Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Tyrosine-protein kinase JAK2 (EC 2.7.10.2) (Janus kinase 2) (JAK-2)

 JAK2_HUMAN              Reviewed;        1132 AA.
O60674; O14636; O75297;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
22-NOV-2017, entry version 197.
RecName: Full=Tyrosine-protein kinase JAK2;
EC=2.7.10.2 {ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:9618263};
AltName: Full=Janus kinase 2;
Short=JAK-2;
Name=JAK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9618263; DOI=10.1006/bbrc.1998.8685;
Saltzman A., Stone M., Franks C., Searfoss G., Munro R., Jaye M.,
Ivashchenko Y.;
"Cloning and characterization of human Jak-2 kinase: high mRNA
expression in immune cells and muscle tissue.";
Biochem. Biophys. Res. Commun. 246:627-633(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9446644;
Dalal I., Arpaia E., Dadi H., Kulkarni S., Squire J., Roifman C.M.;
"Cloning and characterization of the human homolog of mouse Jak2.";
Blood 91:844-851(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH ETV6.
PubMed=9326218;
Peeters P., Raynaud S.D., Cools J., Wlodarska I., Grosgeorge J.,
Philip P., Monpoux F., Van Rompaey L., Baens M., Van Den Berghe H.,
Marynen P.;
"Fusion of TEL, the ETS-variant gene 6 (ETV6), to the receptor-
associated kinase JAK2 as a result of t(9;12) in a lymphoid and
t(9;15;12) in a myeloid leukemia.";
Blood 90:2535-2540(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH IFNGR2, AND
PHOSPHORYLATION.
PubMed=7615558; DOI=10.1074/jbc.270.29.17528;
Sakatsume M., Igarashi K., Winestock K.D., Garotta G., Larner A.C.,
Finbloom D.S.;
"The Jak kinases differentially associate with the alpha and beta
(accessory factor) chains of the interferon gamma receptor to form a
functional receptor unit capable of activating STAT transcription
factors.";
J. Biol. Chem. 270:17528-17534(1995).
[6]
INTERACTION WITH IFNGR2, AND PHOSPHORYLATION.
PubMed=7673114; DOI=10.1074/jbc.270.36.20915;
Kotenko S.V., Izotova L.S., Pollack B.P., Mariano T.M., Donnelly R.J.,
Muthukumaran G., Cook J.R., Garotta G., Silvennoinen O., Ihle J.N.;
"Interaction between the components of the interferon gamma receptor
complex.";
J. Biol. Chem. 270:20915-20921(1995).
[7]
INTERACTION WITH SKB1.
PubMed=10531356; DOI=10.1074/jbc.274.44.31531;
Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L.,
Pestka S.;
"The human homologue of the yeast proteins Skb1 and Hsl7p interacts
with Jak kinases and contains protein methyltransferase activity.";
J. Biol. Chem. 274:31531-31542(1999).
[8]
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).
[9]
FUNCTION, AND INTERACTION WITH IL23R.
PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699;
Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J.,
Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J.,
O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D.,
Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.;
"A receptor for the heterodimeric cytokine IL-23 is composed of IL-
12Rbeta1 and a novel cytokine receptor subunit, IL-23R.";
J. Immunol. 168:5699-5708(2002).
[10]
CHROMOSOMAL TRANSLOCATION WITH PCM1.
PubMed=15805263; DOI=10.1158/0008-5472.CAN-04-4263;
Reiter A., Walz C., Watmore A., Schoch C., Blau I., Schlegelberger B.,
Berger U., Telford N., Aruliah S., Yin J.A., Vanstraelen D.,
Barker H.F., Taylor P.C., O'Driscoll A., Benedetti F., Rudolph C.,
Kolb H.-J., Hochhaus A., Hehlmann R., Chase A., Cross N.C.P.;
"The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute
leukemia that fuses PCM1 to JAK2.";
Cancer Res. 65:2662-2667(2005).
[11]
CHROMOSOMAL TRANSLOCATION WITH PCM1.
PubMed=16034466; DOI=10.1038/sj.leu.2403879;
Murati A., Gelsi-Boyer V., Adelaide J., Perot C., Talmant P.,
Giraudier S., Lode L., Letessier A., Delaval B., Brunel V., Imbert M.,
Garand R., Xerri L., Birnbaum D., Mozziconacci M.-J., Chaffanet M.;
"PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid
leukemia with t(8;9) translocation.";
Leukemia 19:1692-1696(2005).
[12]
CHROMOSOMAL TRANSLOCATION WITH PCM1.
PubMed=16091753; DOI=10.1038/sj.onc.1208850;
Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B.,
Delsol G., Laurent G., Dastugue N., Brousset P.;
"The t(8;9)(p22;p24) translocation in atypical chronic myeloid
leukaemia yields a new PCM1-JAK2 fusion gene.";
Oncogene 24:7248-7252(2005).
[13]
CHROMOSOMAL TRANSLOCATION WITH PCM1.
PubMed=16769584;
Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S.,
Kern W., Schoch C.;
"A combination of cytomorphology, cytogenetic analysis, fluorescence
in situ hybridization and reverse transcriptase polymerase chain
reaction for establishing clonality in cases of persisting
hypereosinophilia.";
Haematologica 91:817-820(2006).
[14]
TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH PCM1.
PubMed=16424865; DOI=10.1038/sj.leu.2404104;
Adelaide J., Perot C., Gelsi-Boyer V., Pautas C., Murati A.,
Copie-Bergman C., Imbert M., Chaffanet M., Birnbaum D.,
Mozziconacci M.-J.;
"A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell
lymphoma.";
Leukemia 20:536-537(2006).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19783980; DOI=10.1038/nature08448;
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
Green A.R., Kouzarides T.;
"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
chromatin.";
Nature 461:819-822(2009).
[16]
ENZYME REGULATION.
PubMed=21036157; DOI=10.1016/j.bbrc.2010.10.101;
Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.;
"Heme controls the regulation of protein tyrosine kinases Jak2 and
Src.";
Biochem. Biophys. Res. Commun. 403:30-35(2010).
[17]
INTERACTION WITH HSP90AB1.
PubMed=20353823; DOI=10.1016/j.cellsig.2010.03.012;
Cheng M.B., Zhang Y., Zhong X., Sutter B., Cao C.Y., Chen X.S.,
Cheng X.K., Zhang Y., Xiao L., Shen Y.F.;
"Stat1 mediates an auto-regulation of hsp90beta gene in heat shock
response.";
Cell. Signal. 22:1206-1213(2010).
