ID   CSK_BOVIN               Reviewed;         450 AA.
AC   Q0VBZ0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Tyrosine-protein kinase CSK;
DE            EC=2.7.10.2;
DE   AltName: Full=C-SRC kinase;
GN   Name=CSK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically phosphorylates 'Tyr-504' on LCK, which acts
CC       as a negative regulatory site. Can also act on the LYN and FYN
CC       kinases (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with PTPN8. Interacts with phosphorylated SIT1,
CC       PAG1, LIME1 and TGFB1I1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Mainly cytoplasmic, also present in lipid rafts
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC120437; AAI20438.1; -; mRNA.
DR   IPI; IPI00698198; -.
DR   RefSeq; NP_001068865.1; -.
DR   UniGene; Bt.20371; -.
DR   SMR; Q0VBZ0; 4-450.
DR   Ensembl; ENSBTAG00000021424; Bos taurus.
DR   GeneID; 509246; -.
DR   KEGG; bta:509246; -.
DR   HOVERGEN; Q0VBZ0; -.
DR   OMA; Q0VBZ0; QDLPFCK.
DR   BRENDA; 2.7.10.2; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kina...; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   InterPro; IPR008266; Tyr_pkinase_AS.
DR   InterPro; IPR015778; Tyrosine_Protein_Kinase_Csk.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   PANTHER; PTHR23256:SF264; Csk_ProtTyrKin; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   ProDom; PD000093; SH2; 1.
DR   ProDom; PD000066; SH3; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 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; Cell membrane; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    450       Tyrosine-protein kinase CSK.
FT                                /FTId=PRO_0000260260.
FT   DOMAIN        9     70       SH3.
FT   DOMAIN       82    171       SH2.
FT   DOMAIN      195    449       Protein kinase.
FT   NP_BIND     201    209       ATP (By similarity).
FT   REGION        9     70       Interaction with PTPN8 (By similarity).
FT   ACT_SITE    314    314       Proton acceptor (By similarity).
FT   BINDING     222    222       ATP (By similarity).
FT   MOD_RES     416    416       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   450 AA;  50633 MW;  B42BD31C645783D0 CRC64;
     MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA KNKVGREGII
     PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLCPPE TGLFLVREST NYPGDYTLCV
     SCDGKVEHYR IMYHASKLSI DEEVYFENLM QLVEHYTSDA DGLCTRLIKP KVMEGTVAAQ
     DEFFRSGWAL NMKDLKLLQT IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM
     TQLRHSNLVQ LLGVIVEEKS GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE
     AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV KWTAPEALRE
     KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE KGYKMDAPDG CPPAVYEVMK
     NCWHLDAATR PSFLQLREQL ERIKTHELHL
//