Non-receptor tyrosine kinase and coding gene in humans
JAK2
Available structures
PDB Ortholog search:
PDBe
RCSB List of PDB id codes
5AEP ,
2B7A ,
2W1I ,
2XA4 ,
3E62 ,
3E63 ,
3E64 ,
3FUP ,
3IO7 ,
3IOK ,
3JY9 ,
3KCK ,
3KRR ,
3LPB ,
3Q32 ,
3RVG ,
3TJC ,
3TJD ,
3UGC ,
3ZMM ,
4AQC ,
4BBE ,
4BBF ,
4C61 ,
4C62 ,
4D0W ,
4D0X ,
4D1S ,
4E4M ,
4E6D ,
4E6Q ,
4F08 ,
4F09 ,
4FVP ,
4FVQ ,
4FVR ,
4GFM ,
4GMY ,
4HGE ,
4IVA ,
4JI9 ,
4JIA ,
4P7E ,
4ZIM ,
4YTC ,
4YTF ,
4YTH ,
4YTI ,
5CF4 ,
5CF5 ,
5CF6 ,
5CF8 ,
5I4N ,
4Z32 ,
5L3A
Identifiers
Aliases
JAK2 , JTK10, THCYT3, Janus kinase 2, MAX2External IDs
OMIM :
147796 ;
MGI :
96629 ;
HomoloGene :
21033 ;
GeneCards :
JAK2 ;
OMA :
JAK2 - orthologs
Wikidata
Janus kinase 2 (commonly called JAK2 ) is a
non-receptor tyrosine kinase . It is a member of the
Janus kinase family and has been implicated in signaling by members of the
type II cytokine receptor family (e.g.
interferon receptors), the
GM-CSF receptor family (
IL-3R ,
IL-5R and
GM-CSF-R ), the
gp130 receptor family (e.g.,
IL-6R ), and the single chain receptors (e.g.
Epo-R ,
Tpo-R ,
GH-R ,
PRL-R ).
[5]
[6]
The distinguishing feature between janus kinase 2 and other JAK kinases is the lack of Src homology binding domains (
SH2 /
SH3 ) and the presence of up to seven
JAK homology domains (JH1-JH7). Nonetheless the terminal JH domains retain a high level of homology to tyrosine kinase domains. An interesting note is that only one of these carboxy-terminal JH domains retains full kinase function (JH1) while the other (JH2), previously thought to have no kinase functionality and accordingly termed a
pseudokinase domain , has since been found to be catalytically active, albeit at only 10% that of the JH1 domain.
[7]
[8]
Loss of Jak2 is lethal by embryonic day 12 in mice.
[9]
JAK2
orthologs
[10] have been identified in all
mammals for which complete genome data are available.
Clinical significance
JAK2 gene fusions with the TEL (ETV6 ) (
TEL-JAK2 ) and PCM1 genes have been found in patients suffering
leukemia , particularly
clonal eosinophilia forms of the disease.
[11]
[12]
[13]
Mutations in JAK2 have been implicated in
polycythemia vera ,
essential thrombocythemia , and
myelofibrosis as well as other
myeloproliferative disorders .
[14] This mutation (V617F), a change of
valine to
phenylalanine at the 617 position, appears to render
hematopoietic cells more sensitive to growth factors such as
erythropoietin and
thrombopoietin , because the receptors for these growth factors require JAK2 for signal transduction.
Jak2 mutation, when demonstrable, is one of the methods of diagnosing
polycythemia vera .
[15]
Interactions
Janus kinase 2 has been shown to
interact with:
Prolactin signals through JAK2 are dependent on
STAT5 , and on the
RUSH transcription factors .
[59]
See also
References
^
a
b
c
GRCh38: Ensembl release 89: ENSG00000096968 –
Ensembl , May 2017
^
a
b
c
GRCm38: Ensembl release 89: ENSMUSG00000024789 –
Ensembl , May 2017
^
"Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^
"Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA (June 1998).
"Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice" . Endocrine Reviews . 19 (3): 225–68.
doi :
10.1210/edrv.19.3.0334 .
PMID
9626554 .