[18]
FUNCTION.
PubMed=20098430; DOI=10.1038/nm.2079;
Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M.,
Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A.,
Torres R.M., Offermanns S., Pacaud P., Loirand G.;
"The Rho exchange factor Arhgef1 mediates the effects of angiotensin
II on vascular tone and blood pressure.";
Nat. Med. 16:183-190(2010).
[19]
FUNCTION IN PHOSPHORYLATION OF CDKN1B.
PubMed=21423214; DOI=10.1038/onc.2011.68;
Jakel H., Weinl C., Hengst L.;
"Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor
signaling to cell cycle control.";
Oncogene 30:3502-3512(2011).
[20]
REVIEW ON FUNCTION.
PubMed=16456223; DOI=10.1385/CBB:44:2:213;
Wallace T.A., Sayeski P.P.;
"Jak2 tyrosine kinase: a mediator of both housekeeping and ligand-
dependent gene expression?";
Cell Biochem. Biophys. 44:213-222(2006).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-570, 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).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 840-1132 IN COMPLEX WITH
SYNTHETIC INHIBITOR, IDENTIFICATION BY MASS SPECTROMETRY, AND
PHOSPHORYLATION AT TYR-1007 AND TYR-1008.
PubMed=16174768; DOI=10.1182/blood-2005-06-2413;
Lucet I.S., Fantino E., Styles M., Bamert R., Patel O.,
Broughton S.E., Walter M., Burns C.J., Treutlein H., Wilks A.F.,
Rossjohn J.;
"The structural basis of Janus kinase 2 inhibition by a potent and
specific pan-Janus kinase inhibitor.";
Blood 107:176-183(2006).
[24]
VARIANT PV PHE-617.
PubMed=15781101; DOI=10.1016/S0140-6736(05)71142-9;
The cancer genome project;
Baxter E.J., Scott L.M., Campbell P.J., East C., Fourouclas N.,
Swanton S., Vassiliou G.S., Bench A.J., Boyd E.M., Curtin N.,
Scott M.A., Erber W.N., Green A.R.;
"Acquired mutation of the tyrosine kinase JAK2 in human
myeloproliferative disorders.";
Lancet 365:1054-1061(2005).
[25]
ERRATUM.
The cancer genome project;
Baxter E.J., Scott L.M., Campbell P.J., East C., Fourouclas N.,
Swanton S., Vassiliou G.S., Bench A.J., Boyd E.M., Curtin N.,
Scott M.A., Erber W.N., Green A.R.;
Lancet 366:122-122(2005).
[26]
VARIANT THCYT3 PHE-617.
PubMed=16325696; DOI=10.1016/S0140-6736(05)67785-9;
The United Kingdom myeloproliferative disorders study group;
The medical research council adult leukaemia working party;
The Australasian leukaemia and lymphoma group;
Campbell P.J., Scott L.M., Buck G., Wheatley K., East C.L.,
Marsden J.T., Duffy A., Boyd E.M., Bench A.J., Scott M.A.,
Vassiliou G.S., Milligan D.W., Smith S.R., Erber W.N., Bareford D.,
Wilkins B.S., Reilly J.T., Harrison C.N., Green A.R.;
"Definition of subtypes of essential thrombocythaemia and relation to
polycythaemia vera based on JAK2 V617F mutation status: a prospective
study.";
Lancet 366:1945-1953(2005).
[27]
VARIANT PV PHE-617, AND CHARACTERIZATION OF VARIANT PV PHE-617.
PubMed=15793561; DOI=10.1038/nature03546;
James C., Ugo V., Le Couedic J.-P., Staerk J., Delhommeau F.,
Lacout C., Garcon L., Raslova H., Berger R., Bennaceur-Griscelli A.,
Villeval J.L., Constantinescu S.N., Casadevall N., Vainchenker W.;
"A unique clonal JAK2 mutation leading to constitutive signalling
causes polycythaemia vera.";
Nature 434:1144-1148(2005).
[28]
VARIANT PV PHE-617.
PubMed=15858187; DOI=10.1056/NEJMoa051113;
Kralovics R., Passamonti F., Buser A.S., Teo S.-S., Tiedt R.,
Passweg J.R., Tichelli A., Cazzola M., Skoda R.C.;
"A gain-of-function mutation of JAK2 in myeloproliferative
disorders.";
N. Engl. J. Med. 352:1779-1790(2005).
[29]
ASSOCIATION OF VARIANT PHE-617 WITH SUSCEPTIBILITY BUDD-CHIARI
SYNDROME.
PubMed=16707754; DOI=10.1056/NEJMcpc069006;
Chung R.T., Iafrate A.J., Amrein P.C., Sahani D.V., Misdraji J.;
"Case records of the Massachusetts General Hospital. Case 15-2006: a
46-year-old woman with sudden onset of abdominal distention.";
N. Engl. J. Med. 354:2166-2175(2006).
[30]
VARIANTS AML ASN-607 AND PHE-617.
PubMed=16247455; DOI=10.1038/sj.onc.1209163;
Lee J.W., Kim Y.G., Soung Y.H., Han K.J., Kim S.Y., Rhim H.S.,
Min W.S., Nam S.W., Park W.S., Lee J.Y., Yoo N.J., Lee S.H.;
"The JAK2 V617F mutation in de novo acute myelogenous leukemias.";
Oncogene 25:1434-1436(2006).
[31]
VARIANT PV PHE-617.
PubMed=16603627; DOI=10.1073/pnas.0601462103;
Jamieson C.H.M., Gotlib J., Durocher J.A., Chao M.P., Mariappan M.R.,
Lay M., Jones C., Zehnder J.L., Lilleberg S.L., Weissman I.L.;
"The JAK2 V617F mutation occurs in hematopoietic stem cells in
polycythemia vera and predisposes toward erythroid differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 103:6224-6229(2006).
[32]
VARIANTS MYELOPROLIFERATIVE DISORDER WITH ERYTHROCYTOSIS
537-PHE--LYS-539 DELINS LEU; 538-GLN-LEU-539 AND LEU-539.
