Tyrosine-protein kinase BTK - Mus musculus (Mouse)

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P35991 (BTK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Btk
Synonyms:	Bpk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	659 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Adaptive immunity Apoptosis Immunity Innate immunity Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Disease	Disease mutation
Domain	SH2 domain SH3 domain Zinc-finger
Ligand	ATP-binding Lipid-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB kinase/NF-kappaB cascade 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 innate immune response Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 10872802. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic vesicle Inferred from direct assay PubMed 14657254. Source: MGI cytosol Inferred from electronic annotation. Source: Compara membrane raft Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 11007757. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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: EC phosphatidylinositol-3,4,5-trisphosphate binding Inferred from electronic annotation. Source: Compara protein tyrosine kinase activity Inferred from direct assay PubMed 10872802 PubMed 11007757. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 659

658

Tyrosine-protein kinase BTK

PRO_0000088066

Regions

Domain

3 – 133

131

Domain

214 – 274

SH3

Domain

281 – 377

SH2

Domain

402 – 655

254

Protein kinase

Zinc finger

135 – 171

Btk-type

Nucleotide binding

408 – 416

ATP By similarity

Region

12 – 24

Inositol-(1,3,4,5)-tetrakisphosphate 1-binding By similarity

Region

474 – 479

Inhibitor-binding By similarity

Motif

581 – 588

CAV1-binding By similarity

Sites

Active site

521

Proton acceptor By similarity

Metal binding

143

Zinc By similarity

Metal binding

154

Zinc By similarity

Metal binding

155

Zinc By similarity

Metal binding

165

Zinc By similarity

Binding site

Inositol-(1,3,4,5)-tetrakisphosphate By similarity

Binding site

Inositol-(1,3,4,5)-tetrakisphosphate By similarity

Binding site

Inositol-(1,3,4,5)-tetrakisphosphate By similarity

Binding site

Inositol-(1,3,4,5)-tetrakisphosphate; via carbonyl oxygen By similarity

Binding site

430

ATP By similarity

Binding site

445

Inhibitor By similarity

Binding site

461

Inhibitor By similarity

Binding site

477

Inhibitor By similarity

Binding site

538

Inhibitor By similarity

Binding site

539

Inhibitor; via amide nitrogen By similarity

Binding site

542

Inhibitor; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphotyrosine Ref.13

Modified residue

Phosphoserine By similarity

Modified residue

115

Phosphoserine By similarity

Modified residue

179

Phosphoserine By similarity

Modified residue

180

Phosphoserine; by PKC/PRKCB By similarity

Modified residue

191

Phosphothreonine By similarity

Modified residue

223

Phosphotyrosine; by autocatalysis Ref.5

Modified residue

309

Phosphoserine By similarity

Modified residue

323

Phosphoserine By similarity

Modified residue

342

Phosphoserine By similarity

Modified residue

344

Phosphotyrosine Ref.13

Modified residue

361

Phosphotyrosine By similarity

Modified residue

375

Phosphotyrosine By similarity

Modified residue

551

Phosphotyrosine; by LYN and SYK Ref.7 Ref.13

Modified residue

602

Phosphothreonine By similarity

Modified residue

604

Phosphoserine By similarity

Modified residue

617

Phosphotyrosine By similarity

Modified residue

623

Phosphoserine By similarity

Modified residue

659

Phosphoserine By similarity

Natural variations

Natural variant

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

Experimental info

Mutagenesis

E → K: Constitutive activation. Ref.6

Mutagenesis

223

Y → F: No autophosphorylation. Ref.5

Mutagenesis

430

K → R: Loss of activity and no phosphorylation. Ref.5 Ref.6

Sequence conflict

V → A in L10627. Ref.2

Sequence conflict

123

R → P in AAA37316. Ref.1

Sequence conflict

197

I → IWI Ref.2

Sequence conflict

450

Missing in L10627. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P35991 [UniParc].

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

659

76,437

        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' referencesShow '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, MASS SPECTROMETRY. 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.
IPI	IPI00312116.
PIR	I49553.
RefSeq	NP_038510.2. NM_013482.2.
UniGene	Mm.4475.
3D structure databases
ProteinModelPortal	P35991.
SMR	P35991. Positions 2-170, 216-387, 395-657.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35991. 29 interactions.
PTM databases
PhosphoSite	P35991.
Proteomic databases
PaxDb	P35991.
PRIDE	P35991.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033617; ENSMUSP00000033617; ENSMUSG00000031264.
GeneID	12229.
KEGG	mmu:12229.
Organism-specific databases
CTD	695.
MGI	MGI:88216. Btk.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00640000091251.
HOGENOM	HOG000233859.
HOVERGEN	HBG008761.
InParanoid	P35991.
KO	K07370.
OrthoDB	EOG4DR9BX.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Gene expression databases
ArrayExpress	P35991.
Bgee	P35991.
CleanEx	MM_BTK.
Genevestigator	P35991.
GermOnline	ENSMUSG00000031264. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_cat_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]
Pfam	PF00779. BTK. 1 hit. PF00169. PH. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00402. TECBTKDOMAIN. PR00109. TYRKINASE.
SMART	SM00107. BTK. 1 hit. SM00233. PH. 1 hit. SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other
NextBio	280647.
SOURCE	Search...

Entry information

Entry name

BTK_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents