JAK2_MOUSE
ID JAK2_MOUSE Reviewed; 1132 AA.
AC Q62120; G5E852; Q62124; Q7TQD0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Tyrosine-protein kinase JAK2 {ECO:0000305};
DE EC=2.7.10.2 {ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21726629};
DE AltName: Full=Janus kinase 2;
DE Short=JAK-2;
GN Name=Jak2 {ECO:0000312|MGI:MGI:96629};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8378315; DOI=10.1073/pnas.90.18.8429;
RA Silvennoinen O., Witthuhn B.A., Quelle F.W., Cleveland J.L., Yi T.,
RA Ihle J.N.;
RT "Structure of the murine Jak2 protein-tyrosine kinase and its role in
RT interleukin 3 signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8429-8433(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
RX PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
RA Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
RT "The application of the polymerase chain reaction to cloning members of the
RT protein tyrosine kinase family.";
RL Gene 85:67-74(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 973-1043.
RX PubMed=2466296; DOI=10.1073/pnas.86.5.1603;
RA Wilks A.F.;
RT "Two putative protein-tyrosine kinases identified by application of the
RT polymerase chain reaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1603-1607(1989).
RN [6]
RP FUNCTION, INTERACTION WITH EPOR, PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=8343951; DOI=10.1016/0092-8674(93)90414-l;
RA Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O.,
RA Ihle J.N.;
RT "JAK2 associates with the erythropoietin receptor and is tyrosine
RT phosphorylated and activated following stimulation with erythropoietin.";
RL Cell 74:227-236(1993).
RN [7]
RP INTERACTION WITH CYTOKINE/INTERFERON/GROWTH HORMONE RECEPTORS.
RX PubMed=7775438; DOI=10.1074/jbc.270.23.14015;
RA Zhao Y., Wagner F., Frank S.J., Kraft A.S.;
RT "The amino-terminal portion of the JAK2 protein kinase is necessary for
RT binding and phosphorylation of the granulocyte-macrophage colony-
RT stimulating factor receptor beta c chain.";
RL J. Biol. Chem. 270:13814-13818(1995).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF STAT5A AND STAT5B.
RX PubMed=8702638; DOI=10.1074/jbc.271.32.19483;
RA Nakamura N., Chin H., Miyasaka N., Miura O.;
RT "An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera
RT induces tyrosine phosphorylation of Stat5 and transduces a growth signal in
RT hematopoietic cells.";
RL J. Biol. Chem. 271:19483-19488(1996).
RN [9]
RP FUNCTION, INTERACTION WITH TEC, AND PHOSPHORYLATION AT TYR-1007 BY TEC.
RX PubMed=9473212;
RA Yamashita Y., Watanabe S., Miyazato A., Ohya K., Ikeda U., Shimada K.,
RA Komatsu N., Hatake K., Miura Y., Ozawa K., Mano H.;
RT "Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-
RT fos transcription.";
RL Blood 91:1496-1507(1998).
RN [10]
RP INTERACTION WITH LYN.
RX PubMed=9573010;
RA Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.;
RT "Lyn physically associates with the erythropoietin receptor and may play a
RT role in activation of the Stat5 pathway.";
RL Blood 91:3734-3745(1998).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9590173; DOI=10.1016/s0092-8674(00)81167-8;
RA Parganas E., Wang D., Stravopodis D., Topham D.J., Marine J.C., Teglund S.,
RA Vanin E.F., Bodner S., Colamonici O.R., van Deursen J.M., Grosveld G.,
RA Ihle J.N.;
RT "Jak2 is essential for signaling through a variety of cytokine receptors.";
RL Cell 93:385-395(1998).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9590174; DOI=10.1016/s0092-8674(00)81168-x;
RA Neubauer H., Cumano A., Muller M., Wu H., Huffstadt U., Pfeffer K.;
RT "Jak2 deficiency defines an essential developmental checkpoint in
RT definitive hematopoiesis.";
RL Cell 93:397-409(1998).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP FUNCTION.
RX PubMed=20098430; DOI=10.1038/nm.2079;
RA Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M.,
RA Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M.,
RA Offermanns S., Pacaud P., Loirand G.;
RT "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on
RT vascular tone and blood pressure.";
RL Nat. Med. 16:183-190(2010).
RN [16]
RP INTERACTION WITH SIRPA.