PubMed=17267906; DOI=10.1056/NEJMoa065202;
Scott L.M., Tong W., Levine R.L., Scott M.A., Beer P.A.,
Stratton M.R., Futreal P.A., Erber W.N., McMullin M.F., Harrison C.N.,
Warren A.J., Gilliland D.G., Lodish H.F., Green A.R.;
"JAK2 exon 12 mutations in polycythemia vera and idiopathic
erythrocytosis.";
N. Engl. J. Med. 356:459-468(2007).
[33]
VARIANTS [LARGE SCALE ANALYSIS] ASP-127; GLN-191; ARG-346; GLU-377;
VAL-393 AND HIS-1063.
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).
[34]
VARIANT THCYT3 ILE-617.
PubMed=22397670; DOI=10.1056/NEJMc1200349;
Mead A.J., Rugless M.J., Jacobsen S.E., Schuh A.;
"Germline JAK2 mutation in a family with hereditary thrombocytosis.";
N. Engl. J. Med. 366:967-969(2012).
-!- FUNCTION: Non-receptor tyrosine kinase involved in various
processes such as cell growth, development, differentiation or
histone modifications. Mediates essential signaling events in both
innate and adaptive immunity. In the cytoplasm, plays a pivotal
role in signal transduction via its association with type I
receptors such as growth hormone (GHR), prolactin (PRLR), leptin
(LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II
receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple
interleukins (PubMed:7615558). Following ligand-binding to cell
surface receptors, phosphorylates specific tyrosine residues on
the cytoplasmic tails of the receptor, creating docking sites for
STATs proteins (PubMed:9618263). 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, cell stimulation with erythropoietin (EPO) during
erythropoiesis leads to JAK2 autophosphorylation, activation, and
its association with erythropoietin receptor (EPOR) that becomes
phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or
STAT5B) is recruited, phosphorylated and activated by JAK2. Once
activated, dimerized STAT5 translocates into the nucleus and
promotes the transcription of several essential genes involved in
the modulation of erythropoiesis. In addition, JAK2 mediates
angiotensin-2-induced ARHGEF1 phosphorylation (PubMed:20098430).
Plays a role in cell cycle by phosphorylating CDKN1B
(PubMed:21423214). Cooperates with TEC through reciprocal
phosphorylation to mediate cytokine-driven activation of FOS
transcription. In the nucleus, plays a key role in chromatin by
specifically mediating phosphorylation of 'Tyr-41' of histone H3
(H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1
alpha) from chromatin (PubMed:19783980).
{ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:19783980,
ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21423214,
ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:9618263}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:7615558,
ECO:0000269|PubMed:9618263}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is
likely to be the in vivo cofactor. {ECO:0000305|PubMed:7615558};
-!- ENZYME REGULATION: Regulated by autophosphorylation, can both
activate or decrease activity (By similarity). Heme regulates its
activity by enhancing the phosphorylation on Tyr-1007 and Tyr-
1008. {ECO:0000250, ECO:0000269|PubMed:21036157}.
-!- SUBUNIT: Interacts with EPOR, LYN, SIRPA, SH2B1 and TEC (By
similarity). Interacts with IL23R (PubMed:12023369). Interacts
with SKB1 (PubMed:10531356). Interacts with STAM2
(PubMed:10899310). Interacts with IFNGR2 (via intracellular
domain) (PubMed:7673114, PubMed:7615558). Interacts with LEPR
(Isoform B) (By similarity). Interacts with HSP90AB1; promotes
functional activation in a heat shock-dependent manner
(PubMed:20353823). {ECO:0000250|UniProtKB:Q62120,
ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:10899310,
ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:16174768,
ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:7615558,
ECO:0000269|PubMed:7673114}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-518647, EBI-518647;
P32927:CSF2RB; NbExp=4; IntAct=EBI-518647, EBI-1809771;
Q01344:IL5RA; NbExp=2; IntAct=EBI-518647, EBI-1759442;
P23458:JAK1; NbExp=4; IntAct=EBI-518647, EBI-1383438;
P40238:MPL; NbExp=6; IntAct=EBI-518647, EBI-6511486;
P16333:NCK1; NbExp=2; IntAct=EBI-518647, EBI-389883;
P18031:PTPN1; NbExp=5; IntAct=EBI-518647, EBI-968788;
Q9JHI9:Slc40a1 (xeno); NbExp=3; IntAct=EBI-518647, EBI-2931424;
P29597:TYK2; NbExp=2; IntAct=EBI-518647, EBI-1383454;
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:19783980}. Nucleus
{ECO:0000269|PubMed:19783980}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed throughout most
tissues. {ECO:0000269|PubMed:16424865}.
-!- DOMAIN: Possesses 2 protein kinase domains. The second one
probably contains the catalytic domain, while the presence of
slight differences suggest a different role for protein kinase 1
(By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated, leading to regulate its activity. Leptin
promotes phosphorylation on tyrosine residues, including
phosphorylation on Tyr-813 (By similarity). Autophosphorylation on
Tyr-119 in response to EPO down-regulates its kinase activity (By
similarity). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972
in response to growth hormone (GH) are required for maximal kinase
activity (By similarity). Also phosphorylated by TEC (By
similarity). Phosphorylated on tyrosine residues in response to
interferon gamma signaling (PubMed:7615558, PubMed:7673114).
{ECO:0000250|UniProtKB:Q62120, ECO:0000269|PubMed:7615558,
ECO:0000269|PubMed:7673114}.
-!- DISEASE: Note=Chromosomal aberrations involving JAK2 are found in
both chronic and acute forms of eosinophilic, lymphoblastic and
myeloid leukemia. Translocation t(8;9)(p22;p24) with PCM1 links
the protein kinase domain of JAK2 to the major portion of PCM1.
Translocation t(9;12)(p24;p13) with ETV6.
-!- DISEASE: Budd-Chiari syndrome (BDCHS) [MIM:600880]: A syndrome
caused by obstruction of hepatic venous outflow involving either
the hepatic veins or the terminal segment of the inferior vena
cava. Obstructions are generally caused by thrombosis and lead to
hepatic congestion and ischemic necrosis. Clinical manifestations
observed in the majority of patients include hepatomegaly, right
upper quadrant pain and abdominal ascites. Budd-Chiari syndrome is
associated with a combination of disease states including primary
myeloproliferative syndromes and thrombophilia due to factor V
Leiden, protein C deficiency and antithrombin III deficiency.
