ID Q59FK4_HUMAN Unreviewed; 1167 AA. AC Q59FK4; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096}; DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92693.1}; RN [1] {ECO:0000313|EMBL:BAD92693.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAD92693.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. 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|RuleBase:RU362096}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000256|RuleBase:RU362096}. 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 EMBL; AB209456; BAD92693.1; -; mRNA. DR RefSeq; NP_005148.2; NM_005157.5. DR RefSeq; NP_009297.2; NM_007313.2. DR AlphaFoldDB; Q59FK4; -. DR SMR; Q59FK4; -. DR PeptideAtlas; Q59FK4; -. DR DNASU; 25; -. DR GeneID; 25; -. DR KEGG; hsa:25; -. DR CTD; 25; -. DR PharmGKB; PA24413; -. DR OrthoDB; 1614410at2759; -. DR BioGRID-ORCS; 25; 30 hits in 1205 CRISPR screens. DR GenomeRNAi; 25; -. DR GO; GO:0005829; C:cytosol; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0007154; P:cell communication; IEA:UniProt. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt. DR GO; GO:0023052; P:signaling; IEA:UniProt. DR CDD; cd05052; PTKc_Abl; 1. DR CDD; cd09935; SH2_ABL; 1. DR CDD; cd11850; SH3_Abl; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR035837; ABL_SH2. DR InterPro; IPR015015; F-actin-binding. 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; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF438; TYROSINE-PROTEIN KINASE ABL1; 1. DR Pfam; PF08919; F_actin_bind; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q59FK4; HS. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141, KW ECO:0000256|RuleBase:RU362096}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE- KW ProRule:PRU00191}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137, KW ECO:0000256|RuleBase:RU362096}. FT DOMAIN 98..158 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 164..254 FT /note="SH2" FT /evidence="ECO:0000259|PROSITE:PS50001" FT DOMAIN 279..530 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 555..1033 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..586 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 616..638 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..675 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..740 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..790 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 795..809 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 907..931 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 308 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD92693.1" SQ SEQUENCE 1167 AA; 127257 MW; F05C6B7355BE8945 CRC64; PFWKILNPLL ERGTYYYFMG QQPGKVLGDQ RRPSLPALHF IKGAGKKESS RHGGPHCNVF VEHEALQRPV ASDFEPQGLS EAARWNSKEN LLAGPSENDP NLFVALYDFV ASGDNTLSIT KGEKLRVLGY NHNGEWCEAQ TKNGQGWVPS NYITPVNSLE KHSWYHGPVS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH YRINTASDGK LYVSSESRFN TLAELVHHHS TVADGLITTL HYPAPKRNKP TVYGVSPNYD KWEMERTDIT MKHKLGGGQY GEVYEGVWKK YSLTVAVKTL KEDTMEVEEF LKEAAVMKEI KHPNLVQLLG VCTREPPFYI ITEFMTYGNL LDYLRECNRQ EVNAVVLLYM ATQISSAMEY LEKKNFIHRD LAARNCLVGE NHLVKVADFG LSRLMTGDTY TAHAGAKFPI KWTAPESLAY NKFSIKSDVW AFGVLLWEIA TYGMSPYPGI DLSQVYELLE KDYRMERPEG CPEKVYELMR ACWQWNPSDR PSFAEIHQAF ETMFQESSIS DEVEKELGKQ GVRGAVSTLL QAPELPTKTR TSRRAAEHRD TTDVPEMPHS KGQGESDPLD HEPAVSPLLP RKERGPPEGG LNEDERLLPK DKKTNLFSAL IKKKKKTAPT PPKRSSSFRE MDGQPERRGA GEEEGRDISN GALAFTPLDT ADPAKSPKPS NGAGVPNGAL RESGGSGFRS PHLWKKSSTL TSSRLATGEE EGGGSSSKRF LRSCSASCVP HGAKDTEWRS VTLPRDLQST GRQFDSSTFG GHKSEKPALP RKRAGENRSD QVTRGTVTPP PRLVKKNEEA ADEVFKDIME SSPGSSPPNL TPKPLRRQVT VAPASGLPHK EEAGKGSALG TPAAAEPVTP TSKAGSGAPG GTSKGPAEES RVRRHKHSSE SPGRDKGKLS RLKPAPPPPP AASAGKAGGK PSQSPSQEAA GEAVLGAKTK ATSLVDAVNS DAAKPSQPGE GLKKPVLPAT PKPQSAKPSG TPISPAPVPS TLPSASSALA GDQPSSTAFI PLISTRVSLR KTRQPPERIA SGAITKGVVL DSTEALCLAI SRNSEQMASH SAVLEAGKNL YTFCVSYVDS IQQMRNKFAF REAINKLENN LRELQICPAT AGSGPAATQD FSKLLSSVKE ISDIVQR //