CSK_CHICK
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 03-AUG-2022, entry version 149.
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}.
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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.ENSGALP00000002008; -.
DR GeneID; 396396; -.
DR KEGG; gga:396396; -.
DR CTD; 1445; -.
DR VEuPathDB; HostDB:geneid_396396; -.
DR eggNOG; KOG0197; Eukaryota.
DR InParanoid; P41239; -.
DR OrthoDB; 491765at2759; -.
DR PhylomeDB; P41239; -.
DR BRENDA; 2.7.10.2; 1306.
DR PRO; PR:P41239; -.
DR Proteomes; UP000000539; Unplaced.
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; IEA:UniProtKB-EC.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR CDD; cd09937; SH2_csk_like; 1.
DR Gene3D; 3.30.505.10; -; 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 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; 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 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