Budd-Chiari syndrome is a rare but typical complication in
patients with polycythemia vera. {ECO:0000269|PubMed:16707754}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Polycythemia vera (PV) [MIM:263300]: A myeloproliferative
disorder characterized by abnormal proliferation of all
hematopoietic bone marrow elements, erythroid hyperplasia, an
absolute increase in total blood volume, but also by myeloid
leukocytosis, thrombocytosis and splenomegaly.
{ECO:0000269|PubMed:15781101, ECO:0000269|PubMed:15793561,
ECO:0000269|PubMed:15858187, ECO:0000269|PubMed:16603627}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Thrombocythemia 3 (THCYT3) [MIM:614521]: A
myeloproliferative disorder characterized by excessive platelet
production, resulting in increased numbers of circulating
platelets. It can be associated with spontaneous hemorrhages and
thrombotic episodes. {ECO:0000269|PubMed:16325696,
ECO:0000269|PubMed:22397670}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myelofibrosis (MYELOF) [MIM:254450]: A disorder
characterized by replacement of the bone marrow by fibrous tissue,
occurring in association with a myeloproliferative disorder.
Clinical manifestations may include anemia, pallor, splenomegaly,
hypermetabolic state, petechiae, ecchymosis, bleeding,
lymphadenopathy, hepatomegaly, portal hypertension. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype
of acute leukemia, a cancer of the white blood cells. AML is a
malignant disease of bone marrow characterized by maturational
arrest of hematopoietic precursors at an early stage of
development. Clonal expansion of myeloid blasts occurs in bone
marrow, blood, and other tissue. Myelogenous leukemias develop
from changes in cells that normally produce neutrophils,
basophils, eosinophils and monocytes.
{ECO:0000269|PubMed:16247455}. 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}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/JAKID98.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF058925; AAC23982.1; -; mRNA.
EMBL; AF001362; AAC23653.1; -; mRNA.
EMBL; AF005216; AAB82092.1; -; mRNA.
EMBL; AL161450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS6457.1; -.
PIR; JW0091; JW0091.
RefSeq; NP_001309123.1; NM_001322194.1.
RefSeq; NP_001309124.1; NM_001322195.1.
RefSeq; NP_001309125.1; NM_001322196.1.
RefSeq; NP_001309133.1; NM_001322204.1.
RefSeq; NP_004963.1; NM_004972.3.
UniGene; Hs.656213; -.
PDB; 2B7A; X-ray; 2.00 A; A/B=840-1132.
PDB; 2W1I; X-ray; 2.60 A; A/B=835-1132.
PDB; 2XA4; X-ray; 2.04 A; A/B=835-1132.
PDB; 3E62; X-ray; 1.92 A; A=839-1131.
PDB; 3E63; X-ray; 1.90 A; A=839-1131.
PDB; 3E64; X-ray; 1.80 A; A=839-1131.
PDB; 3FUP; X-ray; 2.40 A; A/B=840-1132.
PDB; 3IO7; X-ray; 2.60 A; A=842-1132.
PDB; 3IOK; X-ray; 2.10 A; A=842-1132.
PDB; 3JY9; X-ray; 2.10 A; A=842-1130.
PDB; 3KCK; X-ray; 2.20 A; A=842-1132.
PDB; 3KRR; X-ray; 1.80 A; A=840-1132.
PDB; 3LPB; X-ray; 2.00 A; A/B=840-1132.
PDB; 3Q32; X-ray; 2.50 A; A/B=839-1132.
PDB; 3RVG; X-ray; 2.50 A; A=835-1132.
PDB; 3TJC; X-ray; 2.40 A; A/B=837-1132.
PDB; 3TJD; X-ray; 2.90 A; A/B=837-1132.
PDB; 3UGC; X-ray; 1.34 A; A=840-1132.
PDB; 3ZMM; X-ray; 2.51 A; A/B=835-1132.
PDB; 4AQC; X-ray; 1.90 A; A/B=835-1132.
PDB; 4BBE; X-ray; 1.90 A; A/B/C/D=839-1132.
PDB; 4BBF; X-ray; 2.00 A; A/B/C/D=839-1132.
PDB; 4C61; X-ray; 2.45 A; A/B=835-1132.
PDB; 4C62; X-ray; 2.75 A; A/B=835-1132.
PDB; 4D0W; X-ray; 1.77 A; A=835-1132.
PDB; 4D0X; X-ray; 1.82 A; A=835-1132.
PDB; 4D1S; X-ray; 1.66 A; A=835-1132.
PDB; 4E4M; X-ray; 2.25 A; A/B/D/E=833-1132.
PDB; 4E6D; X-ray; 2.22 A; A/B=835-1132.
PDB; 4E6Q; X-ray; 1.95 A; A/B=835-1132.
PDB; 4F08; X-ray; 2.82 A; A/B=833-1132.
PDB; 4F09; X-ray; 2.40 A; A=833-1132.
PDB; 4FVP; X-ray; 2.01 A; A=536-812.
PDB; 4FVQ; X-ray; 1.75 A; A=536-812.
PDB; 4FVR; X-ray; 2.00 A; A=536-812.
PDB; 4GFM; X-ray; 2.30 A; A=833-1132.
PDB; 4GMY; X-ray; 2.40 A; A=833-1132.
PDB; 4HGE; X-ray; 2.30 A; A/B=833-1132.
PDB; 4IVA; X-ray; 1.50 A; A=833-1132.
PDB; 4JI9; X-ray; 2.40 A; A/B=833-1132.
PDB; 4JIA; X-ray; 1.85 A; A=833-1132.
PDB; 4P7E; X-ray; 2.40 A; A/B=840-1132.
PDB; 4YTC; X-ray; 2.16 A; A=842-1132.
PDB; 4YTF; X-ray; 1.78 A; A=842-1132.
PDB; 4YTH; X-ray; 2.04 A; A=842-1132.
PDB; 4YTI; X-ray; 2.52 A; A=842-1132.
PDB; 4Z32; X-ray; 3.04 A; A/B/C/D/E/F/G/H=31-516.
PDB; 4ZIM; X-ray; 2.65 A; A/B=839-1132.
PDB; 5AEP; X-ray; 1.95 A; A=835-1132.
PDB; 5CF4; X-ray; 2.38 A; A/B=839-1132.
PDB; 5CF5; X-ray; 2.45 A; A/B=839-1132.
PDB; 5CF6; X-ray; 2.50 A; A/B=839-1132.
PDB; 5CF8; X-ray; 1.80 A; A/B=839-1132.
PDB; 5HEZ; X-ray; 2.66 A; A/B/C/D=833-1132.
PDB; 5I4N; X-ray; 1.54 A; A=535-812.
PDB; 5L3A; X-ray; 1.98 A; A=840-1132.
PDB; 5TQ3; X-ray; 2.69 A; A/B=837-1132.
PDB; 5TQ4; X-ray; 2.30 A; A=837-1132.
PDB; 5TQ5; X-ray; 2.30 A; A=837-1132.
PDB; 5TQ6; X-ray; 2.06 A; A/B=837-1132.
PDB; 5TQ7; X-ray; 2.10 A; A/B=837-1132.
PDB; 5TQ8; X-ray; 1.59 A; A=837-1132.
PDB; 5USY; X-ray; 2.00 A; A/B=840-1132.
PDB; 5USZ; X-ray; 2.10 A; A=536-812.
PDB; 5UT0; X-ray; 2.10 A; A=536-812.
PDB; 5UT1; X-ray; 1.95 A; A=536-812.
PDB; 5UT2; X-ray; 1.75 A; A=536-812.
PDB; 5UT3; X-ray; 1.50 A; A=536-812.
PDB; 5UT4; X-ray; 2.00 A; A=536-812.
PDB; 5UT5; X-ray; 1.90 A; A=536-812.
PDB; 5UT6; X-ray; 1.65 A; A=536-812.
PDB; 5WEV; X-ray; 1.85 A; A=833-1132.
PDBsum; 2B7A; -.
PDBsum; 2W1I; -.
PDBsum; 2XA4; -.
PDBsum; 3E62; -.
PDBsum; 3E63; -.
PDBsum; 3E64; -.
PDBsum; 3FUP; -.
PDBsum; 3IO7; -.
PDBsum; 3IOK; -.
PDBsum; 3JY9; -.
PDBsum; 3KCK; -.
PDBsum; 3KRR; -.
PDBsum; 3LPB; -.
PDBsum; 3Q32; -.
PDBsum; 3RVG; -.
PDBsum; 3TJC; -.
PDBsum; 3TJD; -.
PDBsum; 3UGC; -.
PDBsum; 3ZMM; -.
PDBsum; 4AQC; -.
PDBsum; 4BBE; -.
PDBsum; 4BBF; -.
PDBsum; 4C61; -.
PDBsum; 4C62; -.
PDBsum; 4D0W; -.
PDBsum; 4D0X; -.
PDBsum; 4D1S; -.
PDBsum; 4E4M; -.
PDBsum; 4E6D; -.
PDBsum; 4E6Q; -.
PDBsum; 4F08; -.
PDBsum; 4F09; -.
PDBsum; 4FVP; -.
PDBsum; 4FVQ; -.
PDBsum; 4FVR; -.
PDBsum; 4GFM; -.
PDBsum; 4GMY; -.
PDBsum; 4HGE; -.
PDBsum; 4IVA; -.
PDBsum; 4JI9; -.
PDBsum; 4JIA; -.
PDBsum; 4P7E; -.
PDBsum; 4YTC; -.
PDBsum; 4YTF; -.
PDBsum; 4YTH; -.
PDBsum; 4YTI; -.
PDBsum; 4Z32; -.
PDBsum; 4ZIM; -.
PDBsum; 5AEP; -.
PDBsum; 5CF4; -.
PDBsum; 5CF5; -.
PDBsum; 5CF6; -.
PDBsum; 5CF8; -.
PDBsum; 5HEZ; -.
PDBsum; 5I4N; -.
PDBsum; 5L3A; -.
PDBsum; 5TQ3; -.
PDBsum; 5TQ4; -.
PDBsum; 5TQ5; -.
PDBsum; 5TQ6; -.
PDBsum; 5TQ7; -.
PDBsum; 5TQ8; -.
PDBsum; 5USY; -.
PDBsum; 5USZ; -.
PDBsum; 5UT0; -.
PDBsum; 5UT1; -.
PDBsum; 5UT2; -.
PDBsum; 5UT3; -.
PDBsum; 5UT4; -.
PDBsum; 5UT5; -.
PDBsum; 5UT6; -.
PDBsum; 5WEV; -.
ProteinModelPortal; O60674; -.
SMR; O60674; -.
BioGrid; 109920; 104.
CORUM; O60674; -.
DIP; DIP-33880N; -.
IntAct; O60674; 35.
MINT; MINT-158048; -.
STRING; 9606.ENSP00000371067; -.
BindingDB; O60674; -.
ChEMBL; CHEMBL2971; -.
DrugBank; DB07162; 4-(3-amino-1H-indazol-5-yl)-N-tert-butylbenzenesulfonamide.
DrugBank; DB08067; 4-[(2-{4-[(CYCLOPROPYLCARBAMOYL)AMINO]-1H-PYRAZOL-3-YL}-1H-BENZIMIDAZOL-6-YL)METHYL]MORPHOLIN-4-IUM.
DrugBank; DB07161; 5-phenyl-1H-indazol-3-amine.
DrugBank; DB08877; Ruxolitinib.
DrugBank; DB08895; Tofacitinib.
DrugBank; DB05243; XL019.
GuidetoPHARMACOLOGY; 2048; -.
iPTMnet; O60674; -.
PhosphoSitePlus; O60674; -.
BioMuta; JAK2; -.
EPD; O60674; -.
MaxQB; O60674; -.
PaxDb; O60674; -.
PeptideAtlas; O60674; -.
PRIDE; O60674; -.
DNASU; 3717; -.
Ensembl; ENST00000381652; ENSP00000371067; ENSG00000096968.
GeneID; 3717; -.
KEGG; hsa:3717; -.
UCSC; uc003ziw.3; human.
CTD; 3717; -.
DisGeNET; 3717; -.
EuPathDB; HostDB:ENSG00000096968.12; -.
GeneCards; JAK2; -.
HGNC; HGNC:6192; JAK2.
HPA; CAB013089; -.
HPA; HPA040820; -.
HPA; HPA043870; -.
MalaCards; JAK2; -.
MIM; 147796; gene.
MIM; 254450; phenotype.
MIM; 263300; phenotype.
MIM; 600880; phenotype.
MIM; 601626; phenotype.
MIM; 614521; phenotype.
neXtProt; NX_O60674; -.
