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P35991 (BTK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Btk
Synonyms:Bpk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.14

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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. Ref.11

Subunit structure

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. Ref.10 Ref.12

Subcellular location

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. Ref.10

Domain

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. Ref.8

Post-translational modification

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. Ref.5 Ref.7

Involvement in disease

Defects in Btk are the cause of murine X-linked immunodeficiency (XID). Ref.10 Ref.17

Disruption phenotype

Prevents BCR-induced activation of NF-kappa-B. Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.

Contains 1 Btk-type zinc finger.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Apoptosis
Immunity
Innate immunity
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   DiseaseDisease mutation
   DomainSH2 domain
SH3 domain
Zinc-finger
   LigandATP-binding
Lipid-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 14597404. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell maturation

Inferred from mutant phenotype PubMed 14734712. Source: MGI

histamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10872802. Source: MGI

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 12235209. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to organic substance

Inferred from electronic annotation. Source: Ensembl

response to reactive oxygen species

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11007757. Source: MGI

cytoplasmic vesicle

Inferred from direct assay PubMed 14657254. Source: MGI

cytosol

Traceable author statement. Source: Reactome

mast cell granule

Inferred from electronic annotation. Source: GOC

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 11007757. Source: MGI

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 15102471PubMed 21441935. Source: IntAct

protein tyrosine kinase activity

Inferred from direct assay PubMed 10872802PubMed 11007757. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 659658Tyrosine-protein kinase BTK
PRO_0000088066

Regions

Domain3 – 133131PH
Domain214 – 27461SH3
Domain281 – 37797SH2
Domain402 – 655254Protein kinase
Zinc finger135 – 17137Btk-type
Nucleotide binding408 – 4169ATP By similarity
Region12 – 2413Inositol-(1,3,4,5)-tetrakisphosphate 1-binding By similarity
Region474 – 4796Inhibitor-binding By similarity
Motif581 – 5888CAV1-binding By similarity

Sites

Active site5211Proton acceptor By similarity
Metal binding1431Zinc By similarity
Metal binding1541Zinc By similarity
Metal binding1551Zinc By similarity
Metal binding1651Zinc By similarity
Binding site261Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding site281Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding site391Inositol-(1,3,4,5)-tetrakisphosphate By similarity
Binding site531Inositol-(1,3,4,5)-tetrakisphosphate; via carbonyl oxygen By similarity
Binding site4301ATP By similarity
Binding site4451Inhibitor By similarity
Binding site4611Inhibitor By similarity
Binding site4771Inhibitor By similarity
Binding site5381Inhibitor By similarity
Binding site5391Inhibitor; via amide nitrogen By similarity
Binding site5421Inhibitor; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue211Phosphoserine By similarity
Modified residue401Phosphotyrosine Ref.13
Modified residue551Phosphoserine By similarity
Modified residue1151Phosphoserine By similarity
Modified residue1801Phosphoserine; by PKC/PRKCB By similarity
Modified residue1911Phosphothreonine By similarity
Modified residue2231Phosphotyrosine; by autocatalysis Ref.5
Modified residue3441Phosphotyrosine Ref.13
Modified residue3611Phosphotyrosine By similarity
Modified residue5511Phosphotyrosine; by LYN and SYK Ref.7 Ref.13
Modified residue6171Phosphotyrosine By similarity
Modified residue6231Phosphoserine By similarity
Modified residue6591Phosphoserine By similarity

Natural variations

Natural variant281R → C in XID; prevents interaction with ARID3A. Ref.10 Ref.17

Experimental info

Mutagenesis411E → K: Constitutive activation. Ref.6
Mutagenesis2231Y → F: No autophosphorylation. Ref.5
Mutagenesis4301K → R: Loss of activity and no phosphorylation. Ref.5 Ref.6
Sequence conflict671V → A in L10627. Ref.2
Sequence conflict1231R → P in AAA37316. Ref.1
Sequence conflict1971I → IWI Ref.2
Sequence conflict4501Missing in L10627. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35991 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: E502B798BC36E223

FASTA65976,437
        10         20         30         40         50         60 
MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG SKKGSIDVEK 