RX PubMed=10842184; DOI=10.1074/jbc.m004238200;
RA Stofega M.R., Argetsinger L.S., Wang H., Ullrich A., Carter-Su C.;
RT "Negative regulation of growth hormone receptor/JAK2 signaling by signal
RT regulatory protein alpha.";
RL J. Biol. Chem. 275:28222-28229(2000).
RN [17]
RP FUNCTION, AND INTERACTION WITH EPOR.
RX PubMed=11779507; DOI=10.1016/s1097-2765(01)00401-4;
RA Huang L.J., Constantinescu S.N., Lodish H.F.;
RT "The N-terminal domain of Janus kinase 2 is required for Golgi processing
RT and cell surface expression of erythropoietin receptor.";
RL Mol. Cell 8:1327-1338(2001).
RN [18]
RP INTERACTION WITH LEPR.
RX PubMed=11923481; DOI=10.1210/mend.16.4.0800;
RA Bahrenberg G., Behrmann I., Barthel A., Hekerman P., Heinrich P.C.,
RA Joost H.G., Becker W.;
RT "Identification of the critical sequence elements in the cytoplasmic domain
RT of leptin receptor isoforms required for Janus kinase/signal transducer and
RT activator of transcription activation by receptor heterodimers.";
RL Mol. Endocrinol. 16:859-872(2002).
RN [19]
RP PHOSPHORYLATION AT TYR-119, AND MUTAGENESIS OF TYR-119.
RX PubMed=17024180; DOI=10.1038/sj.emboj.7601365;
RA Funakoshi-Tago M., Pelletier S., Matsuda T., Parganas E., Ihle J.N.;
RT "Receptor specific downregulation of cytokine signaling by
RT autophosphorylation in the FERM domain of Jak2.";
RL EMBO J. 25:4763-4772(2006).
RN [20]
RP INTERACTION WITH SH2B1, AND PHOSPHORYLATION AT TYR-813.
RX PubMed=17565041; DOI=10.1210/me.2007-0111;
RA Li Z., Zhou Y., Carter-Su C., Myers M.G. Jr., Rui L.;
RT "SH2B1 enhances leptin signaling by both Janus kinase 2 Tyr813
RT phosphorylation-dependent and -independent mechanisms.";
RL Mol. Endocrinol. 21:2270-2281(2007).
RN [21]
RP PHOSPHORYLATION AT TYR-868; TYR-966; TYR-972 AND TYR-1008, MUTAGENESIS OF
RP TYR-868; TYR-966; TYR-972 AND TYR-1008, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=20304997; DOI=10.1210/me.2009-0355;
RA Argetsinger L.S., Stuckey J.A., Robertson S.A., Koleva R.I., Cline J.M.,
RA Marto J.A., Myers M.G. Jr., Carter-Su C.;
RT "Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are
RT autophosphorylated and required for maximal JAK2 kinase activity.";
RL Mol. Endocrinol. 24:1062-1076(2010).
RN [22]
RP PHOSPHORYLATION AT TYR-372 AND TYR-373, MUTAGENESIS OF TYR-372 AND TYR-373,
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=21726629; DOI=10.1016/j.cellsig.2011.06.015;
RA Sayyah J., Gnanasambandan K., Kamarajugudda S., Tsuda S.,
RA Caldwell-Busby J., Sayeski P.P.;
RT "Phosphorylation of Y372 is critical for Jak2 tyrosine kinase activation.";
RL Cell. Signal. 23:1806-1815(2011).
RN [23]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=21368206; DOI=10.1073/pnas.1011115108;
RA Berry D.C., Jin H., Majumdar A., Noy N.;
RT "Signaling by vitamin A and retinol-binding protein regulates gene
RT expression to inhibit insulin responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4340-4345(2011).
RN [24]
RP FUNCTION IN PHOSPHORYLATION OF CDKN1B.
RX PubMed=21423214; DOI=10.1038/onc.2011.68;
RA Jakel H., Weinl C., Hengst L.;
RT "Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor
RT signaling to cell cycle control.";
RL Oncogene 30:3502-3512(2011).
RN [25]
RP REVIEW ON FUNCTION.
RX PubMed=17208428; DOI=10.1016/j.gde.2006.12.009;
RA Ihle J.N., Gilliland D.G.;
RT "Jak2: normal function and role in hematopoietic disorders.";
RL Curr. Opin. Genet. Dev. 17:8-14(2007).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 810-820 IN COMPLEX WITH SH2B1,
RP AND PHOSPHORYLATION AT TYR-813.
RX PubMed=16824542; DOI=10.1016/j.jmb.2006.05.070;
RA Hu J., Hubbard S.R.;
RT "Structural basis for phosphotyrosine recognition by the Src homology-2
RT domains of the adapter proteins SH2-B and APS.";
RL J. Mol. Biol. 361:69-79(2006).
CC -!- FUNCTION: Non-receptor tyrosine kinase involved in various processes
CC such as cell growth, development, differentiation or histone
CC modifications. Mediates essential signaling events in both innate and
CC adaptive immunity. In the cytoplasm, plays a pivotal role in signal
CC transduction via its association with type I receptors such as growth
CC hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR),
CC thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-
CC beta, IFN-gamma and multiple interleukins. Following ligand-binding to
CC cell surface receptors, phosphorylates specific tyrosine residues on
CC the cytoplasmic tails of the receptor, creating docking sites for STATs
CC proteins. Subsequently, phosphorylates the STATs proteins once they are
CC recruited to the receptor. Phosphorylated STATs then form homodimer or
CC heterodimers and translocate to the nucleus to activate gene
CC transcription. For example, cell stimulation with erythropoietin (EPO)
CC during erythropoiesis leads to JAK2 autophosphorylation, activation,
CC and its association with erythropoietin receptor (EPOR) that becomes
CC phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or
CC STAT5B) is recruited, phosphorylated and activated by JAK2. Once
CC activated, dimerized STAT5 translocates into the nucleus and promotes
CC the transcription of several essential genes involved in the modulation
CC of erythropoiesis. Part of a signaling cascade that is activated by
CC increased cellular retinol and that leads to the activation of STAT5
CC (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced
CC ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating
CC CDKN1B. Cooperates with TEC through reciprocal phosphorylation to
CC mediate cytokine-driven activation of FOS transcription. In the
CC nucleus, plays a key role in chromatin by specifically mediating
CC phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag
CC that promotes exclusion of CBX5 (HP1 alpha) from chromatin.
CC {ECO:0000269|PubMed:11779507, ECO:0000269|PubMed:20098430,
CC ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:21423214,
CC ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:8702638,
CC ECO:0000269|PubMed:9473212, ECO:0000269|PubMed:9590173,
CC ECO:0000269|PubMed:9590174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21726629};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely
CC to be the in vivo cofactor. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Regulated by autophosphorylation, can both
CC activate or decrease activity (PubMed:8343951, PubMed:20304997,
CC PubMed:21726629). Heme regulates its activity by enhancing the
CC phosphorylation on Tyr-1007 and Tyr-1008 (By similarity).
CC {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:20304997,
CC ECO:0000269|PubMed:21726629, ECO:0000305|PubMed:8343951}.
CC -!- SUBUNIT: Interacts with IL23R, SKB1 and STAM2 (By similarity).
CC Interacts with EPOR (PubMed:8343951, PubMed:11779507). Interacts with
CC LYN (PubMed:9573010). Interacts with SIRPA (PubMed:10842184). Interacts
CC with SH2B1 (PubMed:17565041, PubMed:16824542). Interacts with TEC
CC (PubMed:9473212). Interacts with IFNGR2 (via intracellular domain) (By
CC similarity). Interacts with LEPR (Isoform B) (PubMed:11923481).
CC Interacts with HSP90AB1; promotes functional activation in a heat
CC shock-dependent manner. Interacts with STRA6 (By similarity). Interacts
CC with ASB2; the interaction targets JAK2 for Notch-induced proteasomal
CC degradation (By similarity). {ECO:0000250|UniProtKB:O60674,
CC ECO:0000269|PubMed:10842184, ECO:0000269|PubMed:11779507,
CC ECO:0000269|PubMed:11923481, ECO:0000269|PubMed:16824542,
CC ECO:0000269|PubMed:17565041, ECO:0000269|PubMed:7775438,
CC ECO:0000269|PubMed:8343951, ECO:0000269|PubMed:9473212,
CC ECO:0000269|PubMed:9573010}.
