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Q06187 (BTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Gene names
Name:BTK
Synonyms:AGMX1, ATK, BPK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.16 Ref.23 Ref.28 Ref.29 Ref.30 Ref.31

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

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.15 Ref.19 Ref.22 Ref.24 Ref.25 Ref.27 Ref.30 Ref.31

Subunit structure

Binds GTF2I through the PH domain. Interacts with SH3BP5 via the SH3 domain. Interacts with IBTK via its PH domain. Interacts with ARID3A, CAV1, FASLG, PIN1, TLR8 and TLR9. Ref.17 Ref.19 Ref.24 Ref.25 Ref.27 Ref.29 Ref.31 Ref.32

Subcellular location

Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. 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. Ref.18 Ref.20 Ref.21 Ref.25

Tissue specificity

Predominantly expressed in B-lymphocytes.

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.14 Ref.18 Ref.25 Ref.40

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. Ref.12 Ref.15 Ref.16 Ref.22 Ref.26 Ref.27 Ref.31

Involvement in disease

X-linked agammaglobulinemia (XLA) [MIM:300755]: Humoral immunodeficiency disease which results in developmental defects in the maturation pathway of B-cells. Affected boys have normal levels of pre-B-cells in their bone marrow but virtually no circulating mature B-lymphocytes. This results in a lack of immunoglobulins of all classes and leads to recurrent bacterial infections like otitis, conjunctivitis, dermatitis, sinusitis in the first few years of life, or even some patients present overwhelming sepsis or meningitis, resulting in death in a few hours. Treatment in most cases is by infusion of intravenous immunoglobulin.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.13 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72

X-linked hypogammaglobulinemia and isolated growth hormone deficiency (XLA-IGHD) [MIM:307200]: In rare cases XLA is inherited together with isolated growth hormone deficiency (IGHD).
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.13

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
   Coding sequence diversityAlternative promoter usage
Polymorphism
   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 term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement Ref.34. Source: UniProtKB

B cell receptor signaling pathway

Traceable author statement Ref.34. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

adaptive immune response

Traceable author statement Ref.34. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement PubMed 8688094. Source: ProtInc

calcium-mediated signaling

Traceable author statement PubMed 15046600. Source: HGNC

cell maturation

Inferred from electronic annotation. Source: Ensembl

histamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement Ref.34. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

mesoderm development

Traceable author statement Ref.13. Source: ProtInc

positive regulation of B cell differentiation

Traceable author statement Ref.34. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Traceable author statement Ref.34. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement PubMed 11913944. Source: HGNC

regulation of B cell apoptotic process

Traceable author statement Ref.34. Source: UniProtKB

regulation of B cell cytokine production

Traceable author statement Ref.34. Source: UniProtKB

response to organic substance

Inferred from electronic annotation. Source: Ensembl

response to reactive oxygen species

Inferred from electronic annotation. Source: Ensembl

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Traceable author statement PubMed 15046600. Source: ProtInc

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 17823121. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mast cell granule

Inferred from electronic annotation. Source: GOC

membrane raft

Inferred from direct assay PubMed 15046600. Source: HGNC

nucleus

Traceable author statement Ref.34. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17823121. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.24. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Traceable author statement Ref.34. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay PubMed 17823121. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform BTK-A (identifier: Q06187-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform BTK-C (identifier: Q06187-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MASWSIQQMVIGCPLCGRHCSGGEHTGELQKEEAM
Note: Produced by alternative promoter usage. Predominant form in many tumor cells where it may function as an anti-apoptotic cell survival factor.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 659658Tyrosine-protein kinase BTK
PRO_0000088065

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
Region474 – 4796Inhibitor-binding
Motif581 – 5888CAV1-binding

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.11
Modified residue211Phosphoserine Ref.27
Modified residue401Phosphotyrosine By similarity
Modified residue551Phosphoserine Ref.35
Modified residue1151Phosphoserine Ref.27
Modified residue1801Phosphoserine; by PKC/PRKCB Ref.22
Modified residue1911Phosphothreonine Ref.35
Modified residue2231Phosphotyrosine; by autocatalysis Ref.12 Ref.15 Ref.16 Ref.31
Modified residue3441Phosphotyrosine By similarity
Modified residue3611Phosphotyrosine Ref.35
Modified residue5511Phosphotyrosine; by LYN and SYK Ref.15 Ref.16
Modified residue6171Phosphotyrosine Ref.26
Modified residue6231Phosphoserine Ref.26
Modified residue6591Phosphoserine Ref.35

