ID E9QJS1_MOUSE Unreviewed; 1207 AA. AC E9QJS1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636}; DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636}; GN Name=Tyk2 {ECO:0000313|Ensembl:ENSMUSP00000001036.11, GN ECO:0000313|MGI:MGI:1929470}; 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 {ECO:0000313|Ensembl:ENSMUSP00000001036.11, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0007829|PubMed:17947660} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17947660; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000001036.11, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000001036.11, RC ECO:0000313|Proteomes:UP000000589}; 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] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {ECO:0000313|Ensembl:ENSMUSP00000001036.11} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000001036.11}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|ARBA:ARBA00001149, CC ECO:0000256|PIRNR:PIRNR000636}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; NP_001192241.1; NM_001205312.1. DR ProteomicsDB; 332550; -. DR Antibodypedia; 716; 787 antibodies from 41 providers. DR DNASU; 54721; -. DR Ensembl; ENSMUST00000001036.11; ENSMUSP00000001036.11; ENSMUSG00000032175.12. DR Ensembl; ENSMUST00000216874.2; ENSMUSP00000150354.2; ENSMUSG00000032175.12. DR GeneID; 54721; -. DR UCSC; uc012gpb.1; mouse. DR AGR; MGI:1929470; -. DR CTD; 7297; -. DR MGI; MGI:1929470; Tyk2. DR VEuPathDB; HostDB:ENSMUSG00000032175; -. DR GeneTree; ENSGT00940000159869; -. DR HOGENOM; CLU_008155_1_0_1; -. DR OMA; QAKHEFV; -. DR OrthoDB; 1614410at2759; -. DR TreeFam; TF327041; -. DR BioGRID-ORCS; 54721; 7 hits in 79 CRISPR screens. DR ChiTaRS; Tyk2; mouse. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; ENSMUSG00000032175; Expressed in granulocyte and 234 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005131; F:growth hormone receptor binding; IEA:Ensembl. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl. DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl. DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IEA:Ensembl. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl. DR GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IEA:Ensembl. DR CDD; cd05080; PTKc_Tyk2_rpt2; 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; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. 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; IPR016045; Tyr_kinase_non-rcpt_TYK2_N. DR PANTHER; PTHR45807:SF6; NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2; 1. DR PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 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; PR00109; TYRKINASE. DR PRINTS; PR01827; YKINASETYK2. DR SMART; SM00295; B41; 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. DR Genevisible; E9QJS1; MM. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636- KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636, KW ECO:0000256|PIRSR:PIRSR000636-2}; KW Proteomics identification {ECO:0007829|EPD:E9QJS1, KW ECO:0007829|MaxQB:E9QJS1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW SH2 domain {ECO:0000256|ARBA:ARBA00022999}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000636}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137, KW ECO:0000256|PIRNR:PIRNR000636}. FT DOMAIN 33..453 FT /note="FERM" FT /evidence="ECO:0000259|PROSITE:PS50057" FT DOMAIN 612..889 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 917..1189 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 317..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 350..371 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1043 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000636-1" FT BINDING 923..931 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2" FT BINDING 950 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000636-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 1207 AA; 135901 MW; 7207FF710AC80CE1 CRC64; MVGTMPLCGR RAILEDSKAD GTEAQPLVPT GCLMVLLHWP GPEGGEPWVT FSQTSLTAEE VCIHIAHKVG ITPPCLNLFA LYNAQAKVWL PPNHILDTSQ DMNLYFRMRF YFRNWHGMNP QEPAVYRCGF PGAETSSDRA EQGVQLLDSA SFEYLFEQGW YVGNRAKSSH TSFSIHRSTP QGKHEFMNDV VSLRDLSSEE EIHHFKNESL GMAFLHLCHL ALSRGVPLEE MAREISFKNC IPHSFRQHIR QHNVLTRLRL HRVFRRFLRA FRPGHLSQQV VMVKYLATLE RLAPRFGSER IPVCHLEVLA QPERDPCYIQ NSGQTAGDPG PELPSGPPTH EVLVTGTGGI QWHPLQTQES ERGNSRGNPH GSRSGKKPKA PKAGEHLTES PQEPPWTYFC DFQDISHVVL KERRVHIHLQ DNKCLLLCLC SQAEALSFVA LVDGYFRLTA DSSHYLCHEV APPRLVTSIQ NGIHGPLMDP FVQAKLWPED GLYLIQWSTS HLHRLILTVA HRNPAFSNGP RGLRLRKFPI TQQPGAFVLD GWGRSFASLG DLRLALQGCS LRAGDDCFPL HHCCLPRPRE ISNLVIMRGS RAHTRPLNLS QLSFHRVHQD EITQLSHLGQ GTRTNVYEGL LRVGGPDEGK VDNGCPPEPG GTSGQQLRVV LKVLDPSHHD IALAFYETAS LMSQVSHMHL AFLHGVCVRG SENIIVTEFV EHGPLDVWLR RQRGQVPMTW KMVVAQQLAS ALSYLEDKNL VHGNVCGRNI LLARLGLEEG TNPFIKLSDP GVGQGALSRE ERVERIPWTA PECLSGGTSS LGTATDMWGF GATLLEICFD GEAPLQGRGP SEKERFYTKK HQLPEPSSPE LATLTRQCLT YEPAQRPSFR TILRDLTRLQ PQNLVGTSAV NSDSPASDPT VFHKRYLKKI RDLGEGHFGK VSLYCYDPTN DGTGEMVAVK ALKEGCGPQL RSGWQREIEI LRTLYHEHIV KYKGCCEDQG EKSVQLVMEY VPLGSLRDYL PRHCVGLAQL LLFAQQICEG MAYLHAQHYI HRDLAARNVL LDNDRLVKIG DFGLAKAVPE GHEYYRVRED GDSPVFWYAP ECLKECKFYY ASDVWSFGVT LYELLTYCDS NQSPHMKFTE LIGHTQGQMT VLRLTELLER GERLPRPDRC PCEIYHLMKN CWETEASFRP TFQNLVPILQ TAQEKYQGQV PSVFSVC //