CC -!- INTERACTION:
CC Q62120; P14753: Epor; NbExp=4; IntAct=EBI-646604, EBI-617901;
CC Q62120; P20491: Fcer1g; NbExp=2; IntAct=EBI-646604, EBI-9306159;
CC Q62120; P48356: Lepr; NbExp=3; IntAct=EBI-646604, EBI-2257257;
CC Q62120; Q91ZM2: Sh2b1; NbExp=3; IntAct=EBI-646604, EBI-7178606;
CC Q62120; P46527: CDKN1B; Xeno; NbExp=7; IntAct=EBI-646604, EBI-519280;
CC Q62120; Q5VWK5: IL23R; Xeno; NbExp=2; IntAct=EBI-646604, EBI-10248005;
CC Q62120; P10686: Plcg1; Xeno; NbExp=3; IntAct=EBI-646604, EBI-520788;
CC Q62120; P29353: SHC1; Xeno; NbExp=2; IntAct=EBI-646604, EBI-78835;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein.
CC Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout most tissues.
CC -!- DOMAIN: Possesses 2 protein kinase domains. The second one probably
CC contains the catalytic domain, while the presence of slight differences
CC suggest a different role for protein kinase 1.
CC -!- PTM: Autophosphorylated, leading to regulate its activity. Leptin
CC promotes phosphorylation on tyrosine residues, including
CC phosphorylation on Tyr-813 (PubMed:16824542, PubMed:17565041).
CC Autophosphorylation on Tyr-119 in response to EPO down-regulates its
CC kinase activity (PubMed:17024180). Autophosphorylation on Tyr-868, Tyr-
CC 966 and Tyr-972 in response to growth hormone (GH) are required for
CC maximal kinase activity (PubMed:20304997). Also phosphorylated by TEC
CC (PubMed:9473212). Phosphorylated on tyrosine residues in response to
CC interferon gamma signaling (By similarity). Phosphorylated on tyrosine
CC residues in response to a signaling cascade that is activated by
CC increased cellular retinol (PubMed:21368206).
CC {ECO:0000250|UniProtKB:O60674, ECO:0000269|PubMed:16824542,
CC ECO:0000269|PubMed:17024180, ECO:0000269|PubMed:17565041,
CC ECO:0000269|PubMed:20304997, ECO:0000269|PubMed:21368206,
CC ECO:0000269|PubMed:21726629, ECO:0000269|PubMed:8343951,
CC ECO:0000269|PubMed:9473212}.
CC -!- PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal
CC degradation which is mediated by ASB1 or ASB2, the substrate-
CC recognition components of probable ECS E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250|UniProtKB:O60674}.
CC -!- DISRUPTION PHENOTYPE: Embryos are anemic and die around day 12.5 post-
CC coitum (dpc). Primitive erythrocytes are found, but definitive
CC erythropoiesis is absent. Fetal liver myeloid progenitors, although
CC present based on the expression of lineage specific markers, fail to
CC respond to erythropoietin (Epo), thrombopoietin (Thpo), interleukin-3
CC (Il3), or granulocyte and macrophage colony-stimulating factor 1 (Csf1
CC and Csf2). Fetal liver BFU-E and CFU-E colonies are completely absent.
CC However, multilineage hematopoietic stem cells (CD34(low), c-kit(pos))
CC can be found, and B-lymphopoiesis appears intact.
CC {ECO:0000269|PubMed:9590173, ECO:0000269|PubMed:9590174}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41327.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L16956; AAB41327.1; ALT_FRAME; mRNA.
DR EMBL; AC119228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054807; AAH54807.1; -; mRNA.
DR EMBL; BC059834; AAH59834.1; -; mRNA.
DR EMBL; M33423; AAA40014.1; -; mRNA.
DR CCDS; CCDS37950.1; -.
DR PIR; A47511; A47511.
DR PIR; B39577; B39577.
DR PIR; JH0114; JH0114.
DR RefSeq; NP_001041642.1; NM_001048177.2.
DR RefSeq; NP_032439.2; NM_008413.3.
DR RefSeq; XP_011245457.1; XM_011247155.2.
DR PDB; 2HDX; X-ray; 2.35 A; G/H/I/J/K/L=810-820.
DR PDB; 4GL9; X-ray; 3.90 A; A/B/C/D=836-1129.
DR PDBsum; 2HDX; -.
DR PDBsum; 4GL9; -.
DR AlphaFoldDB; Q62120; -.
DR SMR; Q62120; -.
DR BioGRID; 200857; 41.
DR ComplexPortal; CPX-388; Interleukin-12-receptor complex.
DR ComplexPortal; CPX-389; Interleukin-23-receptor complex.
DR CORUM; Q62120; -.
DR DIP; DIP-320N; -.
DR DIP; DIP-60238N; -.
DR IntAct; Q62120; 26.
DR MINT; Q62120; -.
DR STRING; 10090.ENSMUSP00000064394; -.
DR BindingDB; Q62120; -.
DR ChEMBL; CHEMBL1649049; -.
DR DrugCentral; Q62120; -.
DR iPTMnet; Q62120; -.
DR PhosphoSitePlus; Q62120; -.
DR jPOST; Q62120; -.
DR MaxQB; Q62120; -.
DR PaxDb; Q62120; -.
DR PRIDE; Q62120; -.
DR ProteomicsDB; 269116; -.
DR ProteomicsDB; 328792; -.
DR Antibodypedia; 24086; 1246 antibodies from 48 providers.
DR DNASU; 16452; -.
DR Ensembl; ENSMUST00000025705; ENSMUSP00000025705; ENSMUSG00000024789.
DR Ensembl; ENSMUST00000065796; ENSMUSP00000064394; ENSMUSG00000024789.
DR Ensembl; ENSMUST00000238009; ENSMUSP00000158242; ENSMUSG00000024789.
DR GeneID; 16452; -.
DR KEGG; mmu:16452; -.
DR UCSC; uc008hdb.2; mouse.
DR CTD; 3717; -.
DR MGI; MGI:96629; Jak2.
DR VEuPathDB; HostDB:ENSMUSG00000024789; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000155640; -.
DR HOGENOM; CLU_008155_1_0_1; -.
DR InParanoid; Q62120; -.
DR OMA; ICAVACK; -.
DR OrthoDB; 58906at2759; -.
DR PhylomeDB; Q62120; -.
DR TreeFam; TF327041; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
DR Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
DR Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-877300; Interferon gamma signaling.
DR Reactome; R-MMU-877312; Regulation of IFNG signaling.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR Reactome; R-MMU-9020591; Interleukin-12 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR Reactome; R-MMU-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR Reactome; R-MMU-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 16452; 29 hits in 88 CRISPR screens.
DR ChiTaRS; Jak2; mouse.
DR EvolutionaryTrace; Q62120; -.
DR PRO; PR:Q62120; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q62120; protein.
DR Bgee; ENSMUSG00000024789; Expressed in animal zygote and 278 other tissues.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; ISO:MGI.
DR GO; GO:0042022; C:interleukin-12 receptor complex; IC:ComplexPortal.
DR GO; GO:0072536; C:interleukin-23 receptor complex; IC:ComplexPortal.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005126; F:cytokine receptor binding; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; ISS:BHF-UCL.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0035401; F:histone kinase activity (H3-Y41 specific); ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043560; F:insulin receptor substrate binding; ISO:MGI.
DR GO; GO:0005143; F:interleukin-12 receptor binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISO:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0042976; P:activation of Janus kinase activity; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0031103; P:axon regeneration; ISS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:MGI.
DR GO; GO:0036016; P:cellular response to interleukin-3; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0038065; P:collagen-activated signaling pathway; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IDA:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0038157; P:granulocyte-macrophage colony-stimulating factor signaling pathway; ISO:MGI.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IDA:BHF-UCL.
DR GO; GO:0035409; P:histone H3-Y41 phosphorylation; ISO:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:BHF-UCL.
DR GO; GO:0061180; P:mammary gland epithelium development; IMP:MGI.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:0031959; P:mineralocorticoid receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR GO; GO:0045822; P:negative regulation of heart contraction; ISS:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0050867; P:positive regulation of cell activation; ISS:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; ISO:MGI.
DR GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; ISO:MGI.
DR GO; GO:0060399; P:positive regulation of growth hormone receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IC:ComplexPortal.
DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:BHF-UCL.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:MGI.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IGI:ARUK-UCL.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:ComplexPortal.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; IMP:CACAO.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0034050; P:programmed cell death induced by symbiont; IDA:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:BHF-UCL.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; ISO:MGI.
DR GO; GO:0097012; P:response to granulocyte macrophage colony-stimulating factor; NAS:BHF-UCL.
DR GO; GO:0033194; P:response to hydroperoxide; ISS:BHF-UCL.
DR GO; GO:0070671; P:response to interleukin-12; ISS:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
DR GO; GO:0006979; P:response to oxidative stress; ISS:BHF-UCL.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:MGI.
DR CDD; cd13333; FERM_C_JAK2; 1.
DR CDD; cd05078; PTK_Jak2_rpt1; 1.
DR CDD; cd14205; PTKc_Jak2_rpt2; 1.
DR CDD; cd10379; SH2_Jak2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50091; -.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041155; FERM_F1.
DR InterPro; IPR041046; FERM_F2.
DR InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
DR InterPro; IPR037838; JAK2_FERM_C-lobe.
DR InterPro; IPR035860; JAK2_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035588; PTK_Jak2_rpt1.
DR InterPro; IPR035589; PTKc_Jak2_rpt2.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR InterPro; IPR020693; Tyr_kinase_non-rcpt_Jak2.
DR Pfam; PF18379; FERM_F1; 1.
DR Pfam; PF18377; FERM_F2; 1.
DR Pfam; PF17887; Jak1_Phl; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR PRINTS; PR01823; JANUSKINASE.
DR PRINTS; PR01825; JANUSKINASE2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; ATP-binding; Chromatin regulator;
KW Cytoplasm; Immunity; Innate immunity; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; Transferase;
KW Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..1132
FT /note="Tyrosine-protein kinase JAK2"
FT /id="PRO_0000088113"
FT DOMAIN 37..380
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 401..482
FT /note="SH2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 545..809
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 849..1124
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..239
FT /note="Interaction with cytokine/interferon/growth hormone
FT receptors"
FT ACT_SITE 976
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 855..863
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 882
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 119
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17024180"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21726629"
FT MOD_RES 373
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21726629"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 570
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60674"
FT MOD_RES 813
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:16824542,
FT ECO:0000269|PubMed:17565041"
FT MOD_RES 868
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20304997"
FT MOD_RES 966
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20304997"
FT MOD_RES 972
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20304997"
FT MOD_RES 1007
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9473212"
FT MOD_RES 1008
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20304997"
FT MUTAGEN 119
FT /note="Y->E: Phosphorylation mimic mutant, leads to
FT dissociation of JAK2 from the erythropoietin receptor
FT complex."
FT /evidence="ECO:0000269|PubMed:17024180"
FT MUTAGEN 119
FT /note="Y->F: More stably associated with the erythropoietin
FT receptor complex."
FT /evidence="ECO:0000269|PubMed:17024180"
FT MUTAGEN 372
FT /note="Y->F: About 60% loss of STAT1 phosphorylation by
FT JAK2."
FT /evidence="ECO:0000269|PubMed:21726629"
FT MUTAGEN 373
FT /note="Y->F: Decreased the ability of JAK2 to
FT autophosphorylate."
FT /evidence="ECO:0000269|PubMed:21726629"
FT MUTAGEN 868
FT /note="Y->F: Reduced activity in response to growth
FT hormone."
FT /evidence="ECO:0000269|PubMed:20304997"
FT MUTAGEN 966
FT /note="Y->F: Reduced activity in response to growth
FT hormone."
FT /evidence="ECO:0000269|PubMed:20304997"
FT MUTAGEN 972
FT /note="Y->F: Reduced activity in response to growth
FT hormone."
FT /evidence="ECO:0000269|PubMed:20304997"
FT MUTAGEN 1008
FT /note="Y->F: Affects the phosphorylation pattern."
FT /evidence="ECO:0000269|PubMed:20304997"
FT CONFLICT 155
FT /note="A -> V (in Ref. 1; AAB41327)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="K -> N (in Ref. 1; AAB41327)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="D -> N (in Ref. 3; AAH54807/AAH59834)"
FT CONFLICT 1016
FT /note="S -> R (in Ref. 5; AAA40014)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="E -> Q (in Ref. 1; AAB41327)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042..1043
FT /note="VV -> IP (in Ref. 5; AAA40014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 130595 MW; 7BA35989B880D0A6 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 LIREEDRRTG 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 LRVDQIRDSI AA