        70         80         90        100        110        120 
ITCVETVIPE KNPPPERQIP RRGEESSEME QISIIERFPY PFQVVYDEGP LYVFSPTEEL 

       130        140        150        160        170        180 
RKRWIHQLKN VIRYNSDLVQ KYHPCFWIDG QYLCCSQTAK NAMGCQILEN RNGSLKPGSS 

       190        200        210        220        230        240 
HRKTKKPLPP TPEEDQILKK PLPPEPTAAP ISTTELKKVV ALYDYMPMNA NDLQLRKGEE 

       250        260        270        280        290        300 
YFILEESNLP WWRARDKNGQ EGYIPSNYIT EAEDSIEMYE WYSKHMTRSQ AEQLLKQEGK 

       310        320        330        340        350        360 
EGGFIVRDSS KAGKYTVSVF AKSTGEPQGV IRHYVVCSTP QSQYYLAEKH LFSTIPELIN 

       370        380        390        400        410        420 
YHQHNSAGLI SRLKYPVSKQ NKNAPSTAGL GYGSWEIDPK DLTFLKELGT GQFGVVKYGK 

       430        440        450        460        470        480 
WRGQYDVAIK MIREGSMSED EFIEEAKVMM NLSHEKLVQL YGVCTKQRPI FIITEYMANG 

       490        500        510        520        530        540 
CLLNYLREMR HRFQTQQLLE MCKDVCEAME YLESKQFLHR DLAARNCLVN DQGVVKVSDF 

       550        560        570        580        590        600 
GLSRYVLDDE YTSSVGSKFP VRWSPPEVLM YSKFSSKSDI WAFGVLMWEI YSLGKMPYER 

       610        620        630        640        650 
FTNSETAEHI AQGLRLYRPH LASERVYTIM YSCWHEKADE RPSFKILLSN ILDVMDEES 

« Hide

References

« Hide 'large scale' references
[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]"Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice."
Rawlings D.J., Saffran D.C., Tsukada S., Largaespada D.A., Grimaldi J.C., Cohen L., Mohr R.N., Bazan J.F., Howard M., Copeland N.G., Jenkins N.A., Witte O.N.
Science 261:358-361(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XID CYS-28.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08967 mRNA. Translation: AAA37316.1.
L10627 mRNA. No translation available.
L29788 mRNA. Translation: AAA66943.1.
U58105 Genomic DNA. Translation: AAB47246.1.
CCDSCCDS30396.1.
PIRI49553.
RefSeqNP_038510.2. NM_013482.2.
XP_006528546.1. XM_006528483.1.
XP_006528547.1. XM_006528484.1.
XP_006528548.1. XM_006528485.1.
UniGeneMm.4475.

3D structure databases

ProteinModelPortalP35991.
SMRP35991. Positions 2-170, 216-387, 395-657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198400. 6 interactions.
IntActP35991. 29 interactions.
MINTMINT-1549372.

PTM databases

PhosphoSiteP35991.

Proteomic databases

MaxQBP35991.
PaxDbP35991.
PRIDEP35991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033617; ENSMUSP00000033617; ENSMUSG00000031264.
GeneID12229.
KEGGmmu:12229.
UCSCuc009uge.2. mouse.

Organism-specific databases

CTD695.
MGIMGI:88216. Btk.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091251.
HOGENOMHOG000233859.
HOVERGENHBG008761.
InParanoidP35991.
KOK07370.
OMASCRHYNI.
OrthoDBEOG7KM5SC.
PhylomeDBP35991.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressP35991.
BgeeP35991.
CleanExMM_BTK.
GenevestigatorP35991.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
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]
PfamPF00779. BTK. 1 hit.
PF00169. PH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00402. TECBTKDOMAIN.
PR00109. TYRKINASE.
SMARTSM00107. BTK. 1 hit.
SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50003. 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]
ProtoNetSearch...

Other

NextBio280647.
PROP35991.
SOURCESearch...

Entry information

Entry nameBTK_MOUSE
AccessionPrimary (citable) accession number: P35991
Secondary accession number(s): Q61365
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot