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P35991

- BTK_MOUSE

UniProt

P35991 - BTK_MOUSE

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Protein

Tyrosine-protein kinase BTK

Gene
Btk, Bpk
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Enzyme 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding sitei28 – 281Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding sitei39 – 391Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding sitei53 – 531Inositol-(1,3,4,5)-tetrakisphosphate; via carbonyl oxygen By similarity
Metal bindingi143 – 1431Zinc By similarity
Metal bindingi154 – 1541Zinc By similarity
Metal bindingi155 – 1551Zinc By similarity
Metal bindingi165 – 1651Zinc By similarity
Binding sitei430 – 4301ATP By similarity
Binding sitei445 – 4451Inhibitor By similarity
Binding sitei461 – 4611Inhibitor By similarity
Binding sitei477 – 4771Inhibitor By similarity
Active sitei521 – 5211Proton acceptor By similarity
Binding sitei538 – 5381Inhibitor By similarity
Binding sitei539 – 5391Inhibitor; via amide nitrogen By similarity
Binding sitei542 – 5421Inhibitor; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri135 – 17137Btk-typeAdd
BLAST
Nucleotide bindingi408 – 4169ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
  5. protein binding Source: IntAct
  6. protein tyrosine kinase activity Source: MGI

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell maturation Source: MGI
  3. histamine secretion by mast cell Source: Ensembl
  4. I-kappaB kinase/NF-kappaB signaling Source: MGI
  5. innate immune response Source: UniProtKB-KW
  6. peptidyl-tyrosine phosphorylation Source: MGI
  7. protein autophosphorylation Source: Ensembl
  8. protein phosphorylation Source: MGI
  9. regulation of transcription, DNA-templated Source: UniProtKB-KW
  10. response to organic substance Source: Ensembl
  11. response to reactive oxygen species Source: Ensembl
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Apoptosis, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Lipid-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:88216. Btk.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus
Note: In steady state, BTK is predominantly cytosolic By similarity. Following B-cell receptor (BCR) engagement by antigen, translocates to the plasma membrane through its PH domain By similarity. Plasma membrane localization is a critical step in the activation of BTK By similarity. 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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic vesicle Source: MGI
  3. cytosol Source: Reactome
  4. mast cell granule Source: GOC
  5. membrane raft Source: Ensembl
  6. nucleus Source: MGI
  7. perinuclear region of cytoplasm Source: Ensembl
  8. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in Btk are the cause of murine X-linked immunodeficiency (XID).2 Publications

Disruption phenotypei

Prevents BCR-induced activation of NF-kappa-B.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411E → K: Constitutive activation. 1 Publication
Mutagenesisi223 – 2231Y → F: No autophosphorylation. 1 Publication
Mutagenesisi430 – 4301K → R: Loss of activity and no phosphorylation. 2 Publications

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 659658Tyrosine-protein kinase BTKPRO_0000088066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei21 – 211Phosphoserine By similarity
Modified residuei40 – 401Phosphotyrosine1 Publication
Modified residuei55 – 551Phosphoserine By similarity
Modified residuei115 – 1151Phosphoserine By similarity
Modified residuei180 – 1801Phosphoserine; by PKC/PRKCB By similarity
Modified residuei191 – 1911Phosphothreonine By similarity
Modified residuei223 – 2231Phosphotyrosine; by autocatalysis1 Publication
Modified residuei344 – 3441Phosphotyrosine1 Publication
Modified residuei361 – 3611Phosphotyrosine By similarity
Modified residuei551 – 5511Phosphotyrosine; by LYN and SYK2 Publications
Modified residuei617 – 6171Phosphotyrosine By similarity
Modified residuei623 – 6231Phosphoserine By similarity
Modified residuei659 – 6591Phosphoserine By similarity

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP35991.
PaxDbiP35991.
PRIDEiP35991.

PTM databases

PhosphoSiteiP35991.

Expressioni

Gene expression databases

ArrayExpressiP35991.
BgeeiP35991.
CleanExiMM_BTK.
GenevestigatoriP35991.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd40P275123EBI-625119,EBI-525742
Grb2Q606314EBI-625119,EBI-1688
Myd88P223662EBI-625119,EBI-525108
Ticam1Q80UF72EBI-625119,EBI-3649271

Protein-protein interaction databases

BioGridi198400. 6 interactions.
IntActiP35991. 29 interactions.
MINTiMINT-1549372.

Structurei

3D structure databases

ProteinModelPortaliP35991.
SMRiP35991. Positions 2-170, 216-387, 395-657.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 133131PHAdd
BLAST
Domaini214 – 27461SH3Add
BLAST
Domaini281 – 37797SH2Add
BLAST
Domaini402 – 655254Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 2413Inositol-(1,3,4,5)-tetrakisphosphate 1-binding By similarityAdd
BLAST
Regioni474 – 4796Inhibitor-binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi581 – 5888CAV1-binding By similarity

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

Contains 1 PH domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri135 – 17137Btk-typeAdd
BLAST

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091251.
HOGENOMiHOG000233859.
HOVERGENiHBG008761.
InParanoidiP35991.
KOiK07370.
OMAiSCRHYNI.
OrthoDBiEOG7KM5SC.
PhylomeDBiP35991.
TreeFamiTF351634.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamiPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTiSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50003. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35991-1 [UniParc]FASTAAdd to Basket

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MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG    50
SKKGSIDVEK ITCVETVIPE KNPPPERQIP RRGEESSEME QISIIERFPY 100
PFQVVYDEGP LYVFSPTEEL RKRWIHQLKN VIRYNSDLVQ KYHPCFWIDG 150
QYLCCSQTAK NAMGCQILEN RNGSLKPGSS HRKTKKPLPP TPEEDQILKK 200
PLPPEPTAAP ISTTELKKVV ALYDYMPMNA NDLQLRKGEE YFILEESNLP 250
WWRARDKNGQ EGYIPSNYIT EAEDSIEMYE WYSKHMTRSQ AEQLLKQEGK 300
EGGFIVRDSS KAGKYTVSVF AKSTGEPQGV IRHYVVCSTP QSQYYLAEKH 350
LFSTIPELIN YHQHNSAGLI SRLKYPVSKQ NKNAPSTAGL GYGSWEIDPK 400
DLTFLKELGT GQFGVVKYGK WRGQYDVAIK MIREGSMSED EFIEEAKVMM 450
NLSHEKLVQL YGVCTKQRPI FIITEYMANG CLLNYLREMR HRFQTQQLLE 500
MCKDVCEAME YLESKQFLHR DLAARNCLVN DQGVVKVSDF GLSRYVLDDE 550
YTSSVGSKFP VRWSPPEVLM YSKFSSKSDI WAFGVLMWEI YSLGKMPYER 600
FTNSETAEHI AQGLRLYRPH LASERVYTIM YSCWHEKADE RPSFKILLSN 650
ILDVMDEES 659
Length:659
Mass (Da):76,437
Last modified:January 23, 2007 - v4
Checksum:iE502B798BC36E223
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281R → C in XID; prevents interaction with ARID3A. 2 Publications

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671V → A in L10627. 1 Publication
Sequence conflicti123 – 1231R → P in AAA37316. 1 Publication
Sequence conflicti197 – 1971I → IWI1 Publication
Sequence conflicti450 – 4501Missing in L10627. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L08967 mRNA. Translation: AAA37316.1.
L10627 mRNA. No translation available.
L29788 mRNA. Translation: AAA66943.1.
U58105 Genomic DNA. Translation: AAB47246.1.
CCDSiCCDS30396.1.
PIRiI49553.
RefSeqiNP_038510.2. NM_013482.2.
XP_006528546.1. XM_006528483.1.
XP_006528547.1. XM_006528484.1.
XP_006528548.1. XM_006528485.1.
UniGeneiMm.4475.

Genome annotation databases

EnsembliENSMUST00000033617; ENSMUSP00000033617; ENSMUSG00000031264.
GeneIDi12229.
KEGGimmu:12229.
UCSCiuc009uge.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006528483.1.
XP_006528547.1. XM_006528484.1.
XP_006528548.1. XM_006528485.1.
UniGenei Mm.4475.

3D structure databases

ProteinModelPortali P35991.
SMRi P35991. Positions 2-170, 216-387, 395-657.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198400. 6 interactions.
IntActi P35991. 29 interactions.
MINTi MINT-1549372.

PTM databases

PhosphoSitei P35991.

Proteomic databases

MaxQBi P35991.
PaxDbi P35991.
PRIDEi P35991.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 COG0515.
GeneTreei ENSGT00640000091251.
HOGENOMi HOG000233859.
HOVERGENi HBG008761.
InParanoidi P35991.
KOi K07370.
OMAi SCRHYNI.
OrthoDBi EOG7KM5SC.
PhylomeDBi P35991.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_188185. DAP12 signaling.
REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.

Miscellaneous databases

NextBioi 280647.
PROi P35991.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35991.
Bgeei P35991.
CleanExi MM_BTK.
Genevestigatori P35991.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001562. Znf_Btk_motif.
[Graphical view ]
Pfami PF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTi SM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia."
    Tsukada S., Saffran D.C., Rawlings D.J., Parolini O., Allen R.C., Klisak I., Sparkes R.S., Kubagawa H., Mohandas T., Quan S., Belmont J.W., Cooper M.D., Conley M.E., Witte O.N.
    Cell 72:279-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure and expression of novel protein-tyrosine kinases, Emb and Emt, in hematopoietic cells."
    Yamada N., Kawakami Y., Kimura H., Fukamachi H., Baier G., Altman A., Kato T., Inagaki Y., Kawakami T.
    Biochem. Biophys. Res. Commun. 192:231-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genomic organization of mouse and human Bruton's agammaglobulinemia tyrosine kinase (Btk) loci."
    Sideras P., Mueller S., Shiels H., Jin H., Khan W.N., Nilsson L., Parkinson E., Thomas J.D., Branden L., Larsson I., Paul W.E., Rosen F.S., Alt F.W., Vetrie D., Smith C.I.E., Xanthopoulos K.G.
    J. Immunol. 153:5607-5617(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci."
    Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A.
    Mamm. Genome 6:334-338(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C129.
  5. "Regulation of Btk function by a major autophosphorylation site within the SH3 domain."
    Park H., Wahl M.I., Afar D.E., Turck C.W., Rawlings D.J., Tam C., Scharenberg A.M., Kinet J.P., Witte O.N.
    Immunity 4:515-525(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 219-233, PHOSPHORYLATION AT TYR-223, MUTAGENESIS OF TYR-223 AND LYS-430.
  6. "Activation of Bruton's tyrosine kinase (BTK) by a point mutation in its pleckstrin homology (PH) domain."
    Li T., Tsukada S., Satterthwaite A., Havlik M.H., Park H., Takatsu K., Witte O.N.
    Immunity 2:451-460(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-41 AND LYS-430.
  7. "Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases."
    Rawlings D.J., Scharenberg A.M., Park H., Wahl M.I., Lin S., Kato R.M., Fluckiger A.C., Witte O.N., Kinet J.P.
    Science 271:822-825(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT TYR-551.
  8. "Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain."
    Kojima T., Fukuda M., Watanabe Y., Hamazato F., Mikoshiba K.
    Biochem. Biophys. Res. Commun. 236:333-339(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  9. "Bruton's tyrosine kinase is required for activation of IkappaB kinase and nuclear factor kappaB in response to B cell receptor engagement."
    Petro J.B., Rahman S.M., Ballard D.W., Khan W.N.
    J. Exp. Med. 191:1745-1754(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "The transcription factor Bright associates with Bruton's tyrosine kinase, the defective protein in immunodeficiency disease."
    Webb C.F., Yamashita Y., Ayers N., Evetts S., Paulin Y., Conley M.E., Smith E.A.
    J. Immunol. 165:6956-6965(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARID3A, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT XID CYS-28.
  11. "Regulation of protein kinase CbetaI by two protein-tyrosine kinases, Btk and Syk."
    Kawakami Y., Kitaura J., Hartman S.E., Lowell C.A., Siraganian R.P., Kawakami T.
    Proc. Natl. Acad. Sci. U.S.A. 97:7423-7428(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  12. "Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I."
    Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.
    Mol. Cell. Biol. 26:4758-4768(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GTF2I AND ARID3A, FUNCTION.
  13. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40; TYR-344 AND TYR-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  14. "Defective Toll-like receptor 9-mediated cytokine production in B cells from Bruton's tyrosine kinase-deficient mice."
    Hasan M., Lopez-Herrera G., Blomberg K.E., Lindvall J.M., Berglof A., Smith C.I., Vargas L.
    Immunology 123:239-249(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE TLR PATHWAY.
  15. "Bruton's tyrosine kinase (BTK) as a dual-function regulator of apoptosis."
    Uckun F.M.
    Biochem. Pharmacol. 56:683-691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN REGULATION OF APOPTOSIS.
  16. "Bruton's tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain."
    Mohamed A.J., Yu L., Backesjo C.M., Vargas L., Faryal R., Aints A., Christensson B., Berglof A., Vihinen M., Nore B.F., Smith C.I.
    Immunol. Rev. 228:58-73(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
  17. Cited for: VARIANT XID CYS-28.

Entry informationi

Entry nameiBTK_MOUSE
AccessioniPrimary (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: September 3, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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