sapiens,Human,Protein-tyrosine phosphatase G1,PTPG1,PTPN12,PTP-PEST,Tyrosine-protein phosphatase non-receptor type 12
EIAAB33024 Mouse,MPTP-PEST,Mus musculus,P19-PTP,Protein-tyrosine phosphatase P19,Ptpn12,Tyrosine-protein phosphatase non-receptor type 12
EIAAB33044 HD-PTP,His domain-containing protein tyrosine phosphatase,Homo sapiens,Human,KIAA1471,Protein tyrosine phosphatase TD14,PTPN23,PTP-TD14,Tyrosine-protein phosphatase non-receptor type 23


 

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