OpenTargets; ENSG00000096968; -.
Orphanet; 131; Budd-Chiari syndrome.
Orphanet; 3318; Essential thrombocythemia.
Orphanet; 71493; Familial thrombocytosis.
Orphanet; 824; Myelofibrosis with myeloid metaplasia.
Orphanet; 729; Polycythemia vera.
PharmGKB; PA29989; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00900000140909; -.
HOGENOM; HOG000049158; -.
HOVERGEN; HBG006195; -.
InParanoid; O60674; -.
KO; K04447; -.
OMA; SNCHGPI; -.
OrthoDB; EOG091G01IS; -.
PhylomeDB; O60674; -.
TreeFam; TF327041; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; O60674; -.
SIGNOR; O60674; -.
ChiTaRS; JAK2; human.
EvolutionaryTrace; O60674; -.
GeneWiki; Janus_kinase_2; -.
GenomeRNAi; 3717; -.
PRO; PR:O60674; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000096968; -.
CleanEx; HS_JAK2; -.
ExpressionAtlas; O60674; baseline and differential.
Genevisible; O60674; HS.
GO; GO:0005901; C:caveola; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IDA:HPA.
GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0033130; F:acetylcholine receptor binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005131; F:growth hormone receptor binding; ISS:BHF-UCL.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0035401; F:histone kinase activity (H3-Y41 specific); IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
GO; GO:0005143; F:interleukin-12 receptor binding; ISS:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; NAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:CACAO.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
GO; GO:0030041; P:actin filament polymerization; NAS:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:BHF-UCL.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0042976; P:activation of Janus kinase activity; ISS:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; ISS:BHF-UCL.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0030154; P:cell differentiation; ISS:BHF-UCL.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; ISS:BHF-UCL.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0035409; P:histone H3-Y41 phosphorylation; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; ISS:UniProtKB.
GO; GO:0061180; P:mammary gland epithelium development; ISS:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
GO; GO:0031959; P:mineralocorticoid receptor signaling pathway; IEA:Ensembl.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
GO; GO:0043392; P:negative regulation of DNA binding; ISS:BHF-UCL.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0050867; P:positive regulation of cell activation; IEA:Ensembl.
GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IEA:Ensembl.
GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:BHF-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050727; P:regulation of inflammatory response; IDA:BHF-UCL.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0046677; P:response to antibiotic; IDA:MGI.
GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
GO; GO:0070671; P:response to interleukin-12; IDA:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:BHF-UCL.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
GO; GO:0007262; P:STAT protein import into nucleus; ISS:BHF-UCL.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISS:BHF-UCL.
CDD; cd05078; PTK_Jak2_rpt1; 1.
CDD; cd14205; PTKc_Jak2_rpt2; 1.
CDD; cd10379; SH2_Jak2; 1.
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; IPR035963; FERM_2.
InterPro; IPR000299; FERM_domain.
InterPro; IPR035860; JAK2_SH2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR035588; PTK_Jak2_rpt1.
InterPro; IPR035589; PTKc_Jak2_rpt2.
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; IPR020693; Tyr_kinase_non-rcpt_Jak2.
Pfam; PF07714; Pkinase_Tyr; 2.
Pfam; PF00017; SH2; 1.
PIRSF; PIRSF000636; TyrPK_Jak; 1.
PRINTS; PR01823; JANUSKINASE.
PRINTS; PR01825; JANUSKINASE2.
PRINTS; PR00109; TYRKINASE.
SMART; SM00295; B41; 1.
SMART; SM00252; SH2; 1.
SMART; SM00219; TyrKc; 2.
SUPFAM; SSF47031; SSF47031; 1.
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.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; ATP-binding; Chromatin regulator;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Disease mutation; Immunity; Innate immunity; Kinase; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; Repeat; SH2 domain;
Transferase; Tyrosine-protein kinase.
CHAIN 1 1132 Tyrosine-protein kinase JAK2.
/FTId=PRO_0000088112.
DOMAIN 37 380 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 401 482 SH2; atypical. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 545 809 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 849 1124 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 855 863 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 239 Interaction with
cytokine/interferon/growth hormone
receptors. {ECO:0000250}.
ACT_SITE 976 976 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 882 882 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 352 353 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 442 443 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 450 451 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 504 505 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
SITE 710 711 Breakpoint for translocation to form
PCM1-JAK2 fusion protein.
MOD_RES 119 119 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 373 373 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 570 570 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 813 813 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 868 868 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 966 966 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 972 972 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q62120}.
MOD_RES 1007 1007 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16174768}.
MOD_RES 1008 1008 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:16174768}.
VARIANT 127 127 G -> D (in dbSNP:rs56118985).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041716.
VARIANT 191 191 K -> Q (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041717.
VARIANT 346 346 K -> R (in dbSNP:rs55667734).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041718.
VARIANT 377 377 A -> E (in dbSNP:rs55953208).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041719.
VARIANT 393 393 L -> V (in dbSNP:rs2230723).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041720.
VARIANT 537 539 FHK -> L (in myeloproliferative disorder
with erythrocytosis).
{ECO:0000269|PubMed:17267906}.
/FTId=VAR_032693.
VARIANT 538 539 HK -> QL (in myeloproliferative disorder
with erythrocytosis).
/FTId=VAR_032694.
VARIANT 539 539 K -> L (in myeloproliferative disorder
with erythrocytosis; requires 2
nucleotide substitutions;
dbSNP:rs121912473).
{ECO:0000269|PubMed:17267906}.
/FTId=VAR_032695.
VARIANT 584 584 D -> E (in dbSNP:rs17490221).
/FTId=VAR_043129.
VARIANT 607 607 K -> N (in AML; dbSNP:rs121912472).
{ECO:0000269|PubMed:16247455}.
/FTId=VAR_032696.
VARIANT 617 617 V -> F (in PV, THCYT3 and AML; associated
with susceptibility to Budd-Chiari
syndrome; somatic mutation in a high
percentage of patients with essential
thrombocythemia or myelofibrosis; leads
to constitutive tyrosine phosphorylation
activity that promotes cytokine
hypersensitivity; dbSNP:rs77375493).
{ECO:0000269|PubMed:15781101,
ECO:0000269|PubMed:15793561,
ECO:0000269|PubMed:15858187,
ECO:0000269|PubMed:16247455,
ECO:0000269|PubMed:16325696,
ECO:0000269|PubMed:16603627}.
/FTId=VAR_032697.
VARIANT 617 617 V -> I (in THCYT3; dbSNP:rs77375493).
{ECO:0000269|PubMed:22397670}.
/FTId=VAR_067534.
VARIANT 1063 1063 R -> H (in dbSNP:rs41316003).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041721.
CONFLICT 321 321 P -> S (in Ref. 1; AAC23982).
{ECO:0000305}.
CONFLICT 1126 1126 I -> V (in Ref. 2; AAC23653).
{ECO:0000305}.
STRAND 38 45 {ECO:0000244|PDB:4Z32}.
TURN 47 49 {ECO:0000244|PDB:4Z32}.
STRAND 53 57 {ECO:0000244|PDB:4Z32}.
STRAND 59 63 {ECO:0000244|PDB:4Z32}.
HELIX 64 75 {ECO:0000244|PDB:4Z32}.
HELIX 79 82 {ECO:0000244|PDB:4Z32}.
STRAND 85 89 {ECO:0000244|PDB:4Z32}.
TURN 90 92 {ECO:0000244|PDB:4Z32}.
STRAND 101 104 {ECO:0000244|PDB:4Z32}.
STRAND 109 116 {ECO:0000244|PDB:4Z32}.
TURN 121 124 {ECO:0000244|PDB:4Z32}.
STRAND 131 133 {ECO:0000244|PDB:4Z32}.
TURN 136 139 {ECO:0000244|PDB:4Z32}.
HELIX 147 162 {ECO:0000244|PDB:4Z32}.
HELIX 172 192 {ECO:0000244|PDB:4Z32}.
HELIX 197 201 {ECO:0000244|PDB:4Z32}.
HELIX 206 209 {ECO:0000244|PDB:4Z32}.
HELIX 212 219 {ECO:0000244|PDB:4Z32}.
HELIX 223 239 {ECO:0000244|PDB:4Z32}.
HELIX 247 261 {ECO:0000244|PDB:4Z32}.
HELIX 263 265 {ECO:0000244|PDB:4Z32}.
STRAND 268 271 {ECO:0000244|PDB:4Z32}.
STRAND 286 291 {ECO:0000244|PDB:4Z32}.
TURN 292 294 {ECO:0000244|PDB:4Z32}.
STRAND 295 300 {ECO:0000244|PDB:4Z32}.
STRAND 315 318 {ECO:0000244|PDB:4Z32}.
HELIX 320 322 {ECO:0000244|PDB:4Z32}.
STRAND 323 329 {ECO:0000244|PDB:4Z32}.
STRAND 340 349 {ECO:0000244|PDB:4Z32}.
STRAND 351 357 {ECO:0000244|PDB:4Z32}.
HELIX 359 376 {ECO:0000244|PDB:4Z32}.
TURN 385 387 {ECO:0000244|PDB:4Z32}.
HELIX 390 397 {ECO:0000244|PDB:4Z32}.
HELIX 406 415 {ECO:0000244|PDB:4Z32}.
STRAND 423 427 {ECO:0000244|PDB:4Z32}.
STRAND 432 443 {ECO:0000244|PDB:4Z32}.
STRAND 446 455 {ECO:0000244|PDB:4Z32}.
HELIX 474 481 {ECO:0000244|PDB:4Z32}.
STRAND 485 488 {ECO:0000244|PDB:4Z32}.
STRAND 491 495 {ECO:0000244|PDB:4Z32}.
STRAND 510 513 {ECO:0000244|PDB:4Z32}.
HELIX 542 544 {ECO:0000244|PDB:5UT3}.
STRAND 545 554 {ECO:0000244|PDB:5UT3}.
STRAND 557 567 {ECO:0000244|PDB:5UT3}.
HELIX 569 571 {ECO:0000244|PDB:5UT3}.
STRAND 573 583 {ECO:0000244|PDB:5UT3}.
HELIX 585 590 {ECO:0000244|PDB:5UT3}.
HELIX 591 602 {ECO:0000244|PDB:5UT3}.
STRAND 612 616 {ECO:0000244|PDB:5UT3}.
STRAND 623 627 {ECO:0000244|PDB:5UT3}.
HELIX 634 640 {ECO:0000244|PDB:5UT3}.
HELIX 642 644 {ECO:0000244|PDB:5UT3}.
HELIX 647 666 {ECO:0000244|PDB:5UT3}.
HELIX 676 678 {ECO:0000244|PDB:5UT3}.
STRAND 679 683 {ECO:0000244|PDB:5UT3}.
HELIX 687 689 {ECO:0000244|PDB:5UT3}.
STRAND 694 697 {ECO:0000244|PDB:5UT3}.
TURN 704 706 {ECO:0000244|PDB:5UT3}.
HELIX 709 714 {ECO:0000244|PDB:5UT3}.
TURN 715 718 {ECO:0000244|PDB:5UT3}.
HELIX 721 725 {ECO:0000244|PDB:5UT3}.
HELIX 727 729 {ECO:0000244|PDB:5UT3}.
HELIX 732 747 {ECO:0000244|PDB:5UT3}.
TURN 748 750 {ECO:0000244|PDB:5UT3}.
TURN 753 756 {ECO:0000244|PDB:5UT3}.
HELIX 759 767 {ECO:0000244|PDB:5UT3}.
HELIX 778 780 {ECO:0000244|PDB:5I4N}.
HELIX 781 787 {ECO:0000244|PDB:5UT3}.
HELIX 792 794 {ECO:0000244|PDB:5UT3}.
HELIX 798 807 {ECO:0000244|PDB:5UT3}.
STRAND 836 838 {ECO:0000244|PDB:4E4M}.
HELIX 846 848 {ECO:0000244|PDB:3UGC}.
STRAND 849 857 {ECO:0000244|PDB:3UGC}.
STRAND 859 868 {ECO:0000244|PDB:3UGC}.
STRAND 872 874 {ECO:0000244|PDB:4IVA}.
STRAND 877 885 {ECO:0000244|PDB:3UGC}.
HELIX 889 903 {ECO:0000244|PDB:3UGC}.
STRAND 913 917 {ECO:0000244|PDB:3UGC}.
HELIX 919 922 {ECO:0000244|PDB:3UGC}.
STRAND 926 930 {ECO:0000244|PDB:3UGC}.
HELIX 937 943 {ECO:0000244|PDB:3UGC}.
HELIX 945 947 {ECO:0000244|PDB:3UGC}.
HELIX 950 969 {ECO:0000244|PDB:3UGC}.
HELIX 979 981 {ECO:0000244|PDB:3UGC}.
STRAND 982 986 {ECO:0000244|PDB:3UGC}.
STRAND 989 992 {ECO:0000244|PDB:3UGC}.
HELIX 995 997 {ECO:0000244|PDB:4D1S}.
STRAND 1006 1009 {ECO:0000244|PDB:4IVA}.
HELIX 1017 1020 {ECO:0000244|PDB:3UGC}.
HELIX 1023 1028 {ECO:0000244|PDB:3UGC}.
STRAND 1030 1032 {ECO:0000244|PDB:4IVA}.
HELIX 1033 1049 {ECO:0000244|PDB:3UGC}.
HELIX 1053 1055 {ECO:0000244|PDB:4IVA}.
HELIX 1057 1065 {ECO:0000244|PDB:3UGC}.
STRAND 1069 1071 {ECO:0000244|PDB:5HEZ}.
HELIX 1072 1083 {ECO:0000244|PDB:3UGC}.
TURN 1084 1086 {ECO:0000244|PDB:5HEZ}.
HELIX 1096 1105 {ECO:0000244|PDB:3UGC}.
HELIX 1110 1112 {ECO:0000244|PDB:3UGC}.
HELIX 1116 1128 {ECO:0000244|PDB:3UGC}.
SEQUENCE 1132 AA; 130674 MW; C30669EF1A7DA80C CRC64;
MGMACLTMTE MEGTSTSSIY QNGDISGNAN SMKQIDPVLQ VYLYHSLGKS EADYLTFPSG
EYVAEEICIA ASKACGITPV YHNMFALMSE TERIWYPPNH VFHIDESTRH NVLYRIRFYF
PRWYCSGSNR AYRHGISRGA EAPLLDDFVM SYLFAQWRHD FVHGWIKVPV THETQEECLG
MAVLDMMRIA KENDQTPLAI YNSISYKTFL PKCIRAKIQD YHILTRKRIR YRFRRFIQQF
SQCKATARNL KLKYLINLET LQSAFYTEKF EVKEPGSGPS GEEIFATIII TGNGGIQWSR
GKHKESETLT EQDLQLYCDF PNIIDVSIKQ ANQEGSNESR VVTIHKQDGK NLEIELSSLR
EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIQSNC HGPISMDFAI SKLKKAGNQT
GLYVLRCSPK DFNKYFLTFA VERENVIEYK HCLITKNENE EYNLSGTKKN FSSLKDLLNC
YQMETVRSDN IIFQFTKCCP PKPKDKSNLL VFRTNGVSDV PTSPTLQRPT HMNQMVFHKI
RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHETEVLL KVLDKAHRNY SESFFEAASM
MSKLSHKHLV LNYGVCVCGD ENILVQEFVK FGSLDTYLKK NKNCINILWK LEVAKQLAWA
MHFLEENTLI HGNVCAKNIL LIREEDRKTG NPPFIKLSDP GISITVLPKD ILQERIPWVP
PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLSALDSQ RKLQFYEDRH QLPAPKWAEL
ANLINNCMDY EPDFRPSFRA IIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD
PTQFEERHLK FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
ILKSLQHDNI VKYKGVCYSA GRRNLKLIME YLPYGSLRDY LQKHKERIDH IKLLQYTSQI
CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV LPQDKEYYKV KEPGESPIFW
YAPESLTESK FSVASDVWSF GVVLYELFTY IEKSKSPPAE FMRMIGNDKQ GQMIVFHLIE
LLKNNGRLPR PDGCPDEIYM IMTECWNNNV NQRPSFRDLA LRVDQIRDNM AG


Related products :

Catalog number Product name Quantity
FP-0040 Fusion proteins: Tyrosine-protein kinase JAK2 (Janus kinase 2) , JAK2 10ug
FP-0040 Tyrosine-protein kinase JAK2 (Janus kinase 2) ; SH2-Domain: JAK2 10ug
bs-0908P Peptides: JAK2(Tyrosine-protein kinase JAK2; Janus kinase 2; JAK-2) Protein Length:12-25 amino acids. 200ug lyophilized
FP-0040 Tyrosine-protein kinase JAK2 (Janus kinase 2) 10ug
CSB-EL011931RA Rat Janus kinase 2 (a protein tyrosine kinase) (JAK2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL011931PI Pig Janus kinase 2 (a protein tyrosine kinase) (JAK2) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL011931HU Human Janus kinase 2 (a protein tyrosine kinase) (JAK2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL011931MO Mouse Janus kinase 2 (a protein tyrosine kinase) (JAK2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL011931CH Chicken Janus kinase 2 (a protein tyrosine kinase) (JAK2) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
FP-0041 Tyrosine-protein kinase JAK3 (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) 10ug
FP-0041 Fusion proteins: Tyrosine-protein kinase JAK3 (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) , JAK3 10ug
FP-0041 Tyrosine-protein kinase JAK3 (Janus kinase 3) (JAK-3) (Leukocyte janus kinase) ; SH2-Domain: JAK3 10ug
32-232 Tyk2 (tyrosine kinase 2),with 1187-amino acid protein (about 131kDa), belongs to the family of non-receptor janus tyrosine kinases, which also includes Jak1, Jak2, and Jak3. Kinases of the Jak family 0.1 mL
EIAAB33008 CCK4,CCK-4,Colon carcinoma kinase 4,Homo sapiens,Human,Inactive tyrosine-protein kinase 7,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
FP-0039 Tyrosine-protein kinase JAK1 (Janus kinase 1) 10ug
FP-0040 Tyrosine_protein kinase JAK2 (Janus kinase 2) 10 ug
E1915m ELISA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
DL-JAK2-Ra Rat Janus Kinase 2 (JAK2) ELISA Kit 96T
EIAAB33010 Inactive tyrosine-protein kinase 7,Mouse,Mus musculus,Protein chuzhoi,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,Ptk7,Tyrosine-protein kinase-like 7
JAK2-336H Protein: Recombinant Human Janus Kinase 2, GST-tagged, Active 5μg
JAK2-336H Protein Recombinant Human Janus Kinase 2, GST-tagged, Active 5μg
U1915h CLIA kit Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur