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_MOUSE              Reviewed;        1129 AA.
Q62120; Q62124; Q7TQD0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
25-OCT-2017, entry version 185.
RecName: Full=Tyrosine-protein kinase JAK2;
EC=2.7.10.2;
AltName: Full=Janus kinase 2;
Short=JAK-2;
Name=Jak2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8378315; DOI=10.1073/pnas.90.18.8429;
Silvennoinen O., Witthuhn B.A., Quelle F.W., Cleveland J.L., Yi T.,
Ihle J.N.;
"Structure of the murine Jak2 protein-tyrosine kinase and its role in
interleukin 3 signal transduction.";
Proc. Natl. Acad. Sci. U.S.A. 90:8429-8433(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
"The application of the polymerase chain reaction to cloning members
of the protein tyrosine kinase family.";
Gene 85:67-74(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
PubMed=2466296; DOI=10.1073/pnas.86.5.1603;
Wilks A.F.;
"Two putative protein-tyrosine kinases identified by application of
the polymerase chain reaction.";
Proc. Natl. Acad. Sci. U.S.A. 86:1603-1607(1989).
[5]
FUNCTION, AND INTERACTION WITH EPOR.
PubMed=8343951; DOI=10.1016/0092-8674(93)90414-L;
Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O.,
Ihle J.N.;
"JAK2 associates with the erythropoietin receptor and is tyrosine
phosphorylated and activated following stimulation with
erythropoietin.";
Cell 74:227-236(1993).
[6]
INTERACTION WITH CYTOKINE/INTERFERON/GROWTH HORMONE RECEPTORS.
PubMed=7775438; DOI=10.1074/jbc.270.23.14015;
Zhao Y., Wagner F., Frank S.J., Kraft A.S.;
"The amino-terminal portion of the JAK2 protein kinase is necessary
for binding and phosphorylation of the granulocyte-macrophage colony-
stimulating factor receptor beta c chain.";
J. Biol. Chem. 270:13814-13818(1995).
[7]
FUNCTION IN PHOSPHORYLATION OF STAT5A AND STAT5B.
PubMed=8702638; DOI=10.1074/jbc.271.32.19483;
Nakamura N., Chin H., Miyasaka N., Miura O.;
"An epidermal growth factor receptor/Jak2 tyrosine kinase domain
chimera induces tyrosine phosphorylation of Stat5 and transduces a
growth signal in hematopoietic cells.";
J. Biol. Chem. 271:19483-19488(1996).
[8]
FUNCTION, INTERACTION WITH TEC, AND PHOSPHORYLATION BY TEC.
PubMed=9473212;
Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K.,
Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.;
"Tec and Jak2 kinases cooperate to mediate cytokine-driven activation
of c-fos transcription.";
Blood 91:1496-1507(1998).
[9]
INTERACTION WITH LYN.
PubMed=9573010;
Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.;
"Lyn physically associates with the erythropoietin receptor and may
play a role in activation of the Stat5 pathway.";
Blood 91:3734-3745(1998).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9590173; DOI=10.1016/S0092-8674(00)81167-8;
Parganas E., Wang D., Stravopodis D., Topham D.J., Marine J.C.,
Teglund S., Vanin E.F., Bodner S., Colamonici O.R., van Deursen J.M.,
Grosveld G., Ihle J.N.;
"Jak2 is essential for signaling through a variety of cytokine
receptors.";
Cell 93:385-395(1998).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9590174; DOI=10.1016/S0092-8674(00)81168-X;
Neubauer H., Cumano A., Muller M., Wu H., Huffstadt U., Pfeffer K.;
"Jak2 deficiency defines an essential developmental checkpoint in
definitive hematopoiesis.";
Cell 93:397-409(1998).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
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).
[15]
INTERACTION WITH SIRPA.
PubMed=10842184; DOI=10.1074/jbc.M004238200;
Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.;
"Negative regulation of growth hormone receptor/JAK2 signaling by
signal regulatory protein alpha.";
J. Biol. Chem. 275:28222-28229(2000).
[16]
FUNCTION, AND INTERACTION WITH EPOR.
PubMed=11779507; DOI=10.1016/S1097-2765(01)00401-4;
Huang L.J., Constantinescu S.N., Lodish H.F.;
"The N-terminal domain of Janus kinase 2 is required for Golgi
processing and cell surface expression of erythropoietin receptor.";
Mol. Cell 8:1327-1338(2001).
[17]
INTERACTION WITH LEPR.
PubMed=11923481; DOI=10.1210/mend.16.4.0800;
Bahrenberg G., Behrmann I., Barthel A., Hekerman P., Heinrich P.C.,
Joost H.G., Becker W.;
"Identification of the critical sequence elements in the cytoplasmic
domain of leptin receptor isoforms required for Janus kinase/signal
transducer and activator of transcription activation by receptor
heterodimers.";
Mol. Endocrinol. 16:859-872(2002).
[18]
PHOSPHORYLATION AT TYR-119, AND MUTAGENESIS OF TYR-119.
PubMed=17024180; DOI=10.1038/sj.emboj.7601365;
Funakoshi-Tago M., Pelletier S., Matsuda T., Parganas E., Ihle J.N.;
"Receptor specific downregulation of cytokine signaling by
autophosphorylation in the FERM domain of Jak2.";
EMBO J. 25:4763-4772(2006).
[19]
INTERACTION WITH SH2B1, AND PHOSPHORYLATION AT TYR-813.
PubMed=17565041; DOI=10.1210/me.2007-0111;
Li Z., Zhou Y., Carter-Su C., Myers M.G. Jr., Rui L.;
"SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813
phosphorylation-dependent and -independent mechanisms.";
Mol. Endocrinol. 21:2270-2281(2007).
[20]
PHOSPHORYLATION AT TYR-868; TYR-966; TYR-972 AND TYR-1008, AND
MUTAGENESIS OF TYR-868; TYR-966; TYR-972 AND TYR-1008.
PubMed=20304997; DOI=10.1210/me.2009-0355;
Argetsinger L.S., Stuckey J.A., Robertson S.A., Koleva R.I.,
Cline J.M., Marto J.A., Myers M.G. Jr., Carter-Su C.;
"Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are
autophosphorylated and required for maximal JAK2 kinase activity.";
Mol. Endocrinol. 24:1062-1076(2010).
[21]
PHOSPHORYLATION AT TYR-372 AND TYR-373, AND MUTAGENESIS OF TYR-372 AND
TYR-373.
PubMed=21726629; DOI=10.1016/j.cellsig.2011.06.015;
Sayyah J., Gnanasambandan K., Kamarajugudda S., Tsuda S.,
Caldwell-Busby J., Sayeski P.P.;
"Phosphorylation of Y372 is critical for Jak2 tyrosine kinase
activation.";
Cell. Signal. 23:1806-1815(2011).
[22]
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).
[23]
REVIEW ON FUNCTION.
PubMed=17208428; DOI=10.1016/j.gde.2006.12.009;
Ihle J.N., Gilliland D.G.;
"Jak2: normal function and role in hematopoietic disorders.";
Curr. Opin. Genet. Dev. 17:8-14(2007).
[24]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 810-820 IN COMPLEX WITH
SH2B1, AND PHOSPHORYLATION AT TYR-813.
PubMed=16824542; DOI=10.1016/j.jmb.2006.05.070;
Hu J., Hubbard S.R.;
"Structural basis for phosphotyrosine recognition by the Src homology-
2 domains of the adapter proteins SH2-B and APS.";
J. Mol. Biol. 361:69-79(2006).
-!- 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. 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, 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. Plays a role in cell cycle by
phosphorylating CDKN1B. 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. {ECO:0000269|PubMed:11779507,
ECO:0000269|PubMed:20098430, ECO:0000269|PubMed:21423214,
ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:8702638,
ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9590173,
ECO:0000269|PubMed:9590174}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- 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};
-!- ENZYME REGULATION: Regulated by autophosphorylation, can both
activate or decrease activity. Heme regulates its activity by
enhancing the phosphorylation on Tyr-1007 and Tyr-1008 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with IL23R, SKB1 and STAM2 (By similarity).
Interacts with EPOR (PubMed:8343951, PubMed:11779507). Interacts
with LYN (PubMed:9573010). Interacts with SIRPA (PubMed:10842184).
