ID JAK3_MOUSE Reviewed; 1100 AA.
AC Q62137; A2RRI3; Q0D2M8; Q61746; Q61747; Q8BTY6; Q8BYU2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 08-NOV-2023, entry version 214.
DE RecName: Full=Tyrosine-protein kinase JAK3 {ECO:0000305};
DE EC=2.7.10.2;
DE AltName: Full=Janus kinase 3;
DE Short=JAK-3;
GN Name=Jak3 {ECO:0000312|MGI:MGI:99928};
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] (ISOFORM 2).
RX PubMed=7518579;
RA Rane S.G., Reddy E.P.;
RT "JAK3: a novel JAK kinase associated with terminal differentiation of
RT hematopoietic cells.";
RL Oncogene 9:2415-2423(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF LEU-853.
RC TISSUE=Thymus;
RX PubMed=8605329;
RA Gurniak C.B., Berg L.J.;
RT "Murine JAK3 is preferentially expressed in hematopoietic tissues and
RT lymphocyte precursor cells.";
RL Blood 87:3151-3160(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=8022486; DOI=10.1038/370153a0;
RA Witthuhn B.A., Silvennoinen O., Miura O., Lai K.S., Cwik C., Liu E.T.,
RA Ihle J.N.;
RT "Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and
RT 4 in lymphoid and myeloid cells.";
RL Nature 370:153-157(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=7481767; DOI=10.1126/science.270.5237.794;
RA Thomis D.C., Gurniak C.B., Tivol E., Sharpe A.H., Berg L.J.;
RT "Defects in B lymphocyte maturation and T lymphocyte activation in mice
RT lacking Jak3.";
RL Science 270:794-797(1995).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=7481769; DOI=10.1126/science.270.5237.800;
RA Nosaka T., van Deursen J.M., Tripp R.A., Thierfelder W.E., Witthuhn B.A.,
RA McMickle A.P., Doherty P.C., Grosveld G.C., Ihle J.N.;
RT "Defective lymphoid development in mice lacking Jak3.";
RL Science 270:800-802(1995).
RN [8]
RP FUNCTION.
RX PubMed=9016869; DOI=10.1084/jem.185.2.197;
RA Thomis D.C., Berg L.J.;
RT "Peripheral expression of Jak3 is required to maintain T lymphocyte
RT function.";
RL J. Exp. Med. 185:197-206(1997).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=9620658; DOI=10.1002/jlb.63.6.669;
RA Baird A.M., Thomis D.C., Berg L.J.;
RT "T cell development and activation in Jak3-deficient mice.";
RL J. Leukoc. Biol. 63:669-677(1998).
RN [10]
RP INTERACTION WITH MYO18A.
RX PubMed=10733938; DOI=10.1006/bbrc.2000.2413;
RA Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.;
RT "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by IL-2
RT deprival.";
RL Biochem. Biophys. Res. Commun. 270:267-271(2000).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Non-receptor tyrosine kinase involved in various processes
CC such as cell growth, development, or differentiation. Mediates
CC essential signaling events in both innate and adaptive immunity and
CC plays a crucial role in hematopoiesis during T-cells development. In
CC the cytoplasm, plays a pivotal role in signal transduction via its
CC association with type I receptors sharing the common subunit gamma such
CC as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. 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, upon IL2R activation by IL2, JAK1 and JAK3
CC molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits
CC inducing the tyrosine phosphorylation of both receptor subunits on
CC their cytoplasmic domain. Then, STAT5A and STAT5B are recruited,
CC phosphorylated and activated by JAK1 and JAK3. Once activated,
CC dimerized STAT5 translocates to the nucleus and promotes the
CC transcription of specific target genes in a cytokine-specific fashion.
CC {ECO:0000269|PubMed:9016869}.
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 -!- SUBUNIT: Interacts with STAM2 and MYO18A. Interacts with SHB (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62137-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62137-2; Sequence=VSP_027575, VSP_027576;
CC -!- TISSUE SPECIFICITY: In contrast with the ubiquitous expression of the
CC other JAKs, JAK3 is predominantly expressed in hematopoietic tissues.
CC {ECO:0000269|PubMed:8605329}.
CC -!- DOMAIN: Possesses two phosphotransferase domains. The second one
CC contains the catalytic domain, while the presence of a pseudokinase
CC domain is required for suppression of basal activity of JAK3.
CC -!- PTM: Autophosphorylated, leading to regulate its activity. IL2 promotes
CC phosphorylation on tyrosine residues, including autophosphorylation on
CC Tyr-781 (By similarity). Dephosphorylation of Tyr-976 and Tyr-977 by
CC PTPN2 negatively regulates cytokine-mediated signaling (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show a severe block in B-cell development at
CC the pre-B stage in the bone marrow. Additionally, they possesses small
CC thymuses revealing a defect in T-cell development. The distribution of
CC developmental subsets is relatively normal, suggesting a block in the
CC expansion of early T-cell progenitors. Peripheral T-cells are present
CC at normal or increased numbers but are functionally incompetent.
