YRK_CHICK
ID YRK_CHICK Reviewed; 536 AA.
AC Q02977;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Proto-oncogene tyrosine-protein kinase Yrk;
DE EC=2.7.10.2;
DE AltName: Full=Yes-related kinase;
DE AltName: Full=p60-Yrk;
GN Name=YRK;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Brain, and Kidney;
RX PubMed=8455940;
RA Sudol M., Greulich H., Newman L., Sarkar A., Sukegawa J., Yamamoto T.;
RT "A novel Yes-related kinase, Yrk, is expressed at elevated levels in neural
RT and hematopoietic tissues.";
RL Oncogene 8:823-831(1993).
CC -!- FUNCTION: May participate in signaling pathways.
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 -!- TISSUE SPECIFICITY: There are elevated levels of this protein in neural
CC and hematopoietic tissues.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X67786; CAA47996.1; -; mRNA.
DR PIR; S33569; S33569.
DR RefSeq; NP_001103257.1; NM_001109787.1.
DR AlphaFoldDB; Q02977; -.
DR SMR; Q02977; -.
DR STRING; 9031.ENSGALP00000007628; -.
DR Ensembl; ENSGALT00000063550; ENSGALP00000043829; ENSGALG00000032199.
DR GeneID; 777583; -.
DR KEGG; gga:777583; -.
DR CTD; 2268; -.
DR VEuPathDB; HostDB:geneid_777583; -.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000157554; -.
DR InParanoid; Q02977; -.
DR OMA; LPCKERG; -.
DR OrthoDB; 539311at2759; -.
DR PhylomeDB; Q02977; -.
DR BRENDA; 2.7.10.2; 1306.
DR PRO; PR:Q02977; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000032199; Expressed in lung and 11 other tissues.
DR ExpressionAtlas; Q02977; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; IEA:Ensembl.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0045088; P:regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0050764; P:regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd12006; SH3_Fyn_Yrk; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035750; Fyn/Yrk_SH3.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Palmitate;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..536
FT /note="Proto-oncogene tyrosine-protein kinase Yrk"
FT /id="PRO_0000088188"
FT DOMAIN 81..142
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 148..245
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 270..523
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 10..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 276..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 419
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 530
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 536 AA; 60002 MW; 61BB5DEE000EE993 CRC64;
MGCVHCKEKI SGKGQGGSGT GTPAHPPSQY DPDPTQLSGA FTHIPDFNNF HAAAVSPPVP
FSGPGFYPCN TLQAHSSITG GGVTLFIALY DYEARTEDDL SFQKGEKFHI INNTEGDWWE
ARSLSSGATG YIPSNYVAPV DSIQAEEWYF GKIGRKDAER QLLCHGNCRG TFLIRESETT
KGAYSLSIRD WDEAKGDHVK HYKIRKLDSG GYYITTRAQF DTIQQLVQHY IERAAGLCCR
LAVPCPKGTP KLADLSVKTK DVWEIPRESL QLLQKLGNGQ FGEVWMGTWN GTTKVAVKTL
KPGTMSPEAF LEEAQIMKRL RHDKLVQLYA VVSEEPIYIV TEFMSQGSLL DFLKDGDGRY
LKLPQLVDMA AQIAAGMAYI ERMNYIHRDL RAANILVGDN LVCKIADFGL ARLIEDNEYT
ARQGAKFPIK WTAPEAALFG KFTIKSDVWS FGILLTELVT KGRVPYPGMN NREVLEQVER
GYRMQCPGGC PPSLHDVMVQ CWKREPEERP TFEYLQSFLE DYFTATEPQY QPGDNQ
