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Tyrosine-protein kinase JAK3 (EC 2.7.10.2) (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) (L-JAK)

 JAK3_HUMAN              Reviewed;        1124 AA.
P52333; Q13259; Q13260; Q13611; Q8N1E8; Q99699; Q9Y6S2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
22-NOV-2017, entry version 197.
RecName: Full=Tyrosine-protein kinase JAK3;
EC=2.7.10.2;
AltName: Full=Janus kinase 3;
Short=JAK-3;
AltName: Full=Leukocyte janus kinase;
Short=L-JAK;
Name=JAK3;
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 2).
PubMed=8022790; DOI=10.1073/pnas.91.14.6374;
Kawamura M., McVicar D.W., Johnston J.A., Blake T.B., Chen Y.-Q.,
Lal B.K., Lloyd A.R., Kelvin D.J., Staples J.E., Ortaldo J.R.,
O'Shea J.J.;
"Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase
expressed in natural killer cells and activated leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 91:6374-6378(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING
(ISOFORM 2).
PubMed=7559633; DOI=10.1074/jbc.270.42.25028;
Lai K.S., Jin Y., Graham D.K., Witthuhn B.A., Ihle J.N., Liu E.T.;
"A kinase-deficient splice variant of the human JAK3 is expressed in
hematopoietic and epithelial cancer cells.";
J. Biol. Chem. 270:25028-25036(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8921370; DOI=10.1006/geno.1996.0520;
Riedy M.C., Dutra A.S., Blake T.B., Modi W., Lal B.K., Davis J.,
Bosse A., O'Shea J.J., Johnston J.A.;
"Genomic sequence, organization, and chromosomal localization of human
JAK3.";
Genomics 37:57-61(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-132 AND ILE-722.
SeattleSNPs variation discovery resource;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Blood;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-191.
PubMed=8662778; DOI=10.1074/jbc.271.24.13976;
Verbsky J.W., Bach E.A., Fang Y.F., Yang L., Randolph D.A.,
Fields L.E.;
"Expression of Janus kinase 3 in human endothelial and other non-
lymphoid and non-myeloid cells.";
J. Biol. Chem. 271:13976-13980(1996).
[9]
FUNCTION IN IL2 SIGNALING PATHWAY.
PubMed=8022485; DOI=10.1038/370151a0;
Johnston J.A., Kawamura M., Kirken R.A., Chen Y.Q., Blake T.B.,
Shibuya K., Ortaldo J.R., McVicar D.W., O'Shea J.J.;
"Phosphorylation and activation of the Jak-3 Janus kinase in response
to interleukin-2.";
Nature 370:151-153(1994).
[10]
FUNCTION IN IL7 SIGNALING PATHWAY.
PubMed=7662955;
Sharfe N., Dadi H.K., Roifman C.M.;
"JAK3 protein tyrosine kinase mediates interleukin-7-induced
activation of phosphatidylinositol-3' kinase.";
Blood 86:2077-2085(1995).
[11]
TISSUE SPECIFICITY.
PubMed=7535338; DOI=10.1084/jem.181.4.1425;
Musso T., Johnston J.A., Linnekin D., Varesio L., Rowe T.K.,
O'Shea J.J., McVicar D.W.;
"Regulation of JAK3 expression in human monocytes: phosphorylation in
response to interleukins 2, 4, and 7.";
J. Exp. Med. 181:1425-1431(1995).
[12]
INTERACTION WITH STAM2.
TISSUE=Fetal brain;
PubMed=10899310; DOI=10.1016/S0014-5793(00)01760-9;
Endo K., Takeshita T., Kasai H., Sasaki Y., Tanaka N., Asao H.,
Kikuchi K., Yamada M., Chenb M., O'Shea J.J., Sugamura K.;
"STAM2, a new member of the STAM family, binding to the Janus
kinases.";
FEBS Lett. 477:55-61(2000).
[13]
INTERACTION WITH SHB.
PubMed=12200137; DOI=10.1016/S0006-291X(02)02016-8;
Lindholm C.K.;
"IL-2 receptor signaling through the Shb adapter protein in T and NK
cells.";
Biochem. Biophys. Res. Commun. 296:929-936(2002).
