UniProt: G7Q392

Database: UniProt
Entry: G7Q392_MACFA

LinkDB:  G7Q392_MACFA 
Original site:  G7Q392_MACFA

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (29)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (6)   
   SMART (4)   
All databases (40)   

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ID   G7Q392_MACFA            Unreviewed;       540 AA.
AC   G7Q392;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=BTK {ECO:0000313|Ensembl:ENSMFAP00000022951.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000022951.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000022951.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000022951.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   AlphaFoldDB; G7Q392; -.
DR   STRING; 9541.ENSMFAP00000022951; -.
DR   Ensembl; ENSMFAT00000031084.2; ENSMFAP00000022951.2; ENSMFAG00000043126.2.
DR   VEuPathDB; HostDB:ENSMFAG00000043126; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000158469; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000233100; Chromosome X.
DR   Bgee; ENSMFAG00000043126; Expressed in spleen and 6 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd10397; SH2_Tec_Btk; 1.
DR   CDD; cd11906; SH3_BTK; 1.
DR   Gene3D; 4.10.1130.10; btk motif of tyrosine-protein kinase itk; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR035574; BTK_SH3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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   InterPro; IPR001562; Znf_Btk_motif.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF92; TYROSINE-PROTEIN KINASE BTK; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00169; PH; 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; PR00452; SH3DOMAIN.
DR   PRINTS; PR00402; TECBTKDOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 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   PROSITE; PS51113; ZF_BTK; 1.
PE   3: Inferred from homology;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00432}.
FT   DOMAIN          186..246
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          253..349
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          374..540
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          143..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         402
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   540 AA;  62113 MW;  0A5E91579EBEB3C8 CRC64;
     MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG SKKGSIDVEK
     ITCVETVVPE KNPPPERQIP RRGEESSEME QISIIERFPY PFQIRYNSDL VQKYHPCFWI
     DGQYLCCSQT AKNAMGCQIL ENRNGSLKPG SSHRKTKKPL PPTPEEDQIL KKPLPPEPAA
     APVSTSELKK VVALYDYMPM NANDLQLRKG DEYFILEESN LPWWRARDKN GQEGYIPSNY
     VTEAEDSIEM YEWYSKHMTR SQAEQLLKQE GKEGGFIVRD SSKAGKYTVS VFAKSTGDPQ
     GVIRHYVVCS TPQSQYYLAE KHLFSTIPEL INYHQHNSAG LISRLKYPVS QQNKNAPSTA
     GLGYGSWEID PKDLTFLKEL GTGQFGVVKY GKWRGQYDVA IKMIKEGSMS EDEFIEEAKV
     MMNLSHEKLV QLYGVCTKQR PIFIITEYMA NGCLLNYLRE MRHRFQTQQL LEMCKDVCEA
     MEYLESKQFL HRDLAARNCL VNDQGVVKVS DFGLSRYVLD DEYTSSVGSK FPVRWSPPES
//

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