UniProtKB - P35991 (BTK_MOUSE)
Protein
Tyrosine-protein kinase BTK
Gene
Btk
Organism
Mus musculus (Mouse)
Status
Functioni
Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.6 Publications
Catalytic activityi
- EC:2.7.10.2PROSITE-ProRule annotation
Cofactori
Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
Activity regulationi
Activated by phosphorylation. In primary B lymphocytes, is almost always non-phosphorylated and is thus catalytically inactive. Stimulation of TLR8 and TLR9 causes BTK activation. As a negative feedback mechanism to fine-tune BCR signaling, activated PRKCB down-modulates BTK function via direct phosphorylation of BTK at Ser-180, resulting in translocation of BTK back to the cytoplasmic fraction. PIN1, SH3BP5, and IBTK were also identified as BTK activity inhibitors. Interaction with CAV1 leads to dramatic down-regulation of the kinase activity of BTK. LFM-13A is a specific inhibitor of BTK. Dasatinib, a cancer drug acting as a tyrosine kinase inhibitor, also blocks BTK activity.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 26 | Inositol-(1,3,4,5)-tetrakisphosphateBy similarity | 1 | |
Binding sitei | 28 | Inositol-(1,3,4,5)-tetrakisphosphateBy similarity | 1 | |
Binding sitei | 39 | Inositol-(1,3,4,5)-tetrakisphosphateBy similarity | 1 | |
Binding sitei | 53 | Inositol-(1,3,4,5)-tetrakisphosphate; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 143 | ZincBy similarity | 1 | |
Metal bindingi | 154 | ZincBy similarity | 1 | |
Metal bindingi | 155 | ZincBy similarity | 1 | |
Metal bindingi | 165 | ZincBy similarity | 1 | |
Binding sitei | 430 | ATPPROSITE-ProRule annotation | 1 | |
Binding sitei | 445 | InhibitorBy similarity | 1 | |
Binding sitei | 461 | InhibitorBy similarity | 1 | |
Binding sitei | 477 | InhibitorBy similarity | 1 | |
Active sitei | 521 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 538 | InhibitorBy similarity | 1 | |
Binding sitei | 539 | Inhibitor; via amide nitrogenBy similarity | 1 | |
Binding sitei | 542 | Inhibitor; via carbonyl oxygenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 135 – 171 | Btk-typePROSITE-ProRule annotationAdd BLAST | 37 | |
Nucleotide bindingi | 408 – 416 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: MGI
- metal ion binding Source: UniProtKB-KW
- non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
- phosphatidylinositol-3,4,5-trisphosphate binding Source: MGI
- protein tyrosine kinase activity Source: MGI
GO - Biological processi
- apoptotic process Source: UniProtKB-KW
- B cell affinity maturation Source: MGI
- cell maturation Source: MGI
- cellular response to interleukin-7 Source: MGI
- cellular response to molecule of fungal origin Source: MGI
- cellular response to reactive oxygen species Source: MGI
- histamine secretion by mast cell Source: MGI
- I-kappaB kinase/NF-kappaB signaling Source: MGI
- innate immune response Source: UniProtKB-KW
- negative regulation of B cell proliferation Source: MGI
- negative regulation of cytokine production Source: CACAO
- peptidyl-tyrosine phosphorylation Source: MGI
- positive regulation of type I hypersensitivity Source: MGI
- positive regulation of type III hypersensitivity Source: MGI
- protein autophosphorylation Source: MGI
- protein phosphorylation Source: MGI
- response to organic substance Source: MGI
Keywordsi
Molecular function | Kinase, Transferase, Tyrosine-protein kinase |
Biological process | Adaptive immunity, Apoptosis, Immunity, Innate immunity, Transcription, Transcription regulation |
Ligand | ATP-binding, Lipid-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 2.7.10.2, 3474 |
Reactomei | R-MMU-2029482, Regulation of actin dynamics for phagocytic cup formation R-MMU-2424491, DAP12 signaling R-MMU-2871809, FCERI mediated Ca+2 mobilization R-MMU-416476, G alpha (q) signalling events R-MMU-416482, G alpha (12/13) signalling events R-MMU-5663213, RHO GTPases Activate WASPs and WAVEs R-MMU-8964315, G beta:gamma signalling through BTK R-MMU-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
Names & Taxonomyi
Protein namesi | Recommended name: Tyrosine-protein kinase BTK (EC:2.7.10.2)Alternative name(s): Agammaglobulinemia tyrosine kinase Short name: ATK B-cell progenitor kinase Short name: BPK Bruton tyrosine kinase Kinase EMB |
Gene namesi | Name:Btk Synonyms:Bpk |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:88216, Btk |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
Nucleus
- Nucleus 1 Publication
Other locations
- Cytoplasm 1 Publication
Note: In steady state, BTK is predominantly cytosolic. Following B-cell receptor (BCR) engagement by antigen, translocates to the plasma membrane through its PH domain. Plasma membrane localization is a critical step in the activation of BTK. A fraction of BTK also shuttles between the nucleus and the cytoplasm, and nuclear export is mediated by the nuclear export receptor CRM1.By similarity
Cytosol
- cytosol Source: MGI
Nucleus
- nucleus Source: MGI
Plasma Membrane
- plasma membrane Source: MGI
Other locations
- cytoplasm Source: MGI
- cytoplasmic vesicle Source: MGI
- membrane raft Source: MGI
- perinuclear region of cytoplasm Source: MGI
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, NucleusPathology & Biotechi
Involvement in diseasei
Defects in Btk are the cause of murine X-linked immunodeficiency (XID).
Disruption phenotypei
Prevents BCR-induced activation of NF-kappa-B.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 41 | E → K: Constitutive activation. 1 Publication | 1 | |
Mutagenesisi | 223 | Y → F: No autophosphorylation. 1 Publication | 1 | |
Mutagenesisi | 430 | K → R: Loss of activity and no phosphorylation. 2 Publications | 1 |
Keywords - Diseasei
Disease variantChemistry databases
ChEMBLi | CHEMBL3259478 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000088066 | 2 – 659 | Tyrosine-protein kinase BTKAdd BLAST | 658 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 21 | PhosphoserineBy similarity | 1 | |
Modified residuei | 40 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 55 | PhosphoserineBy similarity | 1 | |
Modified residuei | 115 | PhosphoserineBy similarity | 1 | |
Modified residuei | 180 | Phosphoserine; by PKC/PRKCBBy similarity | 1 | |
Modified residuei | 191 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 223 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
Modified residuei | 344 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 361 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 551 | Phosphotyrosine; by LYN and SYKCombined sources1 Publication | 1 | |
Modified residuei | 604 | PhosphoserineBy similarity | 1 | |
Modified residuei | 617 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 623 | PhosphoserineBy similarity | 1 | |
Modified residuei | 659 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Following B-cell receptor (BCR) engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-551 by LYN and SYK. Phosphorylation at Tyr-551 is followed by autophosphorylation of Tyr-223 which may create a docking site for a SH2 containing protein. Phosphorylation at Ser-180 by PRKCB, leads in translocation of BTK back to the cytoplasmic fraction. Phosphorylation at Ser-21 and Ser-115 creates a binding site for PIN1 at these Ser-Pro motifs, and promotes it's recruitment (By similarity).By similarity
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | P35991 |
PaxDbi | P35991 |
PeptideAtlasi | P35991 |
PRIDEi | P35991 |
PTM databases
iPTMneti | P35991 |
PhosphoSitePlusi | P35991 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000031264, Expressed in granulocyte and 103 other tissues |
ExpressionAtlasi | P35991, baseline and differential |
Genevisiblei | P35991, MM |
Interactioni
Subunit structurei
Binds GTF2I through the PH domain.
Interacts with SH3BP5 via the SH3 domain.
Interacts with IBTK via its PH domain (By similarity).
Interacts with ARID3A.
Interacts with CAV1, FASLG, PIN1, TLR8 and TLR9 (By similarity).
By similarityBinary interactionsi
Hide detailsP35991
With | #Exp. | IntAct |
---|---|---|
Cd40 [P27512] | 3 | EBI-625119,EBI-525742 |
Grb2 [Q60631] | 4 | EBI-625119,EBI-1688 |
Myd88 [P22366] | 2 | EBI-625119,EBI-525108 |
Ticam1 [Q80UF7] | 2 | EBI-625119,EBI-3649271 |
GO - Molecular functioni
- identical protein binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 198400, 25 interactors |
CORUMi | P35991 |
ELMi | P35991 |
IntActi | P35991, 29 interactors |
STRINGi | 10090.ENSMUSP00000033617 |
Chemistry databases
BindingDBi | P35991 |
Miscellaneous databases
RNActi | P35991, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P35991 |
SMRi | P35991 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 3 – 133 | PHPROSITE-ProRule annotationAdd BLAST | 131 | |
Domaini | 214 – 274 | SH3PROSITE-ProRule annotationAdd BLAST | 61 | |
Domaini | 281 – 377 | SH2PROSITE-ProRule annotationAdd BLAST | 97 | |
Domaini | 402 – 655 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 254 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 12 – 24 | Inositol-(1,3,4,5)-tetrakisphosphate 1-bindingBy similarityAdd BLAST | 13 | |
Regioni | 474 – 479 | Inhibitor-bindingBy similarity | 6 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 581 – 588 | CAV1-bindingBy similarity | 8 |
Domaini
The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain.1 Publication
Sequence similaritiesi
Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 135 – 171 | Btk-typePROSITE-ProRule annotationAdd BLAST | 37 |
Keywords - Domaini
SH2 domain, SH3 domain, Zinc-fingerPhylogenomic databases
eggNOGi | KOG0197, Eukaryota |
GeneTreei | ENSGT00940000158469 |
HOGENOMi | CLU_000288_7_2_1 |
InParanoidi | P35991 |
OMAi | DPRHLTF |
OrthoDBi | 1047190at2759 |
PhylomeDBi | P35991 |
TreeFami | TF351634 |
Family and domain databases
CDDi | cd11906, SH3_BTK, 1 hit |
Gene3Di | 2.30.29.30, 1 hit 3.30.505.10, 1 hit |
InterProi | View protein in InterPro IPR035574, BTK_SH3 IPR011009, Kinase-like_dom_sf IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR001245, Ser-Thr/Tyr_kinase_cat_dom IPR000980, SH2 IPR036860, SH2_dom_sf IPR036028, SH3-like_dom_sf IPR001452, SH3_domain IPR008266, Tyr_kinase_AS IPR020635, Tyr_kinase_cat_dom IPR001562, Znf_Btk_motif |
Pfami | View protein in Pfam PF00779, BTK, 1 hit PF00169, PH, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit PF00017, SH2, 1 hit PF00018, SH3_1, 1 hit |
PRINTSi | PR00401, SH2DOMAIN PR00452, SH3DOMAIN PR00402, TECBTKDOMAIN PR00109, TYRKINASE |
SMARTi | View protein in SMART SM00107, BTK, 1 hit SM00233, PH, 1 hit SM00252, SH2, 1 hit SM00326, SH3, 1 hit SM00219, TyrKc, 1 hit |
SUPFAMi | SSF50044, SSF50044, 1 hit SSF55550, SSF55550, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50003, PH_DOMAIN, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00109, PROTEIN_KINASE_TYR, 1 hit PS50001, SH2, 1 hit PS50002, SH3, 1 hit PS51113, ZF_BTK, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P35991-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG
60 70 80 90 100
SKKGSIDVEK ITCVETVIPE KNPPPERQIP RRGEESSEME QISIIERFPY
110 120 130 140 150
PFQVVYDEGP LYVFSPTEEL RKRWIHQLKN VIRYNSDLVQ KYHPCFWIDG
160 170 180 190 200
QYLCCSQTAK NAMGCQILEN RNGSLKPGSS HRKTKKPLPP TPEEDQILKK
210 220 230 240 250
PLPPEPTAAP ISTTELKKVV ALYDYMPMNA NDLQLRKGEE YFILEESNLP
260 270 280 290 300
WWRARDKNGQ EGYIPSNYIT EAEDSIEMYE WYSKHMTRSQ AEQLLKQEGK
310 320 330 340 350
EGGFIVRDSS KAGKYTVSVF AKSTGEPQGV IRHYVVCSTP QSQYYLAEKH
360 370 380 390 400
LFSTIPELIN YHQHNSAGLI SRLKYPVSKQ NKNAPSTAGL GYGSWEIDPK
410 420 430 440 450
DLTFLKELGT GQFGVVKYGK WRGQYDVAIK MIREGSMSED EFIEEAKVMM
460 470 480 490 500
NLSHEKLVQL YGVCTKQRPI FIITEYMANG CLLNYLREMR HRFQTQQLLE
510 520 530 540 550
MCKDVCEAME YLESKQFLHR DLAARNCLVN DQGVVKVSDF GLSRYVLDDE
560 570 580 590 600
YTSSVGSKFP VRWSPPEVLM YSKFSSKSDI WAFGVLMWEI YSLGKMPYER
610 620 630 640 650
FTNSETAEHI AQGLRLYRPH LASERVYTIM YSCWHEKADE RPSFKILLSN
ILDVMDEES
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA2BDW0 | A2BDW0_MOUSE | Tyrosine-protein kinase | Btk | 483 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 67 | V → A in L10627 (PubMed:8476425).Curated | 1 | |
Sequence conflicti | 123 | R → P in AAA37316 (PubMed:8425221).Curated | 1 | |
Sequence conflicti | 197 | I → IWI (PubMed:8476425).Curated | 1 | |
Sequence conflicti | 450 | Missing in L10627 (PubMed:8476425).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 28 | R → C in XID; prevents interaction with ARID3A. 2 Publications | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L08967 mRNA Translation: AAA37316.1 L10627 mRNA No translation available. L29788 mRNA Translation: AAA66943.1 U58105 Genomic DNA Translation: AAB47246.1 |
CCDSi | CCDS30396.1 |
PIRi | I49553 |
RefSeqi | NP_038510.2, NM_013482.2 XP_006528546.1, XM_006528483.3 XP_006528547.1, XM_006528484.3 XP_006528548.1, XM_006528485.3 |
Genome annotation databases
Ensembli | ENSMUST00000033617; ENSMUSP00000033617; ENSMUSG00000031264 |
GeneIDi | 12229 |
KEGGi | mmu:12229 |
UCSCi | uc009uge.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L08967 mRNA Translation: AAA37316.1 L10627 mRNA No translation available. L29788 mRNA Translation: AAA66943.1 U58105 Genomic DNA Translation: AAB47246.1 |
CCDSi | CCDS30396.1 |
PIRi | I49553 |
RefSeqi | NP_038510.2, NM_013482.2 XP_006528546.1, XM_006528483.3 XP_006528547.1, XM_006528484.3 XP_006528548.1, XM_006528485.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4XI2 | X-ray | 2.60 | A | 214-659 | [»] | |
BMRBi | P35991 | |||||
SMRi | P35991 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 198400, 25 interactors |
CORUMi | P35991 |
ELMi | P35991 |
IntActi | P35991, 29 interactors |
STRINGi | 10090.ENSMUSP00000033617 |
Chemistry databases
BindingDBi | P35991 |
ChEMBLi | CHEMBL3259478 |
PTM databases
iPTMneti | P35991 |
PhosphoSitePlusi | P35991 |
Proteomic databases
MaxQBi | P35991 |
PaxDbi | P35991 |
PeptideAtlasi | P35991 |
PRIDEi | P35991 |
Protocols and materials databases
Antibodypediai | 699, 1212 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000033617; ENSMUSP00000033617; ENSMUSG00000031264 |
GeneIDi | 12229 |
KEGGi | mmu:12229 |
UCSCi | uc009uge.2, mouse |
Organism-specific databases
CTDi | 695 |
MGIi | MGI:88216, Btk |
Phylogenomic databases
eggNOGi | KOG0197, Eukaryota |
GeneTreei | ENSGT00940000158469 |
HOGENOMi | CLU_000288_7_2_1 |
InParanoidi | P35991 |
OMAi | DPRHLTF |
OrthoDBi | 1047190at2759 |
PhylomeDBi | P35991 |
TreeFami | TF351634 |
Enzyme and pathway databases
BRENDAi | 2.7.10.2, 3474 |
Reactomei | R-MMU-2029482, Regulation of actin dynamics for phagocytic cup formation R-MMU-2424491, DAP12 signaling R-MMU-2871809, FCERI mediated Ca+2 mobilization R-MMU-416476, G alpha (q) signalling events R-MMU-416482, G alpha (12/13) signalling events R-MMU-5663213, RHO GTPases Activate WASPs and WAVEs R-MMU-8964315, G beta:gamma signalling through BTK R-MMU-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
Miscellaneous databases
BioGRID-ORCSi | 12229, 0 hits in 17 CRISPR screens |
ChiTaRSi | Btk, mouse |
PROi | PR:P35991 |
RNActi | P35991, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000031264, Expressed in granulocyte and 103 other tissues |
ExpressionAtlasi | P35991, baseline and differential |
Genevisiblei | P35991, MM |
Family and domain databases
CDDi | cd11906, SH3_BTK, 1 hit |
Gene3Di | 2.30.29.30, 1 hit 3.30.505.10, 1 hit |
InterProi | View protein in InterPro IPR035574, BTK_SH3 IPR011009, Kinase-like_dom_sf IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR001245, Ser-Thr/Tyr_kinase_cat_dom IPR000980, SH2 IPR036860, SH2_dom_sf IPR036028, SH3-like_dom_sf IPR001452, SH3_domain IPR008266, Tyr_kinase_AS IPR020635, Tyr_kinase_cat_dom IPR001562, Znf_Btk_motif |
Pfami | View protein in Pfam PF00779, BTK, 1 hit PF00169, PH, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit PF00017, SH2, 1 hit PF00018, SH3_1, 1 hit |
PRINTSi | PR00401, SH2DOMAIN PR00452, SH3DOMAIN PR00402, TECBTKDOMAIN PR00109, TYRKINASE |
SMARTi | View protein in SMART SM00107, BTK, 1 hit SM00233, PH, 1 hit SM00252, SH2, 1 hit SM00326, SH3, 1 hit SM00219, TyrKc, 1 hit |
SUPFAMi | SSF50044, SSF50044, 1 hit SSF55550, SSF55550, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS50003, PH_DOMAIN, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00109, PROTEIN_KINASE_TYR, 1 hit PS50001, SH2, 1 hit PS50002, SH3, 1 hit PS51113, ZF_BTK, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BTK_MOUSE | |
Accessioni | P35991Primary (citable) accession number: P35991 Secondary accession number(s): Q61365 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 204 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human and mouse protein kinases
Human and mouse protein kinases: classification and index