Interacts with SH2B1 (PubMed:17565041, PubMed:16824542). Interacts
with TEC (PubMed:9473212). Interacts with IFNGR2 (via
intracellular domain) (By similarity). Interacts with LEPR
(Isoform B) (PubMed:11923481). Interacts with HSP90AB1; promotes
functional activation in a heat shock-dependent manner (By
similarity). {ECO:0000250|UniProtKB:O60674,
ECO:0000269|PubMed:10842184, ECO:0000269|PubMed:11779507,
ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:16824542,
ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:7775438,
ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:9473212,
ECO:0000269|PubMed:9573010}.
-!- INTERACTION:
P46527:CDKN1B (xeno); NbExp=7; IntAct=EBI-646604, EBI-519280;
P14753:Epor; NbExp=4; IntAct=EBI-646604, EBI-617901;
P20491:Fcer1g; NbExp=2; IntAct=EBI-646604, EBI-9306159;
Q5VWK5:IL23R (xeno); NbExp=2; IntAct=EBI-646604, EBI-10248005;
P48356:Lepr; NbExp=3; IntAct=EBI-646604, EBI-2257257;
P10686:Plcg1 (xeno); NbExp=3; IntAct=EBI-646604, EBI-520788;
Q91ZM2:Sh2b1; NbExp=3; IntAct=EBI-646604, EBI-7178606;
P29353:SHC1 (xeno); NbExp=2; IntAct=EBI-646604, EBI-78835;
-!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed throughout most
tissues.
-!- 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.
-!- PTM: Autophosphorylated, leading to regulate its activity. Leptin
promotes phosphorylation on tyrosine residues, including
phosphorylation on Tyr-813 (PubMed:16824542, PubMed:17565041).
Autophosphorylation on Tyr-119 in response to EPO down-regulates
its kinase activity (PubMed:17024180). Autophosphorylation on Tyr-
868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are
required for maximal kinase activity (PubMed:20304997). Also
phosphorylated by TEC (PubMed:9473212). Phosphorylated on tyrosine
residues in response to interferon gamma signaling (By
similarity). {ECO:0000250|UniProtKB:O60674,
ECO:0000269|PubMed:16824542, ECO:0000269|PubMed:17024180,
ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:20304997,
ECO:0000269|PubMed:21726629, ECO:0000269|PubMed:9473212}.
-!- DISRUPTION PHENOTYPE: Embryos are anemic and die around day 12.5
post-coitum (dpc). Primitive erythrocytes are found, but
definitive erythropoiesis is absent. Fetal liver myeloid
progenitors, although present based on the expression of lineage
specific markers, fail to respond to erythropoietin (Epo),
thrombopoietin (Thpo), interleukin-3 (Il3), or granulocyte and
macrophage colony-stimulating factor 1 (Csf1 and Csf2). Fetal
liver BFU-E and CFU-E colonies are completely absent. However,
multilineage hematopoietic stem cells (CD34(low), c-kit(pos)) can
be found, and B-lymphopoiesis appears intact.
{ECO:0000269|PubMed:9590173, ECO:0000269|PubMed:9590174}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. JAK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L16956; AAB41327.1; -; mRNA.
EMBL; BC054807; AAH54807.1; -; mRNA.
EMBL; BC059834; AAH59834.1; -; mRNA.
EMBL; M33423; AAA40014.1; -; mRNA.
PIR; A47511; A47511.
PIR; B39577; B39577.
PIR; JH0114; JH0114.
RefSeq; NP_001041642.1; NM_001048177.2.
RefSeq; NP_032439.2; NM_008413.3.
UniGene; Mm.275839; -.
PDB; 2HDX; X-ray; 2.35 A; G/H/I/J/K/L=810-820.
PDB; 4GL9; X-ray; 3.90 A; A/B/C/D=836-1129.
PDBsum; 2HDX; -.
PDBsum; 4GL9; -.
ProteinModelPortal; Q62120; -.
SMR; Q62120; -.
BioGrid; 200857; 31.
CORUM; Q62120; -.
DIP; DIP-320N; -.
IntAct; Q62120; 22.
MINT; MINT-188474; -.
STRING; 10090.ENSMUSP00000025705; -.
BindingDB; Q62120; -.
ChEMBL; CHEMBL1649049; -.
iPTMnet; Q62120; -.
PhosphoSitePlus; Q62120; -.
MaxQB; Q62120; -.
PaxDb; Q62120; -.
PRIDE; Q62120; -.
GeneID; 16452; -.
KEGG; mmu:16452; -.
CTD; 3717; -.
MGI; MGI:96629; Jak2.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000049158; -.
HOVERGEN; HBG006195; -.
InParanoid; Q62120; -.
KO; K04447; -.
PhylomeDB; Q62120; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
Reactome; R-MMU-447115; Interleukin-12 family signaling.
Reactome; R-MMU-877312; Regulation of IFNG signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
ChiTaRS; Jak2; mouse.
EvolutionaryTrace; Q62120; -.
PRO; PR:Q62120; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_JAK2; -.
GO; GO:0005901; C:caveola; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
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:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0035401; F:histone kinase activity (H3-Y41 specific); ISS:UniProtKB.
GO; GO:0005143; F:interleukin-12 receptor binding; IPI:MGI.
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:0004672; F:protein kinase activity; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0042976; P:activation of Janus kinase activity; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; ISS:BHF-UCL.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0031103; P:axon regeneration; ISS:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
GO; GO:0036016; P:cellular response to interleukin-3; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; IDA:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0060396; P:growth hormone receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0035409; P:histone H3-Y41 phosphorylation; ISS:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0034050; P:host programmed cell death induced by symbiont; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; IDA:MGI.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
GO; GO:0061180; P:mammary gland epithelium development; IMP:MGI.
GO; GO:0031959; P:mineralocorticoid receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; ISS:BHF-UCL.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0050867; P:positive regulation of cell activation; ISS:BHF-UCL.
GO; GO:0045597; P:positive regulation of cell differentiation; ISS:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; ISS:BHF-UCL.
GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:BHF-UCL.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; ISS:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:CACAO.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
GO; GO:0050727; P:regulation of inflammatory response; ISS:BHF-UCL.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0046677; P:response to antibiotic; ISO:MGI.
GO; GO:0097012; P:response to granulocyte macrophage colony-stimulating factor; NAS:BHF-UCL.
GO; GO:0033194; P:response to hydroperoxide; ISS:BHF-UCL.
GO; GO:0070671; P:response to interleukin-12; ISS:BHF-UCL.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0006979; P:response to oxidative stress; ISS:BHF-UCL.
GO; GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
GO; GO:0007262; P:STAT protein import into nucleus; IDA:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:BHF-UCL.
GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:MGI.
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_3-hlx.
InterPro; IPR035963; FERM_2.
InterPro; IPR000299; FERM_domain.
InterPro; IPR035860; JAK2_SH2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR011993; PH_dom-like.
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;
Complete proteome; Cytoplasm; Immunity; Innate immunity; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; SH2 domain; Transferase;
Tyrosine-protein kinase.
CHAIN 1 1129 Tyrosine-protein kinase JAK2.
/FTId=PRO_0000088113.
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.
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}.
MOD_RES 119 119 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:17024180}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000269|PubMed:21726629}.
MOD_RES 373 373 Phosphotyrosine.
{ECO:0000269|PubMed:21726629}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 570 570 Phosphotyrosine.
{ECO:0000250|UniProtKB:O60674}.
MOD_RES 813 813 Phosphotyrosine.
{ECO:0000269|PubMed:16824542,
ECO:0000269|PubMed:17565041}.
MOD_RES 868 868 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20304997}.
MOD_RES 966 966 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20304997}.
MOD_RES 972 972 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20304997}.
MOD_RES 1007 1007 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:9473212}.
MOD_RES 1008 1008 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20304997}.
MUTAGEN 119 119 Y->E: Phosphorylation mimic mutant, leads
to dissociation of JAK2 from the
erythropoietin receptor complex.
{ECO:0000269|PubMed:17024180}.
MUTAGEN 119 119 Y->F: More stably associated with the
erythropoietin receptor complex.
{ECO:0000269|PubMed:17024180}.
MUTAGEN 372 372 Y->F: About 60% loss of STAT1
phosphorylation by JAK2.
{ECO:0000269|PubMed:21726629}.
MUTAGEN 373 373 Y->F: Decreased the ability of JAK2 to
autophosphorylate.
