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Protein

Tyrosine-protein kinase BTK

Gene

BTK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by phosphorylation. In primary B lymphocytes, is almost always non-phosphorylated and is thus catalytically inactive. Stimulation of TLR8 and TLR9 causes BTK activation. As a negative feedback mechanism to fine-tune BCR signaling, activated PRKCB down-modulates BTK function via direct phosphorylation of BTK at Ser-180, resulting in translocation of BTK back to the cytoplasmic fraction. PIN1, SH3BP5, and IBTK were also identified as BTK activity inhibitors. Interaction with CAV1 leads to dramatic down-regulation of the kinase activity of BTK. LFM-13A is a specific inhibitor of BTK. Dasatinib, a cancer drug acting as a tyrosine kinase inhibitor, also blocks BTK activity.8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei26Inositol-(1,3,4,5)-tetrakisphosphate1 Publication1
Binding sitei28Inositol-(1,3,4,5)-tetrakisphosphate1 Publication1
Binding sitei39Inositol-(1,3,4,5)-tetrakisphosphate1 Publication1
Binding sitei53Inositol-(1,3,4,5)-tetrakisphosphate; via carbonyl oxygen1 Publication1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi143Zinc3 Publications1
Metal bindingi154Zinc3 Publications1
Metal bindingi155Zinc3 Publications1
Metal bindingi165Zinc3 Publications1
Binding sitei430ATPPROSITE-ProRule annotation1
Binding sitei445Inhibitor3 Publications1
Binding sitei461Inhibitor3 Publications1
Binding sitei477Inhibitor3 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei521Proton acceptorPROSITE-ProRule annotation1
Binding sitei538Inhibitor3 Publications1
Binding sitei539Inhibitor; via amide nitrogen3 Publications1
Binding sitei542Inhibitor; via carbonyl oxygen3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri135 – 171Btk-typePROSITE-ProRule annotationAdd BLAST37
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi408 – 416ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: HGNC
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • protein tyrosine kinase activity Source: Reactome

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Apoptosis, Immunity, Innate immunity, Transcription, Transcription regulation
LigandATP-binding, Lipid-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1236974 ER-Phagosome pathway
R-HSA-166058 MyD88:MAL(TIRAP) cascade initiated on plasma membrane
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2424491 DAP12 signaling
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-5602498 MyD88 deficiency (TLR2/4)
R-HSA-5603041 IRAK4 deficiency (TLR2/4)
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q06187

SIGNOR Signaling Network Open Resource

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SIGNORi
Q06187

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tyrosine-protein kinase BTK (EC:2.7.10.2)
Alternative name(s):
Agammaglobulinemia tyrosine kinase
Short name:
ATK
B-cell progenitor kinase
Short name:
BPK
Bruton tyrosine kinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BTK
Synonyms:AGMX1, ATK, BPK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000010671.15

Human Gene Nomenclature Database

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HGNCi
HGNC:1133 BTK

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300300 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q06187

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

X-linked agammaglobulinemia (XLA)26 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionHumoral 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.
See also OMIM:300755
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00621611L → P in XLA. 1
Natural variantiVAR_00621712K → R in XLA. 1 Publication1
Natural variantiVAR_00621814S → F in XLA. 1
Natural variantiVAR_00829119K → E in XLA. 1 Publication1
Natural variantiVAR_00621925F → S in XLA. 1 Publication1
Natural variantiVAR_00829227K → R in XLA. 1
Natural variantiVAR_00829328R → C in XLA; no effect on phosphorylation of GTF2I. 1
Natural variantiVAR_00622028R → H in XLA; moderate. 3 PublicationsCorresponds to variant dbSNP:rs128620185EnsemblClinVar.1
Natural variantiVAR_00622128R → P in XLA. 1 Publication1
Natural variantiVAR_00622233T → P in XLA; severe. 2 PublicationsCorresponds to variant dbSNP:rs128620189EnsemblClinVar.1
Natural variantiVAR_00896039Y → S in XLA. 1 Publication1
Natural variantiVAR_00829440Y → C in XLA. 1
Natural variantiVAR_00829540Y → N in XLA. 1
Natural variantiVAR_00829661I → N in XLA. 1 Publication1
Natural variantiVAR_00829764V → D in XLA. 1
Natural variantiVAR_00622364V → F in XLA. 1 Publication1
Natural variantiVAR_006224103Q → QSVFSSTR in XLA. 1
Natural variantiVAR_006225113V → D in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621190EnsemblClinVar.1
Natural variantiVAR_008298115S → F in XLA. 1
Natural variantiVAR_008299117T → P in XLA. 1 Publication1
Natural variantiVAR_008300127Q → H in XLA. 1 Publication1
Natural variantiVAR_008301154C → S in XLA. 1 Publication1
Natural variantiVAR_008302155C → G in XLA. 1
Natural variantiVAR_008303155C → R in XLA. 2 Publications1
Natural variantiVAR_008304184T → P in XLA. 1
Natural variantiVAR_006226260 – 280Missing in XLA; severe. 1 PublicationAdd BLAST21
Natural variantiVAR_008305288R → Q in XLA. 1 Publication1
Natural variantiVAR_006227288R → W in XLA. 4 PublicationsCorresponds to variant dbSNP:rs128621194EnsemblClinVar.1
Natural variantiVAR_006228295L → P in XLA. 2 Publications1
Natural variantiVAR_006230302G → E in XLA. 2 Publications1
Natural variantiVAR_008306302G → R in XLA. 1
Natural variantiVAR_006229302Missing in XLA. 1 Publication1
Natural variantiVAR_006231307R → G in XLA; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs128621195EnsemblClinVar.1
Natural variantiVAR_008307307R → T in XLA. 1 Publication1
Natural variantiVAR_008308308D → E in XLA. 1
Natural variantiVAR_008309319V → A in XLA; moderate. 1
Natural variantiVAR_006232334Y → S in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621196EnsemblClinVar.1
Natural variantiVAR_006233358L → F in XLA. 1 Publication1
Natural variantiVAR_006234361Y → C in XLA; mild. 1 PublicationCorresponds to variant dbSNP:rs28935478EnsemblClinVar.1
Natural variantiVAR_006235362H → Q in XLA. 1
Natural variantiVAR_006236364H → P in XLA. 1
Natural variantiVAR_006237365N → Y in XLA. 1
Natural variantiVAR_008310366S → F in XLA. 1
Natural variantiVAR_008311369L → F in XLA. 1 Publication1
Natural variantiVAR_006238370I → M in XLA. 1 Publication1
Natural variantiVAR_008312372R → G in XLA. 1 Publication1
Natural variantiVAR_006239408L → P in XLA; moderate. 1 PublicationCorresponds to variant dbSNP:rs128621198EnsemblClinVar.1
Natural variantiVAR_008313414G → R in XLA. 1 Publication1
Natural variantiVAR_006240418Y → H in XLA. Corresponds to variant dbSNP:rs144079566Ensembl.1
Natural variantiVAR_006241429I → N in XLA. 1 Publication1
Natural variantiVAR_006242430K → E in XLA; loss of phosphorylation of GTF2I. 1 PublicationCorresponds to variant dbSNP:rs128620184EnsemblClinVar.1
Natural variantiVAR_008314430K → R in XLA. 1 Publication1
Natural variantiVAR_008315445E → D in XLA. 1 Publication1
Natural variantiVAR_008316462G → D in XLA. 1
Natural variantiVAR_008317462G → V in XLA. 1
Natural variantiVAR_006243476Y → D in XLA. 1 Publication1
Natural variantiVAR_006244477M → R in XLA. 1 Publication1
Natural variantiVAR_006245502C → F in XLA. 1
Natural variantiVAR_006246502C → W in XLA. 1 PublicationCorresponds to variant dbSNP:rs41310709Ensembl.1
Natural variantiVAR_006247506C → R in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621200EnsemblClinVar.1
Natural variantiVAR_006248506C → Y in XLA. 1 Publication1
Natural variantiVAR_008318508A → D in XLA. 1
Natural variantiVAR_008319509M → I in XLA. 1
Natural variantiVAR_006249509M → V in XLA. 1 Publication1
Natural variantiVAR_008961512L → P in XLA. 1 Publication1
Natural variantiVAR_008962512L → Q in XLA. 1 Publication1
Natural variantiVAR_008320518L → R in XLA. 1
Natural variantiVAR_006251520R → Q in XLA; severe; prevents activation due to absence of contact between the catalytic loop and the regulatory phosphorylated residue. 4 PublicationsCorresponds to variant dbSNP:rs128621202EnsemblClinVar.1
Natural variantiVAR_008321521D → G in XLA. 1 Publication1
Natural variantiVAR_006252521D → H in XLA; severe. 1 Publication1
Natural variantiVAR_006253521D → N in XLA; severe. 1
Natural variantiVAR_008322523A → E in XLA. 1
Natural variantiVAR_008323525R → G in XLA. 1 Publication1
Natural variantiVAR_006254525R → P in XLA. 1 Publication1
Natural variantiVAR_006255525R → Q in XLA; severe; disturbs ATP-binding. 2 PublicationsCorresponds to variant dbSNP:rs128620183EnsemblClinVar.1
Natural variantiVAR_006256526N → K in XLA. 1 Publication1
Natural variantiVAR_008324535V → F in XLA. 1 Publication1
Natural variantiVAR_006257542L → P in XLA; growth hormone deficiency. 1 PublicationCorresponds to variant dbSNP:rs128621203EnsemblClinVar.1
Natural variantiVAR_008963544R → G in XLA. 1 Publication1
Natural variantiVAR_006258544R → K in XLA. 1 Publication1
Natural variantiVAR_008325559F → S in XLA. 1 Publication1
Natural variantiVAR_006259562R → P in XLA. 2 PublicationsCorresponds to variant dbSNP:rs104894770EnsemblClinVar.1
Natural variantiVAR_006260562R → W in XLA. 4 PublicationsCorresponds to variant dbSNP:rs128621204EnsemblClinVar.1
Natural variantiVAR_008326563W → L in XLA. 1 Publication1
Natural variantiVAR_006261567E → K in XLA; severe. 1 Publication1
Natural variantiVAR_008964578S → Y in XLA. 1 Publication1
Natural variantiVAR_006262581W → R in XLA. Corresponds to variant dbSNP:rs128621205EnsemblClinVar.1
Natural variantiVAR_006263582A → V in XLA. 2 Publications1
Natural variantiVAR_008327583F → S in XLA. 1
Natural variantiVAR_006264587M → L in XLA; mild. 1 Publication1
Natural variantiVAR_008328589E → D in XLA. 1
Natural variantiVAR_006265589E → G in XLA; moderate; interferes with substrate binding. 2 PublicationsCorresponds to variant dbSNP:rs128621206EnsemblClinVar.1
Natural variantiVAR_008965589E → K in XLA. 1 Publication1
Natural variantiVAR_006267592S → P in XLA. 1 Publication1
Natural variantiVAR_006268594G → E in XLA; mild; interferes with substrate binding. 2 Publications1
Natural variantiVAR_006269594G → R in XLA. 1 Publication1
Natural variantiVAR_006270598Y → C in XLA. 1
Natural variantiVAR_006271607A → D in XLA; mild. 1 PublicationCorresponds to variant dbSNP:rs128621208EnsemblClinVar.1
Natural variantiVAR_006272613G → D in XLA; mild; interferes with substrate binding and/or domain interactions. 2 PublicationsCorresponds to variant dbSNP:rs128621209EnsemblClinVar.1
Natural variantiVAR_008330619P → A in XLA. 1
Natural variantiVAR_006273619P → S in XLA. 1
Natural variantiVAR_008331619P → T in XLA. 1 Publication1
Natural variantiVAR_008332622A → P in XLA. 1 Publication1
Natural variantiVAR_008333626V → G in XLA. 1 Publication1
Natural variantiVAR_006275630M → K in XLA. 2 PublicationsCorresponds to variant dbSNP:rs128621210EnsemblClinVar.1
Natural variantiVAR_008334630M → T in XLA. 1
Natural variantiVAR_006276633C → Y in XLA. 1 Publication1
Natural variantiVAR_006277641R → C in XLA. 1 Publication1
Natural variantiVAR_006278641R → H in XLA; severe. 2 Publications1
Natural variantiVAR_008335644F → L in XLA. 1
Natural variantiVAR_006279644F → S in XLA. 1 Publication1
Natural variantiVAR_006280647L → P in XLA. 1
Natural variantiVAR_006281652L → P in XLA. 1 PublicationCorresponds to variant dbSNP:rs128622212EnsemblClinVar.1
X-linked hypogammaglobulinemia and isolated growth hormone deficiency (XLA-IGHD)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionIn rare cases XLA is inherited together with isolated growth hormone deficiency (IGHD).
See also OMIM:307200

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi41E → K: No effect on phosphorylation of GTF2I. 1 Publication1
Mutagenesisi189P → A: No effect on phosphorylation of GTF2I. 1 Publication1
Mutagenesisi223Y → F: Loss of phosphorylation of GTF2I. 2 Publications1
Mutagenesisi251 – 252WW → LL: Large decrease in binding by SH3BP5. 1 Publication2
Mutagenesisi251W → L: No effect on phosphorylation of GTF2I. 1 Publication1
Mutagenesisi307R → K: Loss of phosphorylation of GTF2I. 1 Publication1
Mutagenesisi551Y → F: Loss of phosphorylation of GTF2I. 1 Publication1
Mutagenesisi617Y → E: Defective in mediating calcium response. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
695

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
BTK

MalaCards human disease database

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MalaCardsi
BTK
MIMi300755 phenotype
307200 phenotype

Open Targets

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OpenTargetsi
ENSG00000010671

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
632 Short stature due to isolated growth hormone deficiency with X-linked hypogammaglobulinemia
47 X-linked agammaglobulinemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25454

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5251

Drug and drug target database

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DrugBanki
DB09053 Ibrutinib
DB05204 XL418

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1948

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
BTK

Domain mapping of disease mutations (DMDM)

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DMDMi
547759

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000880652 – 659Tyrosine-protein kinase BTKAdd BLAST658

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei21Phosphoserine1 Publication1
Modified residuei40PhosphotyrosineBy similarity1
Modified residuei55PhosphoserineCombined sources1
Modified residuei115Phosphoserine1 Publication1
Modified residuei180Phosphoserine; by PKC/PRKCB1 Publication1
Modified residuei191PhosphothreonineCombined sources1
Modified residuei223Phosphotyrosine; by autocatalysisCombined sources4 Publications1
Modified residuei344PhosphotyrosineBy similarity1
Modified residuei361PhosphotyrosineCombined sources1
Modified residuei551Phosphotyrosine; by LYN and SYK2 Publications1
Modified residuei604PhosphoserineCombined sources1
Modified residuei617Phosphotyrosine1 Publication1
Modified residuei623Phosphoserine1 Publication1
Modified residuei659PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Following B-cell receptor (BCR) engagement, translocates to the plasma membrane where it gets phosphorylated at Tyr-551 by LYN and SYK. Phosphorylation at Tyr-551 is followed by autophosphorylation of Tyr-223 which may create a docking site for a SH2 containing protein. Phosphorylation at Ser-180 by PRKCB, leads in translocation of BTK back to the cytoplasmic fraction. Phosphorylation at Ser-21 and Ser-115 creates a binding site for PIN1 at these Ser-Pro motifs, and promotes it's recruitment.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q06187

MaxQB - The MaxQuant DataBase

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MaxQBi
Q06187

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q06187

PeptideAtlas

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PeptideAtlasi
Q06187

PRoteomics IDEntifications database

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PRIDEi
Q06187

ProteomicsDB human proteome resource

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ProteomicsDBi
58419

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q06187

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q06187

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Predominantly expressed in B-lymphocytes.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000010671 Expressed in 163 organ(s), highest expression level in small intestine Peyer's patch

CleanEx database of gene expression profiles

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CleanExi
HS_BTK

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q06187 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q06187 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB016689
HPA001198
HPA002028

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 TLR9.14 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107160, 80 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q06187

Database of interacting proteins

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DIPi
DIP-34071N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q06187

Protein interaction database and analysis system

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IntActi
Q06187, 50 interactors

Molecular INTeraction database

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MINTi
Q06187

STRING: functional protein association networks

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STRINGi
9606.ENSP00000308176

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q06187

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1659
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q06187

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q06187

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q06187

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini3 – 133PHPROSITE-ProRule annotationAdd BLAST131
Domaini214 – 274SH3PROSITE-ProRule annotationAdd BLAST61
Domaini281 – 377SH2PROSITE-ProRule annotationAdd BLAST97
Domaini402 – 655Protein kinasePROSITE-ProRule annotationAdd BLAST254

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni12 – 24Inositol-(1,3,4,5)-tetrakisphosphate 1-bindingAdd BLAST13
Regioni474 – 479Inhibitor-binding6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi581 – 588CAV1-binding8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PH domain mediates the binding to inositol polyphosphate and phosphoinositides, leading to its targeting to the plasma membrane. It is extended in the BTK kinase family by a region designated the TH (Tec homology) domain, which consists of about 80 residues preceding the SH3 domain.4 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. TEC subfamily.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri135 – 171Btk-typePROSITE-ProRule annotationAdd BLAST37

Keywords - Domaini

SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158469

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233859

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008761

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q06187

KEGG Orthology (KO)

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KOi
K07370

Identification of Orthologs from Complete Genome Data

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OMAi
KYGKWQG

Database of Orthologous Groups

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OrthoDBi
EOG091G0D46

Database for complete collections of gene phylogenies

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PhylomeDBi
Q06187

TreeFam database of animal gene trees

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TreeFami
TF351634

Family and domain databases

Conserved Domains Database

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CDDi
cd11906 SH3_BTK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.29.30, 1 hit
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR035574 BTK_SH3
IPR011009 Kinase-like_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001562 Znf_Btk_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00779 BTK, 1 hit
PF00169 PH, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00402 TECBTKDOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00107 BTK, 1 hit
SM00233 PH, 1 hit
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit
PS50002 SH3, 1 hit
PS51113 ZF_BTK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform BTK-A (identifier: Q06187-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MAAVILESIF LKRSQQKKKT SPLNFKKRLF LLTVHKLSYY EYDFERGRRG
60 70 80 90 100
SKKGSIDVEK ITCVETVVPE KNPPPERQIP RRGEESSEME QISIIERFPY
110 120 130 140 150
PFQVVYDEGP LYVFSPTEEL RKRWIHQLKN VIRYNSDLVQ KYHPCFWIDG
160 170 180 190 200
QYLCCSQTAK NAMGCQILEN RNGSLKPGSS HRKTKKPLPP TPEEDQILKK
210 220 230 240 250
PLPPEPAAAP VSTSELKKVV ALYDYMPMNA NDLQLRKGDE YFILEESNLP
260 270 280 290 300
WWRARDKNGQ EGYIPSNYVT EAEDSIEMYE WYSKHMTRSQ AEQLLKQEGK
310 320 330 340 350
EGGFIVRDSS KAGKYTVSVF AKSTGDPQGV IRHYVVCSTP QSQYYLAEKH
360 370 380 390 400
LFSTIPELIN YHQHNSAGLI SRLKYPVSQQ NKNAPSTAGL GYGSWEIDPK
410 420 430 440 450
DLTFLKELGT GQFGVVKYGK WRGQYDVAIK MIKEGSMSED EFIEEAKVMM
460 470 480 490 500
NLSHEKLVQL YGVCTKQRPI FIITEYMANG CLLNYLREMR HRFQTQQLLE
510 520 530 540 550
MCKDVCEAME YLESKQFLHR DLAARNCLVN DQGVVKVSDF GLSRYVLDDE
560 570 580 590 600
YTSSVGSKFP VRWSPPEVLM YSKFSSKSDI WAFGVLMWEI YSLGKMPYER
610 620 630 640 650
FTNSETAEHI AQGLRLYRPH LASEKVYTIM YSCWHEKADE RPTFKILLSN

ILDVMDEES
Length:659
Mass (Da):76,281
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF06B5D1FEC257CC
GO
Isoform BTK-C (identifier: Q06187-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:693
Mass (Da):79,937
Checksum:i8C582E0CD4D6280F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JY90Q5JY90_HUMAN
Tyrosine-protein kinase
BTK hCG_20400
483Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
U3NG26U3NG26_HUMAN
Tyrosine-protein kinase
BTK
568Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti253R → K in BAG37008 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00621611L → P in XLA. 1
Natural variantiVAR_00621712K → R in XLA. 1 Publication1
Natural variantiVAR_00621814S → F in XLA. 1
Natural variantiVAR_00829119K → E in XLA. 1 Publication1
Natural variantiVAR_00621925F → S in XLA. 1 Publication1
Natural variantiVAR_00829227K → R in XLA. 1
Natural variantiVAR_00829328R → C in XLA; no effect on phosphorylation of GTF2I. 1
Natural variantiVAR_00622028R → H in XLA; moderate. 3 PublicationsCorresponds to variant dbSNP:rs128620185EnsemblClinVar.1
Natural variantiVAR_00622128R → P in XLA. 1 Publication1
Natural variantiVAR_00622233T → P in XLA; severe. 2 PublicationsCorresponds to variant dbSNP:rs128620189EnsemblClinVar.1
Natural variantiVAR_00896039Y → S in XLA. 1 Publication1
Natural variantiVAR_00829440Y → C in XLA. 1
Natural variantiVAR_00829540Y → N in XLA. 1
Natural variantiVAR_00829661I → N in XLA. 1 Publication1
Natural variantiVAR_00829764V → D in XLA. 1
Natural variantiVAR_00622364V → F in XLA. 1 Publication1
Natural variantiVAR_04167682R → K1 PublicationCorresponds to variant dbSNP:rs56035945Ensembl.1
Natural variantiVAR_006224103Q → QSVFSSTR in XLA. 1
Natural variantiVAR_006225113V → D in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621190EnsemblClinVar.1
Natural variantiVAR_008298115S → F in XLA. 1
Natural variantiVAR_008299117T → P in XLA. 1 Publication1
Natural variantiVAR_008300127Q → H in XLA. 1 Publication1
Natural variantiVAR_008301154C → S in XLA. 1 Publication1
Natural variantiVAR_008302155C → G in XLA. 1
Natural variantiVAR_008303155C → R in XLA. 2 Publications1
Natural variantiVAR_008304184T → P in XLA. 1
Natural variantiVAR_041677190P → K in a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_006226260 – 280Missing in XLA; severe. 1 PublicationAdd BLAST21
Natural variantiVAR_008305288R → Q in XLA. 1 Publication1
Natural variantiVAR_006227288R → W in XLA. 4 PublicationsCorresponds to variant dbSNP:rs128621194EnsemblClinVar.1
Natural variantiVAR_006228295L → P in XLA. 2 Publications1
Natural variantiVAR_006230302G → E in XLA. 2 Publications1
Natural variantiVAR_008306302G → R in XLA. 1
Natural variantiVAR_006229302Missing in XLA. 1 Publication1
Natural variantiVAR_006231307R → G in XLA; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs128621195EnsemblClinVar.1
Natural variantiVAR_008307307R → T in XLA. 1 Publication1
Natural variantiVAR_008308308D → E in XLA. 1
Natural variantiVAR_008309319V → A in XLA; moderate. 1
Natural variantiVAR_006232334Y → S in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621196EnsemblClinVar.1
Natural variantiVAR_006233358L → F in XLA. 1 Publication1
Natural variantiVAR_006234361Y → C in XLA; mild. 1 PublicationCorresponds to variant dbSNP:rs28935478EnsemblClinVar.1
Natural variantiVAR_006235362H → Q in XLA. 1
Natural variantiVAR_006236364H → P in XLA. 1
Natural variantiVAR_006237365N → Y in XLA. 1
Natural variantiVAR_008310366S → F in XLA. 1
Natural variantiVAR_008311369L → F in XLA. 1 Publication1
Natural variantiVAR_006238370I → M in XLA. 1 Publication1
Natural variantiVAR_008312372R → G in XLA. 1 Publication1
Natural variantiVAR_006239408L → P in XLA; moderate. 1 PublicationCorresponds to variant dbSNP:rs128621198EnsemblClinVar.1
Natural variantiVAR_008313414G → R in XLA. 1 Publication1
Natural variantiVAR_006240418Y → H in XLA. Corresponds to variant dbSNP:rs144079566Ensembl.1
Natural variantiVAR_006241429I → N in XLA. 1 Publication1
Natural variantiVAR_006242430K → E in XLA; loss of phosphorylation of GTF2I. 1 PublicationCorresponds to variant dbSNP:rs128620184EnsemblClinVar.1
Natural variantiVAR_008314430K → R in XLA. 1 Publication1
Natural variantiVAR_008315445E → D in XLA. 1 Publication1
Natural variantiVAR_008316462G → D in XLA. 1
Natural variantiVAR_008317462G → V in XLA. 1
Natural variantiVAR_006243476Y → D in XLA. 1 Publication1
Natural variantiVAR_006244477M → R in XLA. 1 Publication1
Natural variantiVAR_074309481C → S Found in patients with chronic lymphocytic leukemia; unknown pathological significance; results in resistance to ibrutinib therapy; results in a protein that is reversibly inhibited by ibrutinib; disrupts the covalent binding between the enzyme and ibrutinib. 3 PublicationsCorresponds to variants dbSNP:rs1057519825 and dbSNP:rs1057519826EnsemblEnsembl.1
Natural variantiVAR_006245502C → F in XLA. 1
Natural variantiVAR_006246502C → W in XLA. 1 PublicationCorresponds to variant dbSNP:rs41310709Ensembl.1
Natural variantiVAR_006247506C → R in XLA. 1 PublicationCorresponds to variant dbSNP:rs128621200EnsemblClinVar.1
Natural variantiVAR_006248506C → Y in XLA. 1 Publication1
Natural variantiVAR_008318508A → D in XLA. 1
Natural variantiVAR_008319509M → I in XLA. 1
Natural variantiVAR_006249509M → V in XLA. 1 Publication1
Natural variantiVAR_008961512L → P in XLA. 1 Publication1
Natural variantiVAR_008962512L → Q in XLA. 1 Publication1
Natural variantiVAR_008320518L → R in XLA. 1
Natural variantiVAR_006251520R → Q in XLA; severe; prevents activation due to absence of contact between the catalytic loop and the regulatory phosphorylated residue. 4 PublicationsCorresponds to variant dbSNP:rs128621202EnsemblClinVar.1
Natural variantiVAR_008321521D → G in XLA. 1 Publication1
Natural variantiVAR_006252521D → H in XLA; severe. 1 Publication1
Natural variantiVAR_006253521D → N in XLA; severe. 1
Natural variantiVAR_008322523A → E in XLA. 1
Natural variantiVAR_008323525R → G in XLA. 1 Publication1
Natural variantiVAR_006254525R → P in XLA. 1 Publication1
Natural variantiVAR_006255525R → Q in XLA; severe; disturbs ATP-binding. 2 Publications