ID CSK_CHICK Reviewed; 450 AA. AC P41239; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 24-JAN-2024, entry version 155. DE RecName: Full=Tyrosine-protein kinase CSK; DE EC=2.7.10.2 {ECO:0000250|UniProtKB:P41240}; DE AltName: Full=C-Src kinase; GN Name=CSK; 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 TISSUE=Brain; RX PubMed=1372437; DOI=10.1073/pnas.89.6.2190; RA Sabe H., Knudsen B., Okada M., Nada S., Nakagawa H., Hanafusa H.; RT "Molecular cloning and expression of chicken C-terminal Src kinase: lack of RT stable association with c-Src protein."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2190-2194(1992). RN [2] RP FUNCTION. RX PubMed=7935444; DOI=10.1128/mcb.14.11.7306-7313.1994; RA Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H.; RT "Functional analysis of Csk in signal transduction through the B-cell RT antigen receptor."; RL Mol. Cell. Biol. 14:7306-7313(1994). CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an important CC role in the regulation of cell growth, differentiation, migration and CC immune response. Phosphorylates tyrosine residues located in the C- CC terminal tails of Src-family kinases (SFKs). Upon tail phosphorylation, CC Src-family members engage in intramolecular interactions between the CC phosphotyrosine tail and the SH2 domain that result in an inactive CC conformation. To inhibit SFKs, CSK is recruited to the plasma membrane CC via binding to transmembrane proteins or adapter proteins located near CC the plasma membrane (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:7935444}. 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:0000250|UniProtKB:P41240, ECO:0000255|PROSITE- CC ProRule:PRU10028}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P41240}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P41240}; CC -!- SUBUNIT: Homodimer (via SH3-domain). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The architecture of this protein is similar to that of Src- CC family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, CC and a C-terminal kinase domain. {ECO:0000250}. CC -!- PTM: Phosphorylated at Ser-364 by PKA, leading to increased activity. CC Autophosphorylated (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. CSK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; M85039; AAA51436.1; -; mRNA. DR PIR; A41973; A41973. DR RefSeq; NP_990756.1; NM_205425.1. DR AlphaFoldDB; P41239; -. DR SMR; P41239; -. DR BioGRID; 676646; 1. DR MINT; P41239; -. DR STRING; 9031.ENSGALP00000057776; -. DR PaxDb; 9031-ENSGALP00000002008; -. DR GeneID; 396396; -. DR KEGG; gga:396396; -. DR CTD; 1445; -. DR VEuPathDB; HostDB:geneid_396396; -. DR eggNOG; KOG0197; Eukaryota. DR InParanoid; P41239; -. DR PhylomeDB; P41239; -. DR BRENDA; 2.7.10.2; 1306. DR PRO; PR:P41239; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; IBA:GO_Central. DR CDD; cd09937; SH2_csk_like; 1. DR CDD; cd11769; SH3_CSK; 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; IPR035027; Csk-like_SH2. 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:SF407; TYROSINE-PROTEIN KINASE CSK; 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; 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. PE 2: Evidence at transcript level; KW Adaptive immunity; ATP-binding; Cytoplasm; Immunity; Kinase; Magnesium; KW Manganese; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; SH2 domain; SH3 domain; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1..450 FT /note="Tyrosine-protein kinase CSK" FT /id="PRO_0000088069" FT DOMAIN 9..70 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 82..171 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 195..450 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 9..70 FT /note="Interaction with PTPN8" FT /evidence="ECO:0000250" FT ACT_SITE 314 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 201..209 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 364 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250" FT MOD_RES 416 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P41240" SQ SEQUENCE 450 AA; 50751 MW; 5AA3C406AA4F246F CRC64; MSGMQAVWPS GTECIAKYNF HGTAEQDLPF SKGDVLTIVA VTKDPNWYKA KNKVGREGII PANYVQKREG VKAGIKLSLM PWFHGKITRE QAERLLYPPE TGLFLVREST NYPGDYTLCV SCEGKVEHYR IIYSSSKLSI DEEVYFENLM QLVEHYTTDA DGLCSRLIKP KVMEGTVAAQ DEFSRSGWAL NMKDLKLLQI IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM TQLRHSNLVQ LLGVIVEEKS GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE AMEYLEANNF VHRDLAARNV LVSEDNIAKV SDFGLTKEAS STQDTGKLPV KWTAPEALRE KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE KGYKMDPPDG CPAIVYEVMK KCWTLDPGHR PSFHQLREQL VHIKEKELYL //