[14]
FUNCTION IN CYTOKINE SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION
AT TYR-980 AND TYR-981 BY PTPN2.
PubMed=11909529; DOI=10.1016/S0960-9822(02)00697-8;
Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.;
"The T cell protein tyrosine phosphatase is a negative regulator of
janus family kinases 1 and 3.";
Curr. Biol. 12:446-453(2002).
[15]
DOMAIN.
PubMed=12351625; DOI=10.1074/jbc.M205156200;
Saharinen P., Silvennoinen O.;
"The pseudokinase domain is required for suppression of basal activity
of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible
activation of signal transduction.";
J. Biol. Chem. 277:47954-47963(2002).
[16]
PHOSPHORYLATION AT TYR-785, AND MUTAGENESIS OF TYR-785.
PubMed=15121872; DOI=10.1128/MCB.24.10.4557-4570.2004;
Kurzer J.H., Argetsinger L.S., Zhou Y.J., Kouadio J.L., O'Shea J.J.,
Carter-Su C.;
"Tyrosine 813 is a site of JAK2 autophosphorylation critical for
activation of JAK2 by SH2-B beta.";
Mol. Cell. Biol. 24:4557-4570(2004).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[18]
PHOSPHORYLATION AT TYR-904 AND TYR-939, AND MUTAGENESIS OF LYS-855;
TYR-904 AND TYR-939.
PubMed=18250158; DOI=10.1128/MCB.01789-07;
Cheng H., Ross J.A., Frost J.A., Kirken R.A.;
"Phosphorylation of human Jak3 at tyrosines 904 and 939 positively
regulates its activity.";
Mol. Cell. Biol. 28:2271-2282(2008).
[19]
REVIEW ON FUNCTION.
PubMed=19290934; DOI=10.1111/j.1600-065X.2008.00754.x;
Ghoreschi K., Laurence A., O'Shea J.J.;
"Janus kinases in immune cell signaling.";
Immunol. Rev. 228:273-287(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
FUNCTION IN IL15 SIGNALING PATHWAY.
PubMed=20440074; DOI=10.1172/JCI41344;
Malamut G., El Machhour R., Montcuquet N., Martin-Lanneree S.,
Dusanter-Fourt I., Verkarre V., Mention J.J., Rahmi G., Kiyono H.,
Butz E.A., Brousse N., Cellier C., Cerf-Bensussan N., Meresse B.;
"IL-15 triggers an antiapoptotic pathway in human intraepithelial
lymphocytes that is a potential new target in celiac disease-
associated inflammation and lymphomagenesis.";
J. Clin. Invest. 120:2131-2143(2010).
[23]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 814-1103 IN COMPLEX WITH
STAUROSPORINE ANALOG AFN941, AND PHOSPHORYLATION AT TYR-980 AND
TYR-981.
PubMed=15831699; DOI=10.1182/blood-2005-02-0707;
Boggon T.J., Li Y., Manley P.W., Eck M.J.;
"Crystal structure of the Jak3 kinase domain in complex with a
staurosporine analog.";
Blood 106:996-1002(2005).
[24]
VARIANT T(-)B(+)NK(-) SCID CYS-100.
PubMed=7659163; DOI=10.1038/377065a0;
Macchi P., Villa A., Giliani S., Sacco M.G., Frattini A., Porta F.,
Ugazio A.G., Johnston J.A., Candotti F., O'Shea J.J., Vezzoni P.,
Notarangelo L.D.;
"Mutations of Jak-3 gene in patients with autosomal severe combined
immune deficiency (SCID).";
Nature 377:65-68(1995).
[25]
VARIANTS T(-)B(+)NK(-) SCID GLY-481; 586-LEU--MET-592 DEL AND ARG-759.
PubMed=9354668;
Candotti F., Oakes S.A., Johnston J.A., Giliani S., Schumacher R.F.,
Mella P., Fiorini M., Ugazio A.G., Badolato R., Notarangelo L.D.,
Bozzi F., Macchi P., Strina D., Vezzoni P., Blaese R.M., O'Shea J.J.,
Villa A.;
"Structural and functional basis for JAK3-deficient severe combined
immunodeficiency.";
Blood 90:3996-4003(1997).
[26]
VARIANT T(-)B(+)NK(-) SCID TRP-582.
PubMed=9753072; DOI=10.1111/j.1365-2141.1998.tb08990.x;
Bozzi F., Lefranc G., Villa A., Badolato R., Schumacher R.F.,
Khalil G., Loiselet J., Bresciani S., O'Shea J.J., Vezzoni P.,
Notarangelo L.D., Candotti F.;
"Molecular and biochemical characterization of JAK3 deficiency in a
patient with severe combined immunodeficiency over 20 years after bone
marrow transplantation: implications for treatment.";
Br. J. Haematol. 102:1363-1366(1998).
[27]
VARIANTS T(-)B(+)NK(-) SCID ARG-151 AND SER-910, AND VARIANT ILE-722.
PubMed=10982185; DOI=10.1007/s004390051012;
Schumacher R.F., Mella P., Badolato R., Fiorini M., Savoldi G.,
Giliani S., Villa A., Candotti F., Tampalini A., O'Shea J.J.,
Notarangelo L.D.;
"Complete genomic organization of the human JAK3 gene and mutation
analysis in severe combined immunodeficiency by single-strand
conformation polymorphism.";
Hum. Genet. 106:73-79(2000).
[28]
VARIANTS T(-)B(+)NK(-) SCID ALA-58 DEL; GLU-169 AND SER-589, AND
VARIANT ILE-722.
PubMed=14615376; DOI=10.1182/blood-2003-06-2104;
Roberts J.L., Lengi A., Brown S.M., Chen M., Zhou Y.-J., O'Shea J.J.,
Buckley R.H.;
"Janus kinase 3 (JAK3) deficiency: clinical, immunologic, and
molecular analyses of 10 patients and outcomes of stem cell
transplantation.";
Blood 103:2009-2018(2004).
[29]
VARIANTS [LARGE SCALE ANALYSIS] LEU-12; HIS-40; THR-132; ARG-151;
VAL-521; PRO-527; PHE-688 AND ILE-722.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor tyrosine kinase involved in various
processes such as cell growth, development, or differentiation.
Mediates essential signaling events in both innate and adaptive
immunity and plays a crucial role in hematopoiesis during T-cells
development. In the cytoplasm, plays a pivotal role in signal
transduction via its association with type I receptors sharing the
common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and
IL21R. Following ligand binding to cell surface receptors,
phosphorylates specific tyrosine residues on the cytoplasmic tails
of the receptor, creating docking sites for STATs proteins.
Subsequently, phosphorylates the STATs proteins once they are
recruited to the receptor. Phosphorylated STATs then form
homodimer or heterodimers and translocate to the nucleus to
activate gene transcription. For example, upon IL2R activation by
IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma
chain (IL2RG) subunits inducing the tyrosine phosphorylation of
both receptor subunits on their cytoplasmic domain. Then, STAT5A
AND STAT5B are recruited, phosphorylated and activated by JAK1 and
JAK3. Once activated, dimerized STAT5 translocates to the nucleus
and promotes the transcription of specific target genes in a
cytokine-specific fashion. {ECO:0000269|PubMed:11909529,
ECO:0000269|PubMed:20440074, ECO:0000269|PubMed:7662955,
ECO:0000269|PubMed:8022485}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Interacts with STAM2 and MYO18A (By similarity).
Interacts with SHB. {ECO:0000250, ECO:0000269|PubMed:10899310,
ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:15831699}.
-!- INTERACTION:
Q07666:KHDRBS1; NbExp=2; IntAct=EBI-518246, EBI-1364;
Q9UNF1:MAGED2; NbExp=3; IntAct=EBI-518246, EBI-725832;
P55209:NAP1L1; NbExp=3; IntAct=EBI-518246, EBI-356392;
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2; Synonyms=JAK3S, Spleen-JAK3;
IsoId=P52333-1; Sequence=Displayed;
Name=1; Synonyms=JAK3B, Breast-JAK3;
IsoId=P52333-2; Sequence=VSP_004989;
Note=May be inactive as it lacks some part of the kinase
domain.;
Name=3;
IsoId=P52333-4; Sequence=VSP_054165, VSP_054166;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: In NK cells and an NK-like cell line but not
in resting T-cells or in other tissues. The S-form is more
commonly seen in hematopoietic lines, whereas the B-form is
detected in cells both of hematopoietic and epithelial origins.
{ECO:0000269|PubMed:7535338}.
-!- DOMAIN: Possesses two phosphotransferase domains. The second one
probably contains the catalytic domain (By similarity), while the
presence of slight differences suggest a different role for domain
1. {ECO:0000250, ECO:0000269|PubMed:12351625}.
-!- PTM: Tyrosine phosphorylated in response to IL-2 and IL-4.
Dephosphorylation of Tyr-980 and Tyr-981 by PTPN2 negatively
regulates cytokine-mediated signaling (Probable).
{ECO:0000305|PubMed:11909529, ECO:0000305|PubMed:15121872,
ECO:0000305|PubMed:15831699, ECO:0000305|PubMed:18250158}.
-!- DISEASE: Severe combined immunodeficiency autosomal recessive T-
cell-negative/B-cell-positive/NK-cell-negative (T(-)B(+)NK(-)
SCID) [MIM:600802]: A form of severe combined immunodeficiency
(SCID), a genetically and clinically heterogeneous group of rare
congenital disorders characterized by impairment of both humoral
and cell-mediated immunity, leukopenia, and low or absent antibody
levels. Patients present in infancy recurrent, persistent
infections by opportunistic organisms. The common characteristic
of all types of SCID is absence of T-cell-mediated cellular
immunity due to a defect in T-cell development.
{ECO:0000269|PubMed:10982185, ECO:0000269|PubMed:14615376,
ECO:0000269|PubMed:7659163, ECO:0000269|PubMed:9354668,
ECO:0000269|PubMed:9753072}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. JAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAC50227.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS. Was erroneously described as an isoform JAK3M while it is a fragmentary mRNA of INSL3.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JAK3ID41032ch19p13.html";
-!- WEB RESOURCE: Name=JAK3base; Note=JAK3 mutation db;
URL="http://structure.bmc.lu.se/idbase/JAK3base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/jak3/";
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EMBL; U09607; AAA19626.1; -; mRNA.
EMBL; U31601; AAC50226.1; -; mRNA.
EMBL; U31602; AAC50227.1; ALT_SEQ; mRNA.
EMBL; U70065; AAC50950.1; -; Genomic_DNA.
EMBL; AF513860; AAM44860.1; -; Genomic_DNA.
EMBL; AC007201; AAD22741.1; -; Genomic_DNA.
EMBL; CH471106; EAW84639.1; -; Genomic_DNA.
EMBL; BC028068; AAH28068.1; -; mRNA.
EMBL; U57096; AAC50542.1; -; mRNA.
CCDS; CCDS12366.1; -. [P52333-1]
PIR; A55747; A55747.
RefSeq; NP_000206.2; NM_000215.3. [P52333-1]
UniGene; Hs.515247; -.
PDB; 1YVJ; X-ray; 2.55 A; A=814-1103.
PDB; 3LXK; X-ray; 2.00 A; A=806-1124.
PDB; 3LXL; X-ray; 1.74 A; A=806-1124.
PDB; 3PJC; X-ray; 2.20 A; A=812-1124.
PDB; 3ZC6; X-ray; 2.42 A; A/B/C/D=813-1100.
PDB; 3ZEP; X-ray; 2.35 A; A/B/C/D=813-1047, A/B/C/D=813-1100.
PDB; 4HVD; X-ray; 1.85 A; A=811-1124.
PDB; 4HVG; X-ray; 2.75 A; A=811-1124.
PDB; 4HVH; X-ray; 2.30 A; A=811-1124.
PDB; 4HVI; X-ray; 2.40 A; A=811-1124.
PDB; 4I6Q; X-ray; 1.85 A; A=811-1124.
PDB; 4QPS; X-ray; 1.80 A; A/C=811-1103.
PDB; 4QT1; X-ray; 2.40 A; A=811-1124.
PDB; 4RIO; X-ray; 2.69 A; A=810-1100.
PDB; 4V0G; X-ray; 3.00 A; A/B=816-1098.
PDB; 4Z16; X-ray; 2.90 A; A/B/C/D=811-1124.
PDB; 5LWM; X-ray; 1.55 A; A=812-1103.
PDB; 5LWN; X-ray; 1.60 A; A=812-1103.
PDB; 5TOZ; X-ray; 1.98 A; A=812-1124.
PDB; 5TTS; X-ray; 2.34 A; A=812-1124.
PDB; 5TTU; X-ray; 1.72 A; A=812-1124.
PDB; 5TTV; X-ray; 1.93 A; A=812-1124.
PDB; 5VO6; X-ray; 2.65 A; A=812-1100.
PDB; 5W86; X-ray; 2.61 A; A/B/C/D=814-1100.
PDB; 5WFJ; X-ray; 2.48 A; A=810-1100.
PDBsum; 1YVJ; -.
PDBsum; 3LXK; -.
PDBsum; 3LXL; -.
PDBsum; 3PJC; -.
PDBsum; 3ZC6; -.
PDBsum; 3ZEP; -.
PDBsum; 4HVD; -.
PDBsum; 4HVG; -.
PDBsum; 4HVH; -.
PDBsum; 4HVI; -.
PDBsum; 4I6Q; -.
PDBsum; 4QPS; -.
PDBsum; 4QT1; -.
PDBsum; 4RIO; -.
PDBsum; 4V0G; -.
PDBsum; 4Z16; -.
PDBsum; 5LWM; -.
PDBsum; 5LWN; -.
PDBsum; 5TOZ; -.
PDBsum; 5TTS; -.
PDBsum; 5TTU; -.
PDBsum; 5TTV; -.
PDBsum; 5VO6; -.
PDBsum; 5W86; -.
PDBsum; 5WFJ; -.
ProteinModelPortal; P52333; -.
SMR; P52333; -.
BioGrid; 109921; 73.
DIP; DIP-274N; -.
IntAct; P52333; 50.
MINT; MINT-1497014; -.
STRING; 9606.ENSP00000391676; -.
BindingDB; P52333; -.
ChEMBL; CHEMBL2148; -.
DrugBank; DB08895; Tofacitinib.
GuidetoPHARMACOLOGY; 2049; -.
iPTMnet; P52333; -.
PhosphoSitePlus; P52333; -.
BioMuta; JAK3; -.
DMDM; 50403745; -.
MaxQB; P52333; -.
PaxDb; P52333; -.
PeptideAtlas; P52333; -.
PRIDE; P52333; -.
DNASU; 3718; -.
Ensembl; ENST00000458235; ENSP00000391676; ENSG00000105639. [P52333-1]
Ensembl; ENST00000527670; ENSP00000432511; ENSG00000105639. [P52333-1]
Ensembl; ENST00000534444; ENSP00000436421; ENSG00000105639. [P52333-2]
GeneID; 3718; -.
KEGG; hsa:3718; -.
UCSC; uc002nhn.5; human. [P52333-1]
CTD; 3718; -.
DisGeNET; 3718; -.
EuPathDB; HostDB:ENSG00000105639.18; -.
GeneCards; JAK3; -.
HGNC; HGNC:6193; JAK3.
HPA; HPA070314; -.
MalaCards; JAK3; -.
MIM; 600173; gene.
MIM; 600802; phenotype.
neXtProt; NX_P52333; -.
OpenTargets; ENSG00000105639; -.
Orphanet; 35078; T-B+ severe combined immunodeficiency due to JAK3 deficiency.
PharmGKB; PA29990; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140909; -.
HOGENOM; HOG000049158; -.
HOVERGEN; HBG006195; -.
InParanoid; P52333; -.
KO; K11218; -.
OMA; NCMESFL; -.
OrthoDB; EOG091G01IS; -.
PhylomeDB; P52333; -.
TreeFam; TF327041; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-451927; Interleukin-2 family signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-8985947; Interleukin-9 signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P52333; -.
SIGNOR; P52333; -.
EvolutionaryTrace; P52333; -.
GeneWiki; Janus_kinase_3; -.
GenomeRNAi; 3718; -.
PRO; PR:P52333; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105639; -.
CleanEx; HS_JAK3; -.
ExpressionAtlas; P52333; baseline and differential.
Genevisible; P52333; HS.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:BHF-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; ISS:BHF-UCL.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; ISS:BHF-UCL.
GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0002731; P:negative regulation of dendritic cell cytokine production; ISS:BHF-UCL.
GO; GO:0045221; P:negative regulation of FasL biosynthetic process; ISS:BHF-UCL.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISS:BHF-UCL.
GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:BHF-UCL.
GO; GO:0050868; P:negative regulation of T cell activation; ISS:BHF-UCL.
GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; ISS:BHF-UCL.
GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; ISS:BHF-UCL.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0070232; P:regulation of T cell apoptotic process; ISS:BHF-UCL.
GO; GO:0070672; P:response to interleukin-15; TAS:BHF-UCL.
GO; GO:0070669; P:response to interleukin-2; TAS:BHF-UCL.
GO; GO:0070670; P:response to interleukin-4; IDA:BHF-UCL.
GO; GO:0071104; P:response to interleukin-9; TAS:BHF-UCL.
GO; GO:0007262; P:STAT protein import into nucleus; TAS:UniProtKB.
GO; GO:0043029; P:T cell homeostasis; ISS:BHF-UCL.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; TAS:UniProtKB.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR000299; FERM_domain.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
InterPro; IPR020775; Tyr_kinase_non-rcpt_Jak3.
Pfam; PF07714; Pkinase_Tyr; 2.
PIRSF; PIRSF000636; TyrPK_Jak; 1.
PRINTS; PR01823; JANUSKINASE.
PRINTS; PR01826; JANUSKINASE3.
PRINTS; PR00109; TYRKINASE.
SMART; SM00295; B41; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 2.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF55550; SSF55550; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Disease mutation; Immunity;
Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; SCID; SH2 domain;
Transferase; Tyrosine-protein kinase.
CHAIN 1 1124 Tyrosine-protein kinase JAK3.
/FTId=PRO_0000088115.
DOMAIN 24 356 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 375 475 SH2; atypical.
DOMAIN 521 781 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 822 1111 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 828 836 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 223 Interaction with
cytokine/interferon/growth hormone
receptors. {ECO:0000250}.
ACT_SITE 949 949 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 855 855 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000250|UniProtKB:Q62137}.
MOD_RES 785 785 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15121872}.
MOD_RES 904 904 Phosphotyrosine.
{ECO:0000269|PubMed:18250158}.
MOD_RES 939 939 Phosphotyrosine.
{ECO:0000269|PubMed:18250158}.
MOD_RES 980 980 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15831699}.
MOD_RES 981 981 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15831699}.
VAR_SEQ 597 619 TMVQEFVHLGAIDMYLRKRGHLV -> ESPPPTHPTPASPK
SRLFFPPLF (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054165.
VAR_SEQ 620 1124 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054166.
VAR_SEQ 1071 1124 HELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFT
AHPEGKHHSLSFS -> SAAGLASVSQSVDWAGVSGKPAGA
(in isoform 1).
{ECO:0000303|PubMed:7559633}.
/FTId=VSP_004989.
VARIANT 12 12 P -> L (in dbSNP:rs56061056).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041722.
VARIANT 40 40 R -> H (in dbSNP:rs56384680).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041723.
VARIANT 58 58 Missing (in T(-)B(+)NK(-) SCID).
{ECO:0000269|PubMed:14615376}.
/FTId=VAR_019337.
VARIANT 100 100 Y -> C (in T(-)B(+)NK(-) SCID;
dbSNP:rs137852624).
{ECO:0000269|PubMed:7659163}.
/FTId=VAR_006284.
VARIANT 132 132 P -> T (in dbSNP:rs3212723).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_019336.
VARIANT 151 151 P -> R (in T(-)B(+)NK(-) SCID;
dbSNP:rs55778349).
{ECO:0000269|PubMed:10982185,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_010492.
VARIANT 169 169 D -> E (in T(-)B(+)NK(-) SCID;
dbSNP:rs147181709).
{ECO:0000269|PubMed:14615376}.
/FTId=VAR_019338.
VARIANT 481 481 E -> G (in T(-)B(+)NK(-) SCID).
{ECO:0000269|PubMed:9354668}.
/FTId=VAR_010493.
VARIANT 521 521 L -> V (in dbSNP:rs55666418).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041724.
VARIANT 527 527 L -> P (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041725.
VARIANT 582 582 R -> W (in T(-)B(+)NK(-) SCID;
dbSNP:rs193922361).
{ECO:0000269|PubMed:9753072}.
/FTId=VAR_010494.
VARIANT 586 592 Missing (in T(-)B(+)NK(-) SCID; lack of
phosphorylation in response to cytokine
stimulation).
{ECO:0000269|PubMed:9354668}.
/FTId=VAR_010495.
VARIANT 589 589 G -> S (in T(-)B(+)NK(-) SCID).
{ECO:0000269|PubMed:14615376}.
/FTId=VAR_019339.
VARIANT 688 688 I -> F (in dbSNP:rs35785705).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041726.
VARIANT 722 722 V -> I (in dbSNP:rs3213409).
{ECO:0000269|PubMed:10982185,
ECO:0000269|PubMed:14615376,
ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_010496.
VARIANT 759 759 C -> R (in T(-)B(+)NK(-) SCID;
constitutive phosphorylation).
{ECO:0000269|PubMed:9354668}.
/FTId=VAR_010497.
VARIANT 910 910 L -> S (in T(-)B(+)NK(-) SCID).
{ECO:0000269|PubMed:10982185}.
/FTId=VAR_010498.
MUTAGEN 785 785 Y->F: Strong decrease of JAK3
phosphorylation.
{ECO:0000269|PubMed:15121872}.
MUTAGEN 855 855 K->A: More than 90% loss of STAT5a
activation.
{ECO:0000269|PubMed:18250158}.
MUTAGEN 904 904 Y->F: About 40% loss of STAT5a
activation.
{ECO:0000269|PubMed:18250158}.
MUTAGEN 939 939 Y->F: About 80% loss of STAT5a
activation.
{ECO:0000269|PubMed:18250158}.
CONFLICT 34 34 G -> A (in Ref. 1; AAA19626).
{ECO:0000305}.
CONFLICT 45 45 F -> S (in Ref. 3; AAC50950).
{ECO:0000305}.
CONFLICT 103 103 R -> RS (in Ref. 3; AAC50950).
{ECO:0000305}.
CONFLICT 147 147 Missing (in Ref. 8; AAC50542).
{ECO:0000305}.
CONFLICT 187 187 T -> A (in Ref. 8; AAC50542).
{ECO:0000305}.
CONFLICT 212 212 R -> A (in Ref. 1; AAA19626 and 3;
AAC50950). {ECO:0000305}.
CONFLICT 222 222 R -> P (in Ref. 1; AAA19626 and 3;
AAC50950). {ECO:0000305}.
CONFLICT 271 271 L -> F (in Ref. 3; AAC50950).
{ECO:0000305}.
CONFLICT 287 287 Missing (in Ref. 3; AAC50950).
{ECO:0000305}.
CONFLICT 610 610 M -> I (in Ref. 2; AAC50226).
{ECO:0000305}.
CONFLICT 845 846 GD -> AH (in Ref. 1; AAA19626).
{ECO:0000305}.
CONFLICT 895 897 RQS -> EPE (in Ref. 3; AAC50950).
{ECO:0000305}.
CONFLICT 896 897 QS -> PE (in Ref. 1; AAA19626).
{ECO:0000305}.
STRAND 816 818 {ECO:0000244|PDB:5LWM}.
HELIX 819 821 {ECO:0000244|PDB:5LWM}.
STRAND 822 830 {ECO:0000244|PDB:5LWM}.
STRAND 832 841 {ECO:0000244|PDB:5LWM}.
STRAND 845 847 {ECO:0000244|PDB:5LWM}.
STRAND 849 859 {ECO:0000244|PDB:5LWM}.
HELIX 862 877 {ECO:0000244|PDB:5LWM}.
STRAND 886 891 {ECO:0000244|PDB:5LWM}.
STRAND 893 896 {ECO:0000244|PDB:5LWM}.
STRAND 898 903 {ECO:0000244|PDB:5LWM}.
HELIX 910 917 {ECO:0000244|PDB:5LWM}.
HELIX 918 920 {ECO:0000244|PDB:5LWM}.
HELIX 923 942 {ECO:0000244|PDB:5LWM}.
HELIX 952 954 {ECO:0000244|PDB:5LWM}.
STRAND 955 959 {ECO:0000244|PDB:5LWM}.
STRAND 962 965 {ECO:0000244|PDB:5LWM}.
HELIX 968 970 {ECO:0000244|PDB:3LXL}.
STRAND 979 982 {ECO:0000244|PDB:5LWM}.
HELIX 991 993 {ECO:0000244|PDB:5LWM}.
HELIX 996 1001 {ECO:0000244|PDB:5LWM}.
STRAND 1003 1005 {ECO:0000244|PDB:5LWM}.
HELIX 1006 1021 {ECO:0000244|PDB:5LWM}.
TURN 1022 1024 {ECO:0000244|PDB:5LWM}.
HELIX 1026 1028 {ECO:0000244|PDB:5LWM}.
HELIX 1030 1037 {ECO:0000244|PDB:5LWM}.
STRAND 1042 1044 {ECO:0000244|PDB:4QPS}.
HELIX 1046 1055 {ECO:0000244|PDB:5LWM}.
HELIX 1068 1077 {ECO:0000244|PDB:5LWM}.
HELIX 1082 1084 {ECO:0000244|PDB:5LWM}.
HELIX 1088 1102 {ECO:0000244|PDB:5LWM}.
SEQUENCE 1124 AA; 125099 MW; 895D8563439B2B7C CRC64;
MAPPSEETPL IPQRSCSLLS TEAGALHVLL PARGPGPPQR LSFSFGDHLA EDLCVQAAKA
SGILPVYHSL FALATEDLSC WFPPSHIFSV EDASTQVLLY RIRFYFPNWF GLEKCHRFGL
RKDLASAILD LPVLEHLFAQ HRSDLVSGRL PVGLSLKEQG ECLSLAVLDL ARMAREQAQR
PGELLKTVSY KACLPPSLRD LIQGLSFVTR RRIRRTVRRA LRRVAACQAD RHSLMAKYIM
DLERLDPAGA AETFHVGLPG ALGGHDGLGL LRVAGDGGIA WTQGEQEVLQ PFCDFPEIVD
ISIKQAPRVG PAGEHRLVTV TRTDNQILEA EFPGLPEALS FVALVDGYFR LTTDSQHFFC
KEVAPPRLLE EVAEQCHGPI TLDFAINKLK TGGSRPGSYV LRRSPQDFDS FLLTVCVQNP
LGPDYKGCLI RRSPTGTFLL VGLSRPHSSL RELLATCWDG GLHVDGVAVT LTSCCIPRPK
EKSNLIVVQR GHSPPTSSLV QPQSQYQLSQ MTFHKIPADS LEWHENLGHG SFTKIYRGCR
HEVVDGEARK TEVLLKVMDA KHKNCMESFL EAASLMSQVS YRHLVLLHGV CMAGDSTMVQ
EFVHLGAIDM YLRKRGHLVP ASWKLQVVKQ LAYALNYLED KGLPHGNVSA RKVLLAREGA
DGSPPFIKLS DPGVSPAVLS LEMLTDRIPW VAPECLREAQ TLSLEADKWG FGATVWEVFS
GVTMPISALD PAKKLQFYED RQQLPAPKWT ELALLIQQCM AYEPVQRPSF RAVIRDLNSL
ISSDYELLSD PTPGALAPRD GLWNGAQLYA CQDPTIFEER HLKYISQLGK GNFGSVELCR
YDPLGDNTGA LVAVKQLQHS GPDQQRDFQR EIQILKALHS DFIVKYRGVS YGPGRQSLRL
VMEYLPSGCL RDFLQRHRAR LDASRLLLYS SQICKGMEYL GSRRCVHRDL AARNILVESE
AHVKIADFGL AKLLPLDKDY YVVREPGQSP IFWYAPESLS DNIFSRQSDV WSFGVVLYEL
FTYCDKSCSP SAEFLRMMGC ERDVPALCRL LELLEEGQRL PAPPACPAEV HELMKLCWAP
SPQDRPSFSA LGPQLDMLWS GSRGCETHAF TAHPEGKHHS LSFS


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