ID   B1ASP2_MOUSE            Unreviewed;      1153 AA.
AC   B1ASP2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
GN   Name=Jak1 {ECO:0000313|Ensembl:ENSMUSP00000099842.4,
GN   ECO:0000313|MGI:MGI:96628};
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:ENSMUSP00000099842.4, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000099842.4, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099842.4,
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   [2] {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   [3] {ECO:0000313|Ensembl:ENSMUSP00000099842.4}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099842.4};
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, ECO:0000256|RuleBase:RU362096};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR   RefSeq; NP_666257.2; NM_146145.2.
DR   RefSeq; XP_006502875.1; XM_006502812.3.
DR   RefSeq; XP_011238753.1; XM_011240451.2.
DR   AlphaFoldDB; B1ASP2; -.
DR   SMR; B1ASP2; -.
DR   SwissPalm; B1ASP2; -.
DR   jPOST; B1ASP2; -.
DR   MaxQB; B1ASP2; -.
DR   PeptideAtlas; B1ASP2; -.
DR   ProteomicsDB; 332682; -.
DR   Antibodypedia; 3400; 787 antibodies from 43 providers.
DR   DNASU; 16451; -.
DR   Ensembl; ENSMUST00000102781.10; ENSMUSP00000099842.4; ENSMUSG00000028530.15.
DR   GeneID; 16451; -.
DR   UCSC; uc008tvk.1; mouse.
DR   AGR; MGI:96628; -.
DR   CTD; 3716; -.
DR   MGI; MGI:96628; Jak1.
DR   VEuPathDB; HostDB:ENSMUSG00000028530; -.
DR   GeneTree; ENSGT00940000157092; -.
DR   HOGENOM; CLU_008155_1_0_1; -.
DR   OMA; KDIMQGE; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; B1ASP2; -.
DR   TreeFam; TF327041; -.
DR   BioGRID-ORCS; 16451; 40 hits in 91 CRISPR screens.
DR   ChiTaRS; Jak1; mouse.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028530; Expressed in femorotibial joint and 277 other cell types or tissues.
DR   ExpressionAtlas; B1ASP2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031730; F:CCR5 chemokine receptor binding; IEA:Ensembl.
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:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0038154; P:interleukin-11-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0038113; P:interleukin-9-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:0034112; P:positive regulation of homotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0150105; P:protein localization to cell-cell junction; IEA:Ensembl.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; 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; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13332; FERM_C_JAK1; 1.
DR   CDD; cd05077; PTK_Jak1_rpt1; 1.
DR   CDD; cd05079; PTKc_Jak1_rpt2; 1.
DR   CDD; cd10378; SH2_Jak1; 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; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
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; 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; IPR020776; Tyr_kinase_non-rcpt_Jak1.
DR   PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR   PANTHER; PTHR45807:SF5; TYROSINE-PROTEIN KINASE JAK1; 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; PR01824; JANUSKINASE1.
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; SSF47031; Second domain of FERM; 1.
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   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW   2}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW   ECO:0000256|PIRSR:PIRSR000636-2};
KW   Proteomics identification {ECO:0007829|EPD:B1ASP2,
KW   ECO:0007829|MaxQB:B1ASP2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
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          34..420
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          439..528
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          582..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          874..1152
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   COILED          333..362
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        1002
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         880..888
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         907
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1153 AA;  133353 MW;  6E45E960303D66DC CRC64;
     MQYLNIKEDC NAMAFCAKMR SFKKTEVKQV VPEPGVEVTF YLLDREPLRL GSGEYTAEEL
     CIRAAQECSI SPLCHNLFAL YDESTKLWYA PNRIITVDDK TSLRLHYRMR FYFTNWHGTN
     DNEQSVWRHS PKKQKNGYEK KRVPEATPLL DASSLEYLFA QGQYDLIKCL APIRDPKTEQ
     DGHDIENECL GMAVLAISHY AMMKKMQLPE LPKDISYKRY IPETLNKSIR QRNLLTRMRI
     NNVFKDFLKE FNNKTICDSS VSTHDLKVKY LATLETLTKH YGAEIFETSM LLISSENELS
     RCHSNDSGNV LYEVMVTGNL GIQWRQKPNV VPVEKEKNKL KRKKLEYNKH KKDDERNKLR
     EEWNNFSYFP EITHIVIKES VVSINKQDNK NMELKLSSRE EALSFVSLVD GYFRLTADAH
     HYLCTDVAPP LIVHNIQNGC HGPICTEYAI NKLRQEGSEE GMYVLRWSCT DFDNILMTVT
     CFEKSEVLGG QKQFKNFQIE VQKGRYSLHG SMDHFPSLRD LMNHLKKQIL RTDNISFVLK
     RCCQPKPREI SNLLVATKKA QEWQPVYSMS QLSFDRILKK DIIQGEHLGR GTRTHIYSGT
     LLDYKDEEGI AEEKKIKVIL KVLDPSHRDI SLAFFEAASM MRQVSHKHIV YLYGVCVRDV
     ENIMVEEFVE GGPLDLFMHR KSDALTTPWK FKVAKQLASA LSYLEDKDLV HGNVCTKNLL
     LAREGIDSDI GPFIKLSDPG IPVSVLTRQE CIERIPWIAP ECVEDSKNLS VAADKWSFGT
     TLWEICYNGE IPLKDKTLIE KERFYESRCR PVTPSCKELA DLMTRCMNYD PNQRPFFRAI
     MRDINKLEEQ NPDIVSEKQP TTEVDPTHFE KRFLKRIRDL GEGHFGKVEL CRYDPEGDNT
     GEQVAVKSLK PESGGNHIAD LKKEIEILRN LYHENIVKYK GICMEDGGNG IKLIMEFLPS
     GSLKEYLPKN KNKINLKQQL KYAIQICKGM DYLGSRQYVH RDLAARNVLV ESEHQVKIGD
     FGLTKAIETD KEYYTVKDDR DSPVFWYAPE CLIQCKFYIA SDVWSFGVTL HELLTYCDSD
     FSPMALFLKM IGPTHGQMTV TRLVNTLKEG KRLPCPPNCP DEVYQLMRKC WEFQPSNRTT
     FQNLIEGFEA LLK
//