^ Brooks AJ, Dai W, O'Mara ML, Abankwa D, Chhabra Y, Pelekanos RA, et al. (2014). "Mechanism of activation of protein kinase JAK2 by the growth hormone receptor". Science . 344 (6185): 1249783.
doi :
10.1126/science.1249783 .
PMID
24833397 .
S2CID
27946074 .
^ Morgan KJ, Gilliland DG (2008). "A role for JAK2 mutations in myeloproliferative diseases". Annual Review of Medicine . 59 (1): 213–22.
doi :
10.1146/annurev.med.59.061506.154159 .
PMID
17919086 .
^ Ungureanu D, Wu J, Pekkala T, Niranjan Y, Young C, Jensen ON, Xu CF, Neubert TA, Skoda RC, Hubbard SR, Silvennoinen O (August 2011).
"The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling" . Nature Structural & Molecular Biology . 18 (9): 971–976.
doi :
10.1038/nsmb.2099 .
PMC
4504201 .
PMID
21841788 .
^ Neubauer H, Cumano A, Müller M, Wu H, Huffstadt U, Pfeffer K (May 1998).
"Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis" . Cell . 93 (3): 397–409.
doi :
10.1016/S0092-8674(00)81168-X .
PMID
9590174 .
S2CID
11375232 .
^
"OrthoMaM phylogenetic marker: JAK2 coding sequence" . [
permanent dead link ]
^ Lacronique V, Boureux A, Valle VD, Poirel H, Quang CT, Mauchauffé M, Berthou C, Lessard M, Berger R, Ghysdael J, Bernard OA (November 1997). "A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia". Science . 278 (5341): 1309–12.
Bibcode :
1997Sci...278.1309L .
doi :
10.1126/science.278.5341.1309 .
PMID
9360930 .
^ Reiter A, Walz C, Watmore A, Schoch C, Blau I, Schlegelberger B, Berger U, Telford N, Aruliah S, Yin JA, Vanstraelen D, Barker HF, Taylor PC, O'Driscoll A, Benedetti F, Rudolph C, Kolb HJ, Hochhaus A, Hehlmann R, Chase A, Cross NC (April 2005).
"The t(8;9)(p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2" . Cancer Research . 65 (7): 2662–7.
doi :
10.1158/0008-5472.CAN-04-4263 .
PMID
15805263 .
^ Reiter A, Gotlib J (2017).
"Myeloid neoplasms with eosinophilia" . Blood . 129 (6): 704–714.
doi :
10.1182/blood-2016-10-695973 .
PMID
28028030 .
^ Kralovics R, Passamonti F, Buser AS, Teo SS, Tiedt R, Passweg JR, Tichelli A, Cazzola M, Skoda RC (April 2005).
"A gain-of-function mutation of JAK2 in myeloproliferative disorders" . The New England Journal of Medicine . 352 (17): 1779–90.
doi :
10.1056/NEJMoa051113 .
hdl :
11383/2023329 .
PMID
15858187 .
^ Scott LM (August 2011).
"The JAK2 exon 12 mutations: a comprehensive review" . American Journal of Hematology . 86 (8): 668–76.
doi :
10.1002/ajh.22063 .
PMID
21674578 .
S2CID
2905512 .
^ Sarkar S, Pollack BP, Lin KT, Kotenko SV, Cook JR, Lewis A, Pestka S (December 2001).
"hTid-1, a human DnaJ protein, modulates the interferon signaling pathway" . The Journal of Biological Chemistry . 276 (52): 49034–42.
doi :
10.1074/jbc.M103683200 .
PMID
11679576 .
^ Olayioye MA, Beuvink I, Horsch K, Daly JM, Hynes NE (June 1999).
"ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases" . The Journal of Biological Chemistry . 274 (24): 17209–18.
doi :
10.1074/jbc.274.24.17209 .
PMID
10358079 .
^ Huang LJ, Constantinescu SN, Lodish HF (December 2001).
"The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor" . Molecular Cell . 8 (6): 1327–38.
doi :
10.1016/S1097-2765(01)00401-4 .
PMID
11779507 .
^ Witthuhn BA, Quelle FW, Silvennoinen O, Yi T, Tang B, Miura O, Ihle JN (July 1993). "JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin". Cell . 74 (2): 227–36.
doi :
10.1016/0092-8674(93)90414-L .