CC {ECO:0000269|PubMed:7481767, ECO:0000269|PubMed:7481769,
CC ECO:0000269|PubMed:9620658}.
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=AAA21415.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA21565.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L33768; AAA21415.1; ALT_FRAME; mRNA.
DR EMBL; L40172; AAC42085.1; -; mRNA.
DR EMBL; L32955; AAA21565.1; ALT_FRAME; mRNA.
DR EMBL; AK038268; BAC29956.1; -; mRNA.
DR EMBL; AK142178; BAE24964.1; -; mRNA.
DR EMBL; AK156646; BAE33790.1; -; mRNA.
DR EMBL; AK164520; BAE37819.1; -; mRNA.
DR EMBL; AK088365; BAC40305.1; -; mRNA.
DR EMBL; BC105577; AAI05578.1; -; mRNA.
DR EMBL; BC131646; AAI31647.1; -; mRNA.
DR EMBL; BC131647; AAI31648.1; -; mRNA.
DR CCDS; CCDS22403.1; -. [Q62137-1]
DR PIR; I58401; I58401.
DR PIR; S48053; S48053.
DR RefSeq; NP_001177759.1; NM_001190830.1.
DR RefSeq; NP_034719.2; NM_010589.6.
DR AlphaFoldDB; Q62137; -.
DR SMR; Q62137; -.
DR BioGRID; 200858; 5.
DR IntAct; Q62137; 2.
DR MINT; Q62137; -.
DR STRING; 10090.ENSMUSP00000060073; -.
DR BindingDB; Q62137; -.
DR ChEMBL; CHEMBL5250; -.
DR DrugCentral; Q62137; -.
DR iPTMnet; Q62137; -.
DR PhosphoSitePlus; Q62137; -.
DR EPD; Q62137; -.
DR jPOST; Q62137; -.
DR MaxQB; Q62137; -.
DR PaxDb; 10090-ENSMUSP00000060073; -.
DR ProteomicsDB; 269117; -. [Q62137-1]
DR ProteomicsDB; 269118; -. [Q62137-2]
DR DNASU; 16453; -.
DR GeneID; 16453; -.
DR KEGG; mmu:16453; -.
DR UCSC; uc009mel.2; mouse. [Q62137-1]
DR AGR; MGI:99928; -.
DR CTD; 3718; -.
DR MGI; MGI:99928; Jak3.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; Q62137; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; Q62137; -.
DR TreeFam; TF327041; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR BioGRID-ORCS; 16453; 5 hits in 84 CRISPR screens.
DR ChiTaRS; Jak3; mouse.
DR PRO; PR:Q62137; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62137; Protein.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0030183; P:B cell differentiation; IMP:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; IDA:MGI.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:MGI.
DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035771; P:interleukin-4-mediated signaling pathway; ISO:MGI.
DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0048535; P:lymph node development; TAS:MGI.
DR GO; GO:0002731; P:negative regulation of dendritic cell cytokine production; IMP:BHF-UCL.
DR GO; GO:0045221; P:negative regulation of FasL production; IMP:BHF-UCL.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:BHF-UCL.
DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:BHF-UCL.
DR GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IMP:BHF-UCL.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:BHF-UCL.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0070672; P:response to interleukin-15; TAS:BHF-UCL.
DR GO; GO:0070669; P:response to interleukin-2; TAS:BHF-UCL.
DR GO; GO:0070670; P:response to interleukin-4; ISS:BHF-UCL.
DR GO; GO:0071104; P:response to interleukin-9; TAS:BHF-UCL.
DR GO; GO:0043029; P:T cell homeostasis; IMP:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR CDD; cd13334; FERM_C_JAK3; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR019749; Band_41_domain.
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; 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; 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; IPR020775; Tyr_kinase_non-rcpt_Jak3.
DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR PANTHER; PTHR45807:SF3; TYROSINE-PROTEIN KINASE JAK3; 1.
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 PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR PRINTS; PR01823; JANUSKINASE.
DR PRINTS; PR01826; JANUSKINASE3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF55550; SH2 domain; 1.
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.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; ATP-binding; Cytoplasm; Immunity;
KW Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..1100
FT /note="Tyrosine-protein kinase JAK3"
FT /id="PRO_0000088116"
FT DOMAIN 24..353
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 372..472
FT /note="SH2; atypical"
FT DOMAIN 517..777
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 818..1100
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..223
FT /note="Interaction with cytokine/interferon/growth hormone
FT receptors"
FT /evidence="ECO:0000250"
FT ACT_SITE 945
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 824..832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 851
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P52333"
FT MOD_RES 900
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P52333"
FT MOD_RES 935
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P52333"
FT MOD_RES 976
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P52333"
FT MOD_RES 977
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P52333"
FT VAR_SEQ 284
FT /note="E -> EVLGLGLRSGVRGEAWRLVKKPVRTIRKVASPGRADCTTGQGGGVNL
FT KVGPGMELPQGLTWGVTRRVRLDRGRGRTEGDSMDWISGHDPTRPVFSPLTSSPPPHKW
FT RWEGGRRGGCAGSRSVIPWLLSLFLFFFFNGFARQGFSYSSGCPGTHFVRPGWPRTQKS
FT ACLCLSSAVIKGRVPLRRYCLSFLPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7518579"
FT /id="VSP_027575"
FT VAR_SEQ 379
FT /note="L -> LGASWGQQWGWGWAARTVLGWTWLLSWPRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7518579"
FT /id="VSP_027576"
FT MUTAGEN 853
FT /note="L->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8605329"
FT CONFLICT 62
FT /note="G -> A (in Ref. 1; AAA21415 and 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="S -> P (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..283
FT /note="GDQ -> ND (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="K -> N (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="P -> A (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..372
FT /note="EL -> DV (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="G -> A (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="Missing (in Ref. 4; BAC40305)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="N -> Y (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="T -> N (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 518..519
FT /note="EW -> G (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="R -> S (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="C -> G (in Ref. 4; BAC40305/BAC29956/BAE24964/
FT BAE33790/BAE37819)"
FT /evidence="ECO:0000305"
FT CONFLICT 716..717
FT /note="SG -> QR (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="G -> VA (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="K -> N (in Ref. 5; AAI31647)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="Missing (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 857
FT /note="G -> V (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="F -> L (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 915..916
FT /note="AR -> G (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="R -> A (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="R -> S (in Ref. 4; BAC40305/BAC29956/BAE24964/
FT BAE33790/BAE37819)"
FT /evidence="ECO:0000305"
FT CONFLICT 1074
FT /note="W -> V (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="S -> E (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="G -> A (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="A -> G (in Ref. 1; AAA21415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="A -> P (in Ref. 2; AAA21565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 122641 MW; 979A120861ED37C1 CRC64;
MAPPSEETPL IPQRSCSLSS SEAGALHVLL PPRGPGPPQR LSFSFGDYLA EDLCVRAAKA
CGILPVYHSL FALATEDFSC WFPPSHIFCI EDVDTQVLVY RLRFYFPDWF GLETCHRFGL
RKDLTSAILD LHVLEHLFAQ HRSDLVSGRL PVGLSMKEQG EFLSLAVLDL AQMAREQAQR
PGELLKTVSY KACLPPSLRD VIQGQNFVTR RRIRRTVVLA LRRVVACQAD RYALMAKYIL
DLERLHPAAT TETFRVGLPG AQEEPGLLRV AGDNGISWSS GDQELFQTFC DFPEIVDVSI
KQAPRVGPAG EHRLVTVTRM DGHILEAEFP GLPEALSFVA LVDGYFRLIC DSRHYFCKEV
APPRLLEEEA ELCHGPITLD FAIHKLKAAG SLPGTYILRR SPQDYDSFLL TACVQTPLGP
DYKGCLIRQD PSGAFSLVGL SQPHRSLREL LAACWNSGLR VDGAALNLTS CCAPRPKEKS
NLIVVRRGCT PAPAPGCSPS CCALTQLSFH TIPTDSLEWH ENLGHGSFTK IFRGRRREVV
DGETHDSEVL LKVMDSRHRN CMESFLEAAS LMSQVSYPHL VLLHGVCMAG DSIMVQEFVY
LGAIDMYLRK RGHLVSASWK LQVTKQLAYA LNYLEDKGLP HGNVSARKVL LAREGGDGNP
PFIKLSDPGV SPTVLSLEML TDRIPWVAPE CLQEAQTLCL EADKWGFGAT TWEVFSGGPA
HITSLEPAKK LKFYEDQGQL PALKWTELAG LITQCMAYDP GRRPSFRAIL RDLNGLITSD
YELLSDPTPG IPSPRDELCG GAQLYACQDP AIFEERHLKY ISLLGKGNFG SVELCRYDPL
GDNTGPLVAV KQLQHSGPDQ QRDFQREIQI LKALHSDFIV KYRGVSYGPG RQSLRLVMEY
LPSGCLRDFL QRHRARLHTD RLLLFAWQIC KGMEYLGARR CVHRDLAARN ILVESEAHVK
IADFGLAKLL PLGKDYYVVR EPGQSPIFWY APESLSDNIF SRQSDVWSFG VVLYELFTYC
DKSCSPSAEF LRMMGPEREG PPLCRLLELL AEGRRLPPPP TCPTEVQELM QLCWAPSPHD
RPAFGTLSPQ LDALWRGRPG
//