{ECO:0000269|PubMed:21726629}.
MUTAGEN 868 868 Y->F: Reduced activity in response to
growth hormone.
{ECO:0000269|PubMed:20304997}.
MUTAGEN 966 966 Y->F: Reduced activity in response to
growth hormone.
{ECO:0000269|PubMed:20304997}.
MUTAGEN 972 972 Y->F: Reduced activity in response to
growth hormone.
{ECO:0000269|PubMed:20304997}.
MUTAGEN 1008 1008 Y->F: Affects the phosphorylation
pattern. {ECO:0000269|PubMed:20304997}.
CONFLICT 155 155 A -> V (in Ref. 1; AAB41327).
{ECO:0000305}.
CONFLICT 468 468 K -> N (in Ref. 1; AAB41327).
{ECO:0000305}.
CONFLICT 686 686 N -> D (in Ref. 1; AAB41327).
{ECO:0000305}.
CONFLICT 1016 1016 S -> R (in Ref. 4; AAA40014).
{ECO:0000305}.
CONFLICT 1024 1024 E -> Q (in Ref. 1; AAB41327).
{ECO:0000305}.
CONFLICT 1042 1043 VV -> IP (in Ref. 4; AAA40014).
{ECO:0000305}.
CONFLICT 1121 1129 LRVDQIIAA -> FGWIKCGTV (in Ref. 1;
AAB41327). {ECO:0000305}.
SEQUENCE 1129 AA; 130235 MW; DCB90FA000F99631 CRC64;
MGMACLTMTE MEATSTSPVH QNGDIPGSAN SVKQIEPVLQ VYLYHSLGQA EGEYLKFPSG
EYVAEEICVA ASKACGITPV YHNMFALMSE TERIWYPPNH VFHIDESTRH DILYRIRFYF
PHWYCSGSSR TYRYGVSRGA EAPLLDDFVM SYLFAQWRHD FVHGWIKVPV THETQEECLG
MAVLDMMRIA KEKDQTPLAV YNSVSYKTFL PKCVRAKIQD YHILTRKRIR YRFRRFIQQF
SQCKATARNL KLKYLINLET LQSAFYTEQF EVKESARGPS GEEIFATIII TGNGGIQWSR
GKHKESETLT EQDVQLYCDF PDIIDVSIKQ ANQECSNESR IVTVHKQDGK VLEIELSSLK
EALSFVSLID GYYRLTADAH HYLCKEVAPP AVLENIHSNC HGPISMDFAI SKLKKAGNQT
GLYVLRCSPK DFNKYFLTFA VERENVIEYK HCLITKNENG EYNLSGTKRN FSNLKDLLNC
YQMETVRSDS IIFQFTKCCP PKPKDKSNLL VFRTNGISDV QISPTLQRHN NVNQMVFHKI
RNEDLIFNES LGQGTFTKIF KGVRREVGDY GQLHKTEVLL KVLDKAHRNY SESFFEAASM
MSQLSHKHLV LNYGVCVCGE ENILVQEFVK FGSLDTYLKK NKNSINILWK LGVAKQLAWA
MHFLEEKSLI HGNVCAKNIL LIREENRRTG NPPFIKLSDP GISITVLPKD ILQERIPWVP
PECIENPKNL NLATDKWSFG TTLWEICSGG DKPLSALDSQ RKLQFYEDKH QLPAPKWTEL
ANLINNCMDY EPDFRPAFRA VIRDLNSLFT PDYELLTEND MLPNMRIGAL GFSGAFEDRD
PTQFEERHLK FLQQLGKGNF GSVEMCRYDP LQDNTGEVVA VKKLQHSTEE HLRDFEREIE
ILKSLQHDNI VKYKGVCYSA GRRNLRLIME YLPYGSLRDY LQKHKERIDH KKLLQYTSQI
CKGMEYLGTK RYIHRDLATR NILVENENRV KIGDFGLTKV LPQDKEYYKV KEPGESPIFW
YAPESLTESK FSVASDVWSF GVVLYELFTY IEKSKSPPVE FMRMIGNDKQ GQMIVFHLIE
LLKSNGRLPR PEGCPDEIYV IMTECWNNNV SQRPSFRDLS LRVDQIIAA


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