PMID
8343951 .
S2CID
37503350 .
^ Sayeski PP, Ali MS, Safavi A, Lyles M, Kim SO, Frank SJ, Bernstein KE (November 1999).
"A catalytically active Jak2 is required for the angiotensin II-dependent activation of Fyn" . The Journal of Biological Chemistry . 274 (46): 33131–42.
doi :
10.1074/jbc.274.46.33131 .
PMID
10551884 .
^ Chauhan D, Kharbanda SM, Ogata A, Urashima M, Frank D, Malik N, Kufe DW, Anderson KC (December 1995).
"Oncostatin M induces association of Grb2 with Janus kinase JAK2 in multiple myeloma cells" . The Journal of Experimental Medicine . 182 (6): 1801–6.
doi :
10.1084/jem.182.6.1801 .
PMC
2192257 .
PMID
7500025 .
^ Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (December 1995).
"Involvement of Janus kinases in the insulin signaling pathway" . European Journal of Biochemistry . 234 (2): 656–60.
doi :
10.1111/j.1432-1033.1995.656_b.x .
PMID
8536716 .
^ Frank SJ, Yi W, Zhao Y, Goldsmith JF, Gilliland G, Jiang J, Sakai I, Kraft AS (June 1995).
"Regions of the JAK2 tyrosine kinase required for coupling to the growth hormone receptor" . The Journal of Biological Chemistry . 270 (24): 14776–85.
doi :
10.1074/jbc.270.24.14776 .
PMID
7540178 .
^ VanderKuur JA, Wang X, Zhang L, Campbell GS, Allevato G, Billestrup N, Norstedt G, Carter-Su C (August 1994).
"Domains of the growth hormone receptor required for association and activation of JAK2 tyrosine kinase" . The Journal of Biological Chemistry . 269 (34): 21709–17.
doi :
10.1016/S0021-9258(17)31863-X .
PMID
8063815 .
^ Hellgren G, Jansson JO, Carlsson LM, Carlsson B (June 1999). "The growth hormone receptor associates with Jak1, Jak2 and Tyk2 in human liver". Growth Hormone & IGF Research . 9 (3): 212–8.
doi :
10.1054/ghir.1999.0111 .
PMID
10502458 .
^ Gual P, Baron V, Lequoy V, Van Obberghen E (March 1998).
"Interaction of Janus kinases JAK-1 and JAK-2 with the insulin receptor and the insulin-like growth factor-1 receptor" . Endocrinology . 139 (3): 884–93.
doi :
10.1210/endo.139.3.5829 .
PMID
9492017 .
^ Kawazoe Y, Naka T, Fujimoto M, Kohzaki H, Morita Y, Narazaki M, Okumura K, Saitoh H, Nakagawa R, Uchiyama Y, Akira S, Kishimoto T (January 2001).
"Signal transducer and activator of transcription (STAT)-induced STAT inhibitor 1 (SSI-1)/suppressor of cytokine signaling 1 (SOCS1) inhibits insulin signal transduction pathway through modulating insulin receptor substrate 1 (IRS-1) phosphorylation" . The Journal of Experimental Medicine . 193 (2): 263–9.
doi :
10.1084/jem.193.2.263 .
PMC
2193341 .
PMID
11208867 .
^ Yamamoto K, Shibata F, Miura O, Kamiyama R, Hirosawa S, Miyasaka N (April 1999). "Physical interaction between interleukin-12 receptor beta 2 subunit and Jak2 tyrosine kinase: Jak2 associates with cytoplasmic membrane-proximal region of interleukin-12 receptor beta 2 via amino-terminus". Biochemical and Biophysical Research Communications . 257 (2): 400–4.
doi :
10.1006/bbrc.1999.0479 .
PMID
10198225 .
^ Ogata N, Kouro T, Yamada A, Koike M, Hanai N, Ishikawa T, Takatsu K (April 1998).
"JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation" . Blood . 91 (7): 2264–71.
doi :
10.1182/blood.V91.7.2264 .
PMID
9516124 .
^
a
b
c Fuhrer DK, Yang YC (July 1996). "Complex formation of JAK2 with PP2A, P13K, and Yes in response to the hematopoietic cytokine interleukin-11". Biochemical and Biophysical Research Communications . 224 (2): 289–96.
doi :
10.1006/bbrc.1996.1023 .
PMID
8702385 .
^ Zhu T, Goh EL, Lobie PE (April 1998).
"Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription" . The Journal of Biological Chemistry . 273 (17): 10682–9.
doi :
10.1074/jbc.273.17.10682 .
PMID
9553131 .
^ Ryu H, Lee JH, Kim KS, Jeong SM, Kim PH, Chung HT (August 2000).
"Regulation of neutrophil adhesion by pituitary growth hormone accompanies tyrosine phosphorylation of Jak2, p125FAK, and paxillin" . Journal of Immunology . 165 (4): 2116–23.
doi :
10.4049/jimmunol.165.4.2116 .
PMID
10925297 .
^ Yin T, Shen R, Feng GS, Yang YC (January 1997).
"Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases" . The Journal of Biological Chemistry . 272 (2): 1032–7.
doi :
10.1074/jbc.272.2.1032 .
PMID
8995399 .
^ Tauchi T, Damen JE, Toyama K, Feng GS, Broxmeyer HE, Krystal G (June 1996).
"Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis" . Blood . 87 (11): 4495–501.
doi :
10.1182/blood.V87.11.4495.bloodjournal87114495 .
PMID
8639815 .
^ Maegawa H, Kashiwagi A, Fujita T, Ugi S, Hasegawa M, Obata T, Nishio Y, Kojima H, Hidaka H, Kikkawa R (November 1996). "SHPTP2 serves adapter protein linking between Janus kinase 2 and insulin receptor substrates". Biochemical and Biophysical Research Communications . 228 (1): 122–7.
doi :
10.1006/bbrc.1996.1626 .
PMID
8912646 .
^ Jiao H, Berrada K, Yang W, Tabrizi M, Platanias LC, Yi T (December 1996).
"Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1" . Molecular and Cellular Biology . 16 (12): 6985–92.
doi :
10.1128/mcb.16.12.6985 .
PMC
231702 .
PMID
8943354 .
^ Wu DW, Stark KC, Dunnington D, Dillon SB, Yi T, Jones C, Pelus LM (February 2000). "SH2-Containing protein tyrosine phosphatase-1 (SHP-1) association with Jak2 in UT-7/Epo cells". Blood Cells, Molecules & Diseases . 26 (1): 15–24.
doi :
10.1006/bcmd.2000.0273 .
PMID
10772872 .
^ Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (October 1999).
"The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity" . The Journal of Biological Chemistry . 274 (44): 31531–42.
doi :
10.1074/jbc.274.44.31531 .
PMID
10531356 .
^ Rui L, Mathews LS, Hotta K, Gustafson TA, Carter-Su C (November 1997).
"Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2 involved in growth hormone signaling" . Molecular and Cellular Biology . 17 (11): 6633–44.
doi :
10.1128/mcb.17.11.6633 .
PMC
232517 .
PMID
9343427 .
^ Xie S, Lin H, Sun T, Arlinghaus RB (October 2002).
"Jak2 is involved in c-Myc induction by Bcr-Abl" . Oncogene . 21 (47): 7137–46.
doi :
10.1038/sj.onc.1205942 .
PMID
12370803 .
^ VanderKuur J, Allevato G, Billestrup N, Norstedt G, Carter-Su C (March 1995).
"Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2" . The Journal of Biological Chemistry . 270 (13): 7587–93.
doi :
10.1074/jbc.270.13.7587 .
PMID
7535773 .
^ Giordano V, De Falco G, Chiari R, Quinto I, Pelicci PG, Bartholomew L, Delmastro P, Gadina M, Scala G (May 1997).
"Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase" . Journal of Immunology . 158 (9): 4097–103.
doi :
10.4049/jimmunol.158.9.4097 .
PMID
9126968 .
^ Sasaki A, Yasukawa H, Shouda T, Kitamura T, Dikic I, Yoshimura A (September 2000).
"CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2" . The Journal of Biological Chemistry . 275 (38): 29338–47.
doi :
10.1074/jbc.M003456200 .
PMID
10882725 .
^ Sasaki A, Yasukawa H, Suzuki A, Kamizono S, Syoda T, Kinjyo I, Sasaki M, Johnston JA, Yoshimura A (June 1999).
"Cytokine-inducible SH2 protein-3 (CIS3/SOCS3) inhibits Janus tyrosine kinase by binding through the N-terminal kinase inhibitory region as well as SH2 domain" . Genes to Cells . 4 (6): 339–51.
doi :
10.1046/j.1365-2443.1999.00263.x .
PMID
10421843 .
S2CID
24871585 .
^
a
b Masuhara M, Sakamoto H, Matsumoto A, Suzuki R, Yasukawa H, Mitsui K, Wakioka T, Tanimura S, Sasaki A, Misawa H, Yokouchi M, Ohtsubo M, Yoshimura A (October 1997). "Cloning and characterization of novel CIS family genes". Biochemical and Biophysical Research Communications . 239 (2): 439–46.
doi :
10.1006/bbrc.1997.7484 .
PMID
9344848 .
^
a
b Barahmand-Pour F, Meinke A, Groner B, Decker T (May 1998).
"Jak2-Stat5 interactions analyzed in yeast" . The Journal of Biological Chemistry . 273 (20): 12567–75.
doi :
10.1074/jbc.273.20.12567 .
PMID
9575217 .
^
a
b Fujitani Y, Hibi M, Fukada T, Takahashi-Tezuka M, Yoshida H, Yamaguchi T, Sugiyama K, Yamanaka Y, Nakajima K, Hirano T (February 1997).
"An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT" . Oncogene . 14 (7): 751–61.
doi :
10.1038/sj.onc.1200907 .
PMID
9047382 .
^ Takeshita T, Arita T, Higuchi M, Asao H, Endo K, Kuroda H, Tanaka N, Murata K, Ishii N, Sugamura K (April 1997).
"STAM, signal transducing adaptor molecule, is associated with Janus kinases and involved in signaling for cell growth and c-myc induction" . Immunity . 6 (4): 449–57.
doi :
10.1016/S1074-7613(00)80288-5 .
PMID
9133424 .
^ Yasukawa H, Misawa H, Sakamoto H, Masuhara M, Sasaki A, Wakioka T, Ohtsuka S, Imaizumi T, Matsuda T, Ihle JN, Yoshimura A (March 1999).
"The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop" . The EMBO Journal . 18 (5): 1309–20.
doi :
10.1093/emboj/18.5.1309 .
PMC
1171221 .
PMID
10064597 .
^ Dif F, Saunier E, Demeneix B, Kelly PA, Edery M (December 2001).
"Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor" . Endocrinology . 142 (12): 5286–93.
doi :
10.1210/endo.142.12.8549 .
PMID
11713228 .
^ Endo TA, Masuhara M, Yokouchi M, Suzuki R, Sakamoto H, Mitsui K, Matsumoto A, Tanimura S, Ohtsubo M, Misawa H, Miyazaki T, Leonor N, Taniguchi T, Fujita T, Kanakura Y, Komiya S, Yoshimura A (June 1997).
"A new protein containing an SH2 domain that inhibits JAK kinases" . Nature . 387 (6636): 921–4.
Bibcode :
1997Natur.387..921E .
doi :
10.1038/43213 .
PMID
9202126 .
S2CID
4347361 .
^ Pezet A, Favre H, Kelly PA, Edery M (August 1999).
"Inhibition and restoration of prolactin signal transduction by suppressors of cytokine signaling" . The Journal of Biological Chemistry . 274 (35): 24497–502.
doi :
10.1074/jbc.274.35.24497 .
PMID
10455112 .
^ Ungureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O (May 2002).
"Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1" . Molecular and Cellular Biology . 22 (10): 3316–26.
doi :
10.1128/MCB.22.10.3316-3326.2002 .
PMC
133778 .
PMID
11971965 .
^ Takahashi-Tezuka M, Hibi M, Fujitani Y, Fukada T, Yamaguchi T, Hirano T (May 1997).
"Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through JAK" . Oncogene . 14 (19): 2273–82.
doi :
10.1038/sj.onc.1201071 .
PMID
9178903 .
^ Yamashita Y, Watanabe S, Miyazato A, Ohya Ki, Ikeda U, Shimada K, Komatsu N, Hatake K, Miura Y, Ozawa K, Mano H (March 1998).
"Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription" . Blood . 91 (5): 1496–507.
doi :
10.1182/blood.V91.5.1496 .
PMID
9473212 .
^ Guo D, Dunbar JD, Yang CH, Pfeffer LM, Donner DB (March 1998).
"Induction of Jak/STAT signaling by activation of the type 1 TNF receptor" . Journal of Immunology . 160 (6): 2742–50.
doi :
10.4049/jimmunol.160.6.2742 .
PMID
9510175 .
^ Shigematsu H, Iwasaki H, Otsuka T, Ohno Y, Arima F, Niho Y (May 1997).
"Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity" . The Journal of Biological Chemistry . 272 (22): 14334–40.
doi :
10.1074/jbc.272.22.14334 .
PMID
9162069 .
^ Matsuguchi T, Inhorn RC, Carlesso N, Xu G, Druker B, Griffin JD (January 1995).
"Tyrosine phosphorylation of p95Vav in myeloid cells is regulated by GM-CSF, IL-3 and steel factor and is constitutively increased by p210BCR/ABL" . EMBO J . 14 (2): 257–65.
doi :
10.1002/j.1460-2075.1995.tb06999.x .
PMC
398079 .
PMID
7530656 .
^ Helmer RA, Panchoo M, Dertien JS, Bhakta SM, Hewetson A, Chilton BS (August 2010).
"Prolactin-induced Jak2 phosphorylation of RUSH: a key element in Jak/RUSH signaling" . Molecular and Cellular Endocrinology . 325 (1–2): 143–9.
doi :
10.1016/j.mce.2010.05.010 .
PMC
2902710 .
PMID
20562009 .
Further reading
Berger R (May 2006). "[A recurrent mutation of the JAK2 gene in chronic myeloproliferative disorders]". Pathologie-Biologie . 54 (4): 182–4.
doi :
10.1016/j.patbio.2005.07.002 .
PMID
16084028 .
Pargade V, Darnige L, Gaussem P (2006). "[Acquired mutation of JAK2 tyrosine kinase and polycythaemia vera]". Annales de Biologie Clinique . 64 (1): 3–9.
PMID
16420986 .
Staerk J, Kallin A, Royer Y, Diaconu CC, Dusa A, Demoulin JB, Vainchenker W, Constantinescu SN (March 2007). "JAK2, the JAK2 V617F mutant and cytokine receptors". Pathologie-Biologie . 55 (2): 88–91.
doi :
10.1016/j.patbio.2006.06.003 .
PMID
16904848 .
Hsu HC (March 2007).
"Pathogenetic role of JAK2 V617F mutation in chronic myeloproliferative disorders" . Journal of the Chinese Medical Association . 70 (3): 89–93.
doi :
10.1016/S1726-4901(09)70337-5 .
PMID
17389152 .
S2CID
33300937 .
External links
Activity Regulation Classification Kinetics Types
Chemokine
CSF
Interferon
IFNAR (α/β, I)
Agonists:
Albinterferon
Interferon alpha (interferon alfa, IFN-α)
Interferon alfa (
IFNA1 ,
IFNA2 ,
IFNA4 ,
IFNA5 ,
IFNA6 ,
IFNA7 ,
IFNA8 ,
IFNA10 ,
IFNA13 ,
IFNA14 ,
IFNA16 ,
IFNA17 ,
IFNA21 )
Interferon alfa 2a
Interferon alfa 2b
Interferon alfa n1
Interferon alfacon-1
Interferon alpha-n3
Interferon beta (IFN-β) (
IFNB1 ,
IFNB3 )
Interferon beta 1a
Interferon beta 1b
Interferon kappa (IFN-ε/κ/τ/ζ, IFNK)
Interferon omega (IFN-ω, IFNW1)
Peginterferon alfa-2a
Peginterferon alfa-2b
IFNGR (γ, II)
IFNLR (λ, III)
See IL-28R (IFNLR)
here instead.
Interleukin
TGFβ
TNF Others