Natural variations

Alternative sequence11M → MASWSIQQMVIGCPLCGRHC SGGEHTGELQKEEAM in isoform BTK-C.
VSP_053838
Natural variant111L → P in XLA.
VAR_006216
Natural variant121K → R in XLA. Ref.64
VAR_006217
Natural variant141S → F in XLA.
VAR_006218
Natural variant191K → E in XLA. Ref.69
VAR_008291
Natural variant251F → S in XLA. Ref.57
VAR_006219
Natural variant271K → R in XLA.
VAR_008292
Natural variant281R → C in XLA; no effect on phosphorylation of GTF2I.
VAR_008293
Natural variant281R → H in XLA; moderate. Ref.52 Ref.54 Ref.69
VAR_006220
Natural variant281R → P in XLA. Ref.64
VAR_006221
Natural variant331T → P in XLA; severe. Ref.54 Ref.59
VAR_006222
Natural variant391Y → S in XLA. Ref.72
VAR_008960
Natural variant401Y → C in XLA.
VAR_008294
Natural variant401Y → N in XLA.
VAR_008295
Natural variant611I → N in XLA. Ref.69
VAR_008296
Natural variant641V → D in XLA.
VAR_008297
Natural variant641V → F in XLA. Ref.56
VAR_006223
Natural variant821R → K. Ref.73
Corresponds to variant rs56035945 [ dbSNP | Ensembl ].
VAR_041676
Natural variant1031Q → QSVFSSTR in XLA.
VAR_006224
Natural variant1131V → D in XLA. Ref.53
VAR_006225
Natural variant1151S → F in XLA.
VAR_008298
Natural variant1171T → P in XLA. Ref.69
VAR_008299
Natural variant1271Q → H in XLA. Ref.69
VAR_008300
Natural variant1541C → S in XLA. Ref.66
VAR_008301
Natural variant1551C → G in XLA.
VAR_008302
Natural variant1551C → R in XLA. Ref.66 Ref.69
VAR_008303
Natural variant1841T → P in XLA.
VAR_008304
Natural variant1901P → K in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. Ref.73
VAR_041677
Natural variant260 – 28021Missing in XLA; severe.
VAR_006226
Natural variant2881R → Q in XLA. Ref.68
VAR_008305
Natural variant2881R → W in XLA. Ref.51 Ref.52 Ref.57 Ref.65
VAR_006227
Natural variant2951L → P in XLA. Ref.63 Ref.69
VAR_006228
Natural variant3021G → E in XLA. Ref.61 Ref.64
VAR_006230
Natural variant3021G → R in XLA.
VAR_008306
Natural variant3021Missing in XLA. Ref.59
VAR_006229
Natural variant3071R → G in XLA; loss of activity. Ref.51
VAR_006231
Natural variant3071R → T in XLA. Ref.68
VAR_008307
Natural variant3081D → E in XLA.
VAR_008308
Natural variant3191V → A in XLA; moderate.
VAR_008309
Natural variant3341Y → S in XLA. Ref.5
VAR_006232
Natural variant3581L → F in XLA. Ref.62
VAR_006233
Natural variant3611Y → C in XLA; mild. Ref.53
Corresponds to variant rs28935478 [ dbSNP | Ensembl ].
VAR_006234
Natural variant3621H → Q in XLA.
VAR_006235
Natural variant3641H → P in XLA.
VAR_006236
Natural variant3651N → Y in XLA.
VAR_006237
Natural variant3661S → F in XLA.
VAR_008310
Natural variant3691L → F in XLA. Ref.69
VAR_008311
Natural variant3701I → M in XLA. Ref.57
VAR_006238
Natural variant3721R → G in XLA. Ref.69
VAR_008312
Natural variant4081L → P in XLA; moderate. Ref.54
VAR_006239
Natural variant4141G → R in XLA. Ref.69
VAR_008313
Natural variant4181Y → H in XLA.
VAR_006240
Natural variant4291I → N in XLA. Ref.60
VAR_006241
Natural variant4301K → E in XLA; loss of phosphorylation of GTF2I. Ref.55
VAR_006242
Natural variant4301K → R in XLA. Ref.68
VAR_008314
Natural variant4451E → D in XLA. Ref.68
VAR_008315
Natural variant4621G → D in XLA.
VAR_008316
Natural variant4621G → V in XLA.
VAR_008317
Natural variant4761Y → D in XLA. Ref.61
VAR_006243
Natural variant4771M → R in XLA. Ref.60
VAR_006244
Natural variant5021C → F in XLA.
VAR_006245
Natural variant5021C → W in XLA. Ref.64
VAR_006246
Natural variant5061C → R in XLA. Ref.5
VAR_006247
Natural variant5061C → Y in XLA. Ref.69
VAR_006248
Natural variant5081A → D in XLA.
VAR_008318
Natural variant5091M → I in XLA.
VAR_008319
Natural variant5091M → V in XLA. Ref.57
VAR_006249
Natural variant5121L → P in XLA. Ref.72
VAR_008961
Natural variant5121L → Q in XLA. Ref.72
VAR_008962
Natural variant5181L → R in XLA.
VAR_008320
Natural variant5201R → Q in XLA; severe; prevents activation due to absence of contact between the catalytic loop and the regulatory phosphorylated residue. Ref.5 Ref.53 Ref.55 Ref.59
VAR_006251
Natural variant5211D → G in XLA. Ref.69
VAR_008321
Natural variant5211D → H in XLA; severe. Ref.64
VAR_006252
Natural variant5211D → N in XLA; severe.
VAR_006253
Natural variant5231A → E in XLA.
VAR_008322
Natural variant5251R → G in XLA. Ref.68
VAR_008323
Natural variant5251R → P in XLA. Ref.57
VAR_006254
Natural variant5251R → Q in XLA; severe; disturbs ATP-binding. Ref.55 Ref.69
VAR_006255
Natural variant5261N → K in XLA. Ref.57
VAR_006256
Natural variant5351V → F in XLA. Ref.68
VAR_008324
Natural variant5421L → P in XLA; growth hormone deficiency. Ref.53
VAR_006257
Natural variant5441R → G in XLA. Ref.72
VAR_008963
Natural variant5441R → K in XLA. Ref.65
VAR_006258
Natural variant5591F → S in XLA. Ref.69
VAR_008325
Natural variant5621R → P in XLA. Ref.55 Ref.71
Corresponds to variant rs28935176 [ dbSNP | Ensembl ].
VAR_006259
Natural variant5621R → W in XLA. Ref.5 Ref.53 Ref.57 Ref.69
VAR_006260
Natural variant5631W → L in XLA. Ref.68
VAR_008326
Natural variant5671E → K in XLA; severe. Ref.58
VAR_006261
Natural variant5781S → Y in XLA. Ref.72
VAR_008964
Natural variant5811W → R in XLA.
VAR_006262
Natural variant5821A → V in XLA. Ref.55 Ref.57
VAR_006263
Natural variant5831F → S in XLA.
VAR_008327
Natural variant5871M → L in XLA; mild. Ref.58
VAR_006264
Natural variant5891E → D in XLA.
VAR_008328
Natural variant5891E → G in XLA; moderate; interferes with substrate binding. Ref.54 Ref.55
VAR_006265
Natural variant5891E → K in XLA. Ref.72
VAR_008965
Natural variant5921S → P in XLA. Ref.65
VAR_006267
Natural variant5941G → E in XLA; mild; interferes with substrate binding. Ref.55 Ref.69
VAR_006268
Natural variant5941G → R in XLA. Ref.57
VAR_006269
Natural variant5981Y → C in XLA.
VAR_006270
Natural variant6071A → D in XLA; mild. Ref.51
VAR_006271
Natural variant6131G → D in XLA; mild; interferes with substrate binding and/or domain interactions. Ref.54 Ref.55
VAR_006272
Natural variant6191P → A in XLA.
VAR_008330
Natural variant6191P → S in XLA.
VAR_006273
Natural variant6191P → T in XLA. Ref.69
VAR_008331
Natural variant6221A → P in XLA. Ref.68
VAR_008332
Natural variant6261V → G in XLA. Ref.69
VAR_008333
Natural variant6301M → I Polymorphism, 35%.
VAR_006274
Natural variant6301M → K in XLA. Ref.5 Ref.53
VAR_006275
Natural variant6301M → T in XLA.
VAR_008334
Natural variant6331C → Y in XLA. Ref.64
VAR_006276
Natural variant6411R → C in XLA. Ref.59
VAR_006277
Natural variant6411R → H in XLA; severe. Ref.58 Ref.69
VAR_006278
Natural variant6441F → L in XLA.
VAR_008335
Natural variant6441F → S in XLA. Ref.64
VAR_006279
Natural variant6471L → P in XLA.
VAR_006280
Natural variant6521L → P in XLA. Ref.53
VAR_006281

Experimental info

Mutagenesis411E → K: No effect on phosphorylation of GTF2I. Ref.16 Ref.17
Mutagenesis1891P → A: No effect on phosphorylation of GTF2I. Ref.16 Ref.17
Mutagenesis2231Y → F: Loss of phosphorylation of GTF2I. Ref.15 Ref.16 Ref.17
Mutagenesis251 – 2522WW → LL: Large decrease in binding by SH3BP5. Ref.16 Ref.17
Mutagenesis2511W → L: No effect on phosphorylation of GTF2I. Ref.16 Ref.17
Mutagenesis3071R → K: Loss of phosphorylation of GTF2I. Ref.16 Ref.17
Mutagenesis5511Y → F: Loss of phosphorylation of GTF2I. Ref.16 Ref.17
Mutagenesis6171Y → E: Defective in mediating calcium response. Ref.17 Ref.26
Sequence conflict2531R → K in BAG37008. Ref.7

Secondary structure

.................................................................................................................... 659
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform BTK-A [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF06B5D1FEC257CC

FASTA65976,281
        10         20         30         40         50         60 
MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG SKKGSIDVEK 

        70         80         90        100        110        120 
ITCVETVVPE 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 PLPPEPAAAP VSTSELKKVV ALYDYMPMNA NDLQLRKGDE 

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

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

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

       430        440        450        460        470        480 
WRGQYDVAIK MIKEGSMSED 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 LASEKVYTIM YSCWHEKADE RPTFKILLSN ILDVMDEES 

« Hide

Isoform BTK-C [UniParc].

Checksum: 8C582E0CD4D6280F
Show »

FASTA69379,937

References

« Hide 'large scale' references
[1]"The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases."
Vetrie D., Vorechovsky I., Sideras P., Holland J., Davies A., Flinter F., Hammarstroem L., Kinnon C., Levinsky R.J., Bobrow M., Smith C.I.E., Bentley D.R.
Nature 361:226-233(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BTK-A).
[2]Erratum
Vetrie D., Vorechovsky I., Sideras P., Holland J., Davies A., Flinter F., Hammarstroem L., Kinnon C., Levinsky R.J., Bobrow M., Smith C.I.E., Bentley D.R.
Nature 364:362-362(1993)
[3]"Genomic organization and structure of Bruton agammaglobulinemia tyrosine kinase: localization of mutations associated with varied clinical presentations and course in X chromosome-linked agammaglobulinemia."
Ohta Y., Haire R.N., Litman R.T., Fu S.M., Nelson R.P., Kratz J., Kornfeld S.J., la Morena M., Good R.A., Litman G.W.
Proc. Natl. Acad. Sci. U.S.A. 91:9062-9066(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"The genomic structure of human BTK, the defective gene in X-linked agammaglobulinemia."
Rohrer J., Parolini O., Belmont J.W., Conley M.E.
Immunogenetics 40:319-324(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Genomic organization of the Btk gene and exon scanning for mutations in patients with X-linked agammaglobulinemia."
Hagemann T.L., Chen Y., Rosen F.S., Kwan S.-P.
Hum. Mol. Genet. 3:1743-1749(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLA SER-334; ARG-506; GLN-520; TRP-562 AND LYS-630.
[6]"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].
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BTK-A).
Tissue: Umbilical cord blood.
[8]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BTK-A).
[10]"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 OF 1-442.
[11]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12 AND 323-332, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases."
Nore B.F., Mattsson P.T., Antonsson P., Backesjo C.-M., Westlund A., Lennartsson J., Hansson H., Low P., Ronnstrand L., Smith C.I.E.
Biochim. Biophys. Acta 1645:123-132(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 219-235, PHOSPHORYLATION AT TYR-223.
[13]"An exon-skipping mutation in the btk gene of a patient with X-linked agammaglobulinemia and isolated growth hormone deficiency."
Duriez B., Duquesnoy P., Dastot F., Bougneres P., Amselem S., Goossens M.
FEBS Lett. 346:165-170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XLA-IGHD.
[14]"Tec homology (TH) adjacent to the PH domain."
Vihinen M., Nilsson L., Smith C.I.
FEBS Lett. 350:263-265(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN PH.
[15]"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: PHOSPHORYLATION AT TYR-223 AND TYR-551, MUTAGENESIS OF TYR-223, ENZYME REGULATION.
[16]"BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement."
Yang W., Desiderio S.
Proc. Natl. Acad. Sci. U.S.A. 94:604-609(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GTF2I, PHOSPHORYLATION AT TYR-223 AND TYR-551, MUTAGENESIS OF GLU-41; PRO-189; TYR-223; TRP-251; ARG-307 AND TYR-551.
[17]"Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk)."
Matsushita M., Yamadori T., Kato S., Takemoto Y., Inazawa J., Baba Y., Hashimoto S., Sekine S., Arai S., Kunikata T., Kurimoto M., Kishimoto T., Tsukada S.
Biochem. Biophys. Res. Commun. 245:337-343(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 251-TRP-TRP-252, INTERACTION WITH SH3BP5.
[18]"Phosphatidylinositol 3-kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells."
Varnai P., Rother K.I., Balla T.
J. Biol. Chem. 274:10983-10989(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN PH, SUBCELLULAR LOCATION.
[19]"Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein."
Yamadori T., Baba Y., Mastushita M., Hashimoto S., Kurosaki M., Kurosaki T., Kishimoto T., Tsukada S.
Proc. Natl. Acad. Sci. U.S.A. 96:6341-6346(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3BP5, ENZYME REGULATION.
[20]"Redistribution of Bruton's tyrosine kinase by activation of phosphatidylinositol 3-kinase and Rho-family GTPases."
Nore B.F., Vargas L., Mohamed A.J., Branden L.J., Backesjo C.M., Islam T.C., Mattsson P.T., Hultenby K., Christensson B., Smith C.I.
Eur. J. Immunol. 30:145-154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[21]"Nucleocytoplasmic shuttling of Bruton's tyrosine kinase."
Mohamed A.J., Vargas L., Nore B.F., Backesjo C.M., Christensson B., Smith C.I.
J. Biol. Chem. 275:40614-40619(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization."
Kang S.W., Wahl M.I., Chu J., Kitaura J., Kawakami Y., Kato R.M., Tabuchi R., Tarakhovsky A., Kawakami T., Turck C.W., Witte O.N., Rawlings D.J.
EMBO J. 20:5692-5702(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-180, ENZYME REGULATION.
[23]"Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling."
Rodriguez R., Matsuda M., Perisic O., Bravo J., Paul A., Jones N.P., Light Y., Swann K., Williams R.L., Katan M.
J. Biol. Chem. 276:47982-47992(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG2.
[24]"Direct inhibition of Bruton's tyrosine kinase by IBtk, a Btk-binding protein."
Liu W., Quinto I., Chen X., Palmieri C., Rabin R.L., Schwartz O.M., Nelson D.L., Scala G.
Nat. Immunol. 2:939-946(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IBTK, ENZYME REGULATION.
[25]"Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx."
Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T., Smith C.I., Mohamed A.J.
J. Biol. Chem. 277:9351-9357(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, INTERACTION WITH CAV1, SUBCELLULAR LOCATION, ENZYME REGULATION.
[26]"A phosphorylation site in Bruton's tyrosine kinase selectively regulates B cell calcium signaling efficiency by altering phospholipase C-gamma activation."
Guo S., Ferl G.Z., Deora R., Riedinger M., Yin S., Kerwin J.L., Loo J.A., Witte O.N.
Proc. Natl. Acad. Sci. U.S.A. 101:14180-14185(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-617 AND SER-623, MUTAGENESIS OF TYR-617.
[27]"Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1."
Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I.
J. Biol. Chem. 281:18201-18207(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIN1, PHOSPHORYLATION AT SER-21 AND SER-115, ENZYME REGULATION.
[28]"Bruton's tyrosine kinase is required for TLR2 and TLR4-induced TNF, but not IL-6, production."
Horwood N.J., Page T.H., McDaid J.P., Palmer C.D., Campbell J., Mahon T., Brennan F.M., Webster D., Foxwell B.M.
J. Immunol. 176:3635-3641(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE TLR PATHWAY.
[29]"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.
[30]"Suppressor of cytokine signaling 1 negatively regulates Toll-like receptor signaling by mediating Mal degradation."
Mansell A., Smith R., Doyle S.L., Gray P., Fenner J.E., Crack P.J., Nicholson S.E., Hilton D.J., O'Neill L.A., Hertzog P.J.
Nat. Immunol. 7:148-155(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TIRAP, ENZYME REGULATION.
[31]"Signaling by Toll-like receptors 8 and 9 requires Bruton's tyrosine kinase."
Doyle S.L., Jefferies C.A., Feighery C., O'Neill L.A.
J. Biol. Chem. 282:36953-36960(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TLR8 AND TLR9, ENZYME REGULATION, PHOSPHORYLATION AT TYR-223.
[32]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[33]"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.
[34]"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.
[35]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-191; TYR-361 AND SER-659, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"A novel isoform of the B cell tyrosine kinase BTK protects breast cancer cells from apoptosis."
Eifert C., Wang X., Kokabee L., Kourtidis A., Jain R., Gerdes M.J., Conklin D.S.
Genes Chromosomes Cancer 52:961-975(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORM BTK-C).
[38]"Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia."
Hyvoenen M., Saraste M.
EMBO J. 16:3396-3404(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-170 IN COMPLEX WITH ZINC.
[39]"Solution structure of the SH3 domain from Bruton's tyrosine kinase."
Hansson H., Mattsson P.T., Allard P., Haapaniemi P., Vihinen M., Smith C.I.E., Haerd T.
Biochemistry 37:2912-2924(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 212-275.
[40]"Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate."
Baraldi E., Carugo K.D., Hyvoenen M., Surdo P.L., Riley A.M., Potter B.V.L., O'Brien R., Ladbury J.E., Saraste M.
Structure 7:449-460(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-170 IN COMPLEX WITH INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE AND ZINC, DOMAIN PH.
[41]"Solution structure of the human BTK SH3 domain complexed with a proline-rich peptide from p120cbl."
Tzeng S.R., Lou Y.C., Pai M.T., Jain M.L., Cheng J.W.
J. Biomol. NMR 16:303-312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 216-273.
[42]"Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia."
Mao C., Zhou M., Uckun F.M.
J. Biol. Chem. 276:41435-41443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 397-659.
[43]"Solution structure and phosphopeptide binding of the SH2 domain from the human Bruton's tyrosine kinase."
Huang K.C., Cheng H.T., Pai M.T., Tzeng S.R., Cheng J.W.
J. Biomol. NMR 36:73-78(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 270-386.
[44]"A novel, specific Btk inhibitor antagonizes BCR and Fc[gamma]R signaling and suppresses inflammatory arthritis."
Di Paolo J.A., Huang T., Balazs M., Barbosa J., Barck K.H., Carano R.A.D., Darrow J., Davies D.R., DeForge L.E., Dennis G. Jr., Diehl L., Ferrando R.
Submitted (AUG-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 393-656 IN COMPLEX WITH INHIBITOR.
[45]"Crystal structure of PH domain of Bruton's tyrosine kinase."
Murayama K., Kato-Murayama M., Mishima C., Shirouzu M., Yokoyama S.
Submitted (MAY-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 2-170 IN COMPLEX WITH INHIBITOR AND ZINC.
[46]"Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases."
Marcotte D.J., Liu Y.T., Arduini R.M., Hession C.A., Miatkowski K., Wildes C.P., Cullen P.F., Hong V., Hopkins B.T., Mertsching E., Jenkins T.J., Romanowski M.J., Baker D.P., Silvian L.F.
Protein Sci. 19:429-439(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 382-659 IN COMPLEX WITH INHIBITOR DASATINIB.
[47]"A novel, specific BTK inhibitor antagonizes BCR and FcgR signaling and suppresses inflammatory arthritis."
Di Paolo J., Huang T., Balazs M., Barbosa J., Barck K.H., Bravo B., Carano R.A.D., Darrow J., Davies D.R., DeForge L.E., Diehl L., Ferrando R., Gallion S.L., Gianetti A.M., Gribling P., Hurez V., Hymowitz S.G., Jones R. expand/collapse author list , Kropf J.E., Lee W.P., Maciejewski P.M., Mitchell S.A., Rong H., Staker B.L., Whitney J.A., Yeh S., Young W., Yu C., Zhang J., Reif K., Currie K.S.
Submitted (SEP-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 393-659.
[48]"Insights into the conformational flexibility of Bruton's tyrosine kinase from multiple ligand complex structures."
Kuglstatter A., Wong A., Tsing S., Lee S.W., Lou Y., Villasenor A.G., Bradshaw J.M., Shaw D., Barnett J.W., Browner M.F.
Protein Sci. 20:428-436(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 387-659 IN COMPLEX WITH INHIBITOR.
[49]"BTKbase, mutation database for X-linked agammaglobulinemia (XLA)."
Vihinen M., Iwata T., Kinnon C., Kwan S.-P., Ochs H.D., Vorechovsky I., Smith C.I.E.
Nucleic Acids Res. 24:160-165(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS XLA.
[50]"BTKbase, mutation database for X-linked agammaglobulinemia (XLA)."
Vihinen M., Belohradsky B.H., Haire R.N., Holinski-Feder E., Kwan S.-P., Lappalainen I., Lehvaeslaiho H., Lester T., Meindl A., Ochs H.D., Ollila J., Vorechovsky I., Weiss M., Smith C.I.E.
Nucleic Acids Res. 25:166-171(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS XLA.
[51]"Mutation detection in the X-linked agammaglobulinemia gene, BTK, using single strand conformation polymorphism analysis."
Bradley L.A.D., Sweatman A.K., Lovering R.C., Jones A.M., Morgan G., Levinsky R.J., Kinnon C.
Hum. Mol. Genet. 3:79-83(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA TRP-288; GLY-307; ASP-607 AND SER-VAL-PHE-SER-SER-THR-ARG-103 INS.
[52]"Mutation analysis of the Bruton's tyrosine kinase gene in X-linked agammaglobulinemia: identification of a mutation which affects the same codon as is altered in immunodeficient xid mice."
de Weers M., Mensink R.G.J., Kraakman M.E.M., Schuurman R.K.B., Hendriks R.W.
Hum. Mol. Genet. 3:161-166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA HIS-28 AND TRP-288.
[53]"Screening of genomic DNA to identify mutations in the gene for Bruton's tyrosine kinase."
Conley M.E., Fitch-Hilgenberg M.E., Cleveland J.L., Parolini O., Rohrer J.
Hum. Mol. Genet. 3:1751-1756(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA ASP-113; CYS-361; GLN-520; PRO-542; TRP-562; LYS-630 AND PRO-652.
[54]"Unique mutations of Bruton's tyrosine kinase in fourteen unrelated X-linked agammaglobulinemia families."
Zhu Q., Zhang M., Winkelstein J., Chen S.-H., Ochs H.D.
Hum. Mol. Genet. 3:1899-1900(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA HIS-28; PRO-33; PRO-408; GLY-589; ASP-613 AND 260-GLN--GLU-280 DEL.
[55]"Structural basis for chromosome X-linked agammaglobulinemia: a tyrosine kinase disease."
Vihinen M., Vetrie D., Maniar H.S., Ochs H.D., Zhu Q., Vorechovsky I., Webster A.D.B., Notarangelo L.D., Nilsson L., Sowadski J.M., Smith C.I.E.
Proc. Natl. Acad. Sci. U.S.A. 91:12803-12807(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA GLU-430; GLN-520; GLN-525; PRO-562; VAL-582; GLY-589; GLU-594 AND ASP-613.
[56]"Structural basis for pleckstrin homology domain mutations in X-linked agammaglobulinemia."
Vihinen M., Zvelebil J.J.M., Zhu Q., Brooimans R.A., Ochs H.D., Zegers B.J.M., Nilsson L., Waterfield M.D., Smith C.I.E.
Biochemistry 34:1475-1481(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLA PHE-64, CHARACTERIZATION OF OTHER XLA VARIANTS.
[57]"DNA-based mutation analysis of Bruton's tyrosine kinase gene in patients with X-linked agammaglobulinaemia."
Vorechovsky I., Vihinen M., de Saint Basile G., Honsova S., Hammarstroem L., Mueller S., Nilsson L., Fischer A., Smith C.I.E.
Hum. Mol. Genet. 4:51-58(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA SER-25; TRP-288; MET-370; VAL-509; PRO-525; LYS-526; TRP-562; VAL-582 AND ARG-594.
[58]"Identification of Btk mutations in 20 unrelated patients with X-linked agammaglobulinaemia (XLA)."
Jin H., Webster A.D.B., Vihinen M., Sideras P., Vorechovsky I., Hammarstroem L., Bernatowska-Matuszkiewicz E., Smith C.I.E., Bobrow M., Vetrie D.
Hum. Mol. Genet. 4:693-700(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA LYS-567; LEU-587 AND HIS-641.
[59]"Mutation analysis in Bruton's tyrosine kinase, the X-linked agammaglobulinaemia gene, including identification of an insertional hotspot."
Gaspar H.B., Bradley L.A.D., Katz F., Lovering R.C., Roifman C.M., Morgan G., Levinsky R.J., Kinnon C.
Hum. Mol. Genet. 4:755-757(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA PRO-33; GLY-302 DEL; GLN-520 AND CYS-641.
[60]"Improved oligonucleotide primer set for molecular diagnosis of X-linked agammaglobulinaemia: predominance of amino acid substitutions in the catalytic domain of Bruton's tyrosine kinase."
Vorechovsky I., Luo L., de Saint Basile G., Hammarstroem L., Webster A.D.B., Smith C.I.E.
Hum. Mol. Genet. 4:2403-2405(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA ASN-429 AND ARG-477.
[61]"Characterization of germline mutations of the gene encoding Bruton's tyrosine kinase in families with X-linked agammaglobulinemia."
Hagemann T.L., Rosen F.S., Kwan S.-P.
Hum. Mutat. 5:296-302(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA GLU-302 AND ASP-476.
[62]"A new point mutation involving a highly conserved leucine in the Btk SH2 domain in a family with X linked agammaglobulinaemia."
Ohashi Y., Tsuchiya S., Konno T.
J. Med. Genet. 32:77-79(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLA PHE-358.
[63]"Detection of a novel mutation in the SRC homology domain 2 (SH2) of Bruton's tyrosine kinase and direct female carrier evaluation in a family with X-linked agammaglobulinemia."
Schuster V., Seidenspinner S., Kreth H.W.
Am. J. Med. Genet. 63:318-322(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLA PRO-295.
[64]"Identification of Bruton's tyrosine kinase (Btk) gene mutations and characterization of the derived proteins in 35 X-linked agammaglobulinemia families: a nationwide study of Btk deficiency in Japan."
Hashimoto S., Tsukada S., Matsushita M., Miyawaki T., Niida Y., Yachie A., Kobayashi S., Iwata T., Hayakawa H., Matsuoka H., Tsuge I., Yamadori T., Kunikata T., Arai S., Yoshizaki K., Taniguchi N., Kishimoto T.
Blood 88:561-573(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA ARG-12; PRO-28; GLU-302; TRP-502; HIS-521; TYR-633 AND SER-644.
[65]"Mutations of the Btk gene in 12 unrelated families with X-linked agammaglobulinemia in Japan."
Kobayashi S., Iwata T., Saito M., Iwasaki R., Matsumoto H., Naritaka S., Kono Y., Hayashi Y.
Hum. Genet. 97:424-430(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA TRP-288; LYS-544 AND PRO-592.
[66]"Missense mutations affecting a conserved cysteine pair in the TH domain of Btk."
Vihinen M., Nore B., Mattsson P.T., Backesj C.-M., Nars M., Koutaniemi S., Watanabe C., Lester T., Jones A.M., Ochs H.D., Smith C.I.E.
FEBS Lett. 413:205-210(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA SER-154 AND ARG-155.
[67]"Molecular and structural characterization of five novel mutations in the Bruton's tyrosine kinase gene from patients with X-linked agammaglobulinemia."
Saha B.K., Curtis S.K., Vogler L.B., Vihinen M.
Mol. Med. 3:477-485(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA.
[68]"Mutations in btk in patients with presumed X-linked agammaglobulinemia."
Conley M.E., Mathias D., Treadaway J., Minegishi Y., Rohrer J.
Am. J. Hum. Genet. 62:1034-1043(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA GLN-288; THR-307; ARG-430; ASP-445; GLY-525; PHE-535; LEU-563 AND PRO-622.
[69]"Mutation screening of the BTK gene in 56 families with X-linked agammaglobulinemia (XLA): 47 unique mutations without correlation to clinical course."
Holinski-Feder E., Weiss M., Brandau O., Jedele K.B., Nore B., Baeckesjoe C.-M., Vihinen M., Hubbard S.R., Belohradsky B.H., Smith C.I.E., Meindl A.
Pediatrics 101:276-284(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA GLU-19; HIS-28; ASN-61; PRO-117; HIS-127; ARG-155; PRO-295; PHE-369; GLY-372; ARG-414; TYR-506; GLY-521; GLN-525; SER-559; TRP-562; GLU-594; THR-619; GLY-626 AND HIS-641.
[70]"Mutations of the human BTK gene coding for Bruton tyrosine kinase in X-linked agammaglobulinemia."
Vihinen M., Kwan S.-P., Lester T., Ochs H.D., Resnick I., Vaeliaho J., Conley M.E., Smith C.I.E.
Hum. Mutat. 13:280-285(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA.
[71]"Twin carriers of X-linked agammaglobulinemia (XLA) due to germline mutation in the Btk gene."
Curtis S.K., Hebert M.D., Saha B.K.
Am. J. Med. Genet. 90:229-232(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLA PRO-562.
[72]"Identification of nine novel mutations in the Bruton's tyrosine kinase gene in X-linked agammaglobulinaemia patients."
Orlandi P., Ritis K., Moschese V., Angelini F., Arvanitidis K., Speletas M., Sideras P., Plebani A., Rossi P.
Hum. Mutat. 15:117-117(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLA SER-39; PRO-512; GLN-512; GLY-544; TYR-578 AND LYS-589.
[73]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-82 AND LYS-190.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58957 mRNA. Translation: CAA41728.1.
U10087 expand/collapse EMBL AC list , U10084, U10085, U10086 Genomic DNA. Translation: AAB60639.1.
L31572 expand/collapse EMBL AC list , L31557, L31558, L31559, L31561, L31563, L31564, L31565, L31566, L31567, L31568, L31569, L31570, L31571 Genomic DNA. Translation: AAA61479.1.
U13433 expand/collapse EMBL AC list , U13410, U13412, U13413, U13414, U13415, U13416, U13417, U13422, U13423, U13424, U13425, U13427, U13428, U13429, U13430, U13431, U13432 Genomic DNA. Translation: AAC51347.1.
U78027 Genomic DNA. Translation: AAB64205.1.
AK314382 mRNA. Translation: BAG37008.1.
AL035422 Genomic DNA. Translation: CAB55876.1.
BC109079 mRNA. Translation: AAI09080.1.
BC109080 mRNA. Translation: AAI09081.1.
PIRA45184. I37212.
RefSeqNP_000052.1. NM_000061.2.
NP_001274273.1. NM_001287344.1.
NP_001274274.1. NM_001287345.1.
UniGeneHs.159494.
Hs.733206.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWWNMR-A212-275[»]
1AWXNMR-A212-275[»]
1B55X-ray2.40A/B2-170[»]
1BTKX-ray1.60A/B2-170[»]
1BWNX-ray2.10A/B2-170[»]
1K2PX-ray2.10A/B397-659[»]
1QLYNMR-A216-273[»]
2GE9NMR-A270-386[»]
2Z0PX-ray2.58A/B/C/D2-170[»]
3GENX-ray1.60A382-659[»]
3K54X-ray1.94A382-659[»]
3OCSX-ray1.80A393-657[»]
3OCTX-ray1.95A393-656[»]
3P08X-ray2.30A/B393-659[»]
3PIXX-ray1.85A387-659[»]
3PIYX-ray2.55A387-659[»]
3PIZX-ray2.21A387-659[»]
3PJ1X-ray2.00A387-659[»]
3PJ2X-ray1.75A387-659[»]
3PJ3X-ray1.85A387-659[»]
ProteinModelPortalQ06187.
SMRQ06187. Positions 2-170, 216-387, 395-657.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107160. 69 interactions.
DIPDIP-34071N.
IntActQ06187. 41 interactions.
MINTMINT-110243.
STRING9606.ENSP00000308176.

Chemistry

BindingDBQ06187.
ChEMBLCHEMBL5251.
GuidetoPHARMACOLOGY1948.

PTM databases

PhosphoSiteQ06187.

Polymorphism databases

DMDM547759.

Proteomic databases

PaxDbQ06187.
PRIDEQ06187.

Protocols and materials databases

DNASU695.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308731; ENSP00000308176; ENSG00000010671.
ENST00000593575; ENSP00000469726; ENSG00000268897.
GeneID695.
KEGGhsa:695.
UCSCuc004ehg.2. human. [Q06187-1]

Organism-specific databases

CTD695.
GeneCardsGC0XM100604.
HGNCHGNC:1133. BTK.
HPACAB016689.
HPA001198.
HPA002028.
MIM300300. gene.
300755. phenotype.
307200. phenotype.
neXtProtNX_Q06187.
Orphanet632. Short stature due to isolated growth hormone deficiency with X-linked hypogammaglobulinemia.
47. X-linked agammaglobulinemia.
PharmGKBPA25454.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233859.
HOVERGENHBG008761.
InParanoidQ06187.
KOK07370.
OMASCRHYNI.
PhylomeDBQ06187.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_6900. Immune System.
SignaLinkQ06187.

Gene expression databases

ArrayExpressQ06187.
BgeeQ06187.
CleanExHS_BTK.
GenevestigatorQ06187.

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

EvolutionaryTraceQ06187.
GeneWikiBruton%27s_tyrosine_kinase.
GenomeRNAi695.
NextBio2850.
PROQ06187.
SOURCESearch...

Entry information

Entry nameBTK_HUMAN
AccessionPrimary (citable) accession number: Q06187
Secondary accession number(s): B2RAW1, Q32ML5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM