| + |
PRKCB | down-regulates activity 
phosphorylation
|
BTK |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249110 |
Ser180 |
GSLKPGSsHRKTKKP |
Homo sapiens |
RAMOS Cell |
| pmid |
sentence |
| 11598012 |
We provide direct evidence that PKCbeta acts as a feedback loop inhibitor of Btk activation. Inhibition of PKCbeta results in a dramatic increase in B-cell receptor (BCR)-mediated Ca2+ signaling. We identified a highly conserved PKCbeta serine phosphorylation site in a short linker within the Tec homology domain of Btk. Mutation of this phosphorylation site led to enhanced tyrosine phosphorylation and membrane association of Btk, and augmented BCR and FcepsilonRI-mediated signaling in B and mast cells, respectively. | This deductive analysis indicated that PKCbeta phosphorylates S180 in the region bisecting the Btk motif (BM) and the PRR of the TH domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates quantity by destabilization
phosphorylation
|
BTK |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276466 |
Ser51 |
FERGRRGsKKGSIDV |
Homo sapiens |
NAMALWA Cell |
| pmid |
sentence |
| 23754751 |
The activated serine/threonine kinase Akt/protein kinase B (PKB) phosphorylated Btk on two sites prior to 14-3-3ζ binding. The interaction sites were mapped to phosphoserine pS51 in the pleckstrin homology domain and phosphothreonine pT495 in the kinase domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276465 |
Thr495 |
EMRHRFQtQQLLEMC |
Homo sapiens |
NAMALWA Cell |
| pmid |
sentence |
| 23754751 |
The activated serine/threonine kinase Akt/protein kinase B (PKB) phosphorylated Btk on two sites prior to 14-3-3ζ binding. The interaction sites were mapped to phosphoserine pS51 in the pleckstrin homology domain and phosphothreonine pT495 in the kinase domain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates activity 
phosphorylation
|
PLCG2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109746 |
Tyr1197 |
LESEEELySSCRQLR |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109750 |
Tyr1217 |
LNNQLFLyDTHQNLR |
Homo sapiens |
|
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109754 |
Tyr753 |
ERDINSLyDVSRMYV |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109758 |
Tyr759 |
LYDVSRMyVDPSEIN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BTK | up-regulates activity
phosphorylation
|
DAPP1 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250602 |
Tyr139 |
KVEEPSIyESVRVHT |
in vitro |
|
| pmid |
sentence |
| 11524430 |
We present a number of lines of evidence that in vivo, Src-type tyrosine kinases are responsible for the phosphorylation of tyrosine 139 in DAPP-1. | Although Btk appears to phosphorylate DAPP-1 relatively efficiently both in Sf9 cells and in vitro, we find no evidence that in either B cells or PAE cells Btk family kinases phosphorylate DAPP-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249313 |
Tyr139 |
KVEEPSIyESVRVHT |
|
B-lymphocyte |
| pmid |
sentence |
| 10880360 |
Src family kinases mediate receptor-stimulated, phosphoinositide 3-kinase-dependent, tyrosine phosphorylation of dual adaptor for phosphotyrosine and 3-phosphoinositides-1 in endothelial and B cell lines|yrosine phosphorylation of DAPP-1 appears important for appropriate intracellular targeting and creates a potential binding site for Src homology 2 domain-containing proteins. |
|
| Publications: |
2 |
Organism: |
In Vitro, |
| + |
BTK | up-regulates
phosphorylation
|
ITK |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98036 |
Tyr180 |
ETVVIALyDYQTNDP |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanismthe major phosphorylation sites were identified as conserved tyrosines, for itk y180 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates
phosphorylation
|
TEC |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98086 |
Tyr206 |
RLERGQEyLILEKND |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. Here, we could confirm that y223 is the only site in the btk-sh3 domain being detectably phosphorylated |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates
phosphorylation
|
BMX |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98028 |
Tyr216 |
SSTSLAQyDSNSKKI |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98032 |
Tyr224 |
DSNSKKIyGSQPNFN |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. For bmx, we obtained two phosphorylated sites, y215 and y223 (fig. 6c). The bmx-y215 is a conserved tyrosine, which is homologous to btk-y223 and itk-y180 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ABL1 | down-regulates activity
phosphorylation
|
BTK |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260801 |
Tyr223 |
LKKVVALyDYMPMNA |
Homo sapiens |
|
| pmid |
sentence |
| 12445832 |
In this report we describe for the first time that ABL1 and Btk physically interact and that ABL1 can phosphorylate tyrosine 223 in the SH3 domain of Btk. | This is presumably due to the negative regulatory effectof Btk SH3 domain phosphorylation caused by ABL1,which would result in a decreased catalytic activity ofBtk resulting in impaired autophosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
BTK |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254694 |
Tyr223 |
LKKVVALyDYMPMNA |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABL1 |
phosphorylation
|
BTK |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245278 |
Tyr223 |
LKKVVALyDYMPMNA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12445832 |
In this report we describe for the first time that c-Abl and Btk physically interact and that c-Abl can phosphorylate tyrosine 223 in the SH3 domain of Btk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITK | down-regulates activity
phosphorylation
|
BTK |
0.474 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251333 |
Tyr223 |
LKKVVALyDYMPMNA |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Btk-SH3 mutant Y223A was not phosphorylated by Itk. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop.|In Btk, the SH3 domain mutation Y223F results in enhanced fibroblast transformation, implying that the SH3 domain may play a negative regulatory role |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TEC | down-regulates activity
phosphorylation
|
BTK |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246652 |
Tyr223 |
LKKVVALyDYMPMNA |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the SH3 domain via a transphosphorylation mechanism, which for Bruton's tyrosine kinase (Btk) affects tyrosine 223.|In Btk, the SH3 domain mutation Y223F results in enhanced fibroblast transformation, implying that the SH3 domain may play a negative regulatory role |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates activity
phosphorylation
|
GTF2I |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108338 |
Tyr248 |
EESEDPDyYQYNIQA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11373296 |
These residues, tyr248, tyr357, and tyr462, were also found to be the major sites for btk-dependent phosphorylation of bap/tfii-i in vivo. Residues tyr357 and tyr462 are contained within the loop regions of adjacent helix-loop-helix-like repeats within bap/tfii-i. Mutation of either tyr248, tyr357, or tyr462 to phenylalanine reduced transcription from a c-fos promoter relative to wild-type bap/tfii-i in transfected cos-7 cells, consistent with the interpretation that phosphorylation at these sites contributes to transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108342 |
Tyr398 |
QSHVEDLyVEGLPEG |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11373296 |
These residues, tyr248, tyr357, and tyr462, were also found to be the major sites for btk-dependent phosphorylation of bap/tfii-i in vivo. Residues tyr357 and tyr462 are contained within the loop regions of adjacent helix-loop-helix-like repeats within bap/tfii-i. Mutation of either tyr248, tyr357, or tyr462 to phenylalanine reduced transcription from a c-fos promoter relative to wild-type bap/tfii-i in transfected cos-7 cells, consistent with the interpretation that phosphorylation at these sites contributes to transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108346 |
Tyr503 |
EAHPNDLyVEGLPEN |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11373296 |
These residues, tyr248, tyr357, and tyr462, were also found to be the major sites for btk-dependent phosphorylation of bap/tfii-i in vivo. Residues tyr357 and tyr462 are contained within the loop regions of adjacent helix-loop-helix-like repeats within bap/tfii-i. Mutation of either tyr248, tyr357, or tyr462 to phenylalanine reduced transcription from a c-fos promoter relative to wild-type bap/tfii-i in transfected cos-7 cells, consistent with the interpretation that phosphorylation at these sites contributes to transcriptional activation. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
BTK | up-regulates activity
phosphorylation
|
WAS |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273958 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10068673 |
These results demonstrate that WASP, under this experimental condition, can be tyrosine-phosphorylated by the kinase activity of Btk and that the direct interaction between WASP and the SH3 domain of Btk is required for this phosphorylation to occur. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK |
phosphorylation
|
WAS |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86004 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
|
| pmid |
sentence |
| 10068673 |
These results indicate that btk phosphorylates wasp on its tyrosine 291 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates activity
phosphorylation
|
DDX41 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266404 |
Tyr414 |
DVIQEVEyVKEEAKM |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 25704810 |
The kinase and SH3/SH2 interaction domains of BTK bind, respectively, the DEAD-box domain of DDX41 and transmembrane region of STING. BTK phosphorylates DDX41, and its kinase activities are critical for STING-mediated IFN-β production. We show that Tyr364 and Tyr414 of DDX41 are critical for its recognition of AT-rich DNA and binding to STING, and tandem mass spectrometry identifies Tyr414 as the BTK phosphorylation site. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SYK | up-regulates activity
phosphorylation
|
BTK |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247586 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
|
| pmid |
sentence |
| 11226282 |
We have demonstrated that BLNK mediates Syk-dependent Btk activation. In a reconstitution cell system, coexpression of BLNK allows Syk to phosphorylate Btk on its tyrosine 551, leading to the enhancement of Btk activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates
phosphorylation
|
BTK |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-41607 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 8630736 |
Phosphorylation at y551 requires lyn kinase activity, indicating that y551 is a transphosphorylation site \ this transphosphorylation at y551 is followed by phosphorylation at a second site, which is dependent on btk catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BTK | up-regulates
phosphorylation
|
BTK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-41480 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 8630736 |
Overexpression of btk with a src family kinase increases tyrosine phosphorylation and catalytic activity of btk. This occurs by transphosphorylation at y551 in the btk catalytic domain and the enhancement of btk autophosphorylation at a second site. We mapped the major btk autophosphorylation site to y223 within the sh3 domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SRC | up-regulates activity
phosphorylation
|
BTK |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251100 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
|
| pmid |
sentence |
| 8629002 |
This interaction of BTK with SRC kinases transphosphorylated BTK on tyrosine at residue 551, which led to BTK activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates activity
phosphorylation
|
STAT5A |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250603 |
Tyr694 |
LAKAVDGyVKPQIKQ |
in vitro |
|
| pmid |
sentence |
| 11413148 |
Ectopically expressed BTK kinase domain was capable of tyrosine-phosphorylating STAT5A both in vitro and in vivo. BTK-mediated tyrosine phosphorylation of ectopically expressed wild type (but not Tyr(694) mutant) STAT5A enhanced its DNA binding activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
BTK | up-regulates
phosphorylation
|
PLCG2 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111069 |
Tyr753 |
ERDINSLyDVSRMYV |
Homo sapiens |
|
| pmid |
sentence |
| 11606584 |
By measuring the ability of human plcgamma2 to restore calcium responses to the b-cell receptor stimulation or oxidative stress in a b-cell line (dt40) deficient in plcgamma2, we have demonstrated that two tyrosine residues, tyr(753) and tyr(759), were important for the plcgamma2 signaling function.Of the two kinases that previously have been proposed to phosphorylate plcgamma2, btk, and syk, purified btk had much greater ability to phosphorylate recombinant plcgamma2 in vitro, whereas syk efficiently phosphorylated adapter protein blnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111073 |
Tyr759 |
LYDVSRMyVDPSEIN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11606584 |
By measuring the ability of human plcgamma2 to restore calcium responses to the b-cell receptor stimulation or oxidative stress in a b-cell line (dt40) deficient in plcgamma2, we have demonstrated that two tyrosine residues, tyr(753) and tyr(759), were important for the plcgamma2 signaling function.Of the two kinases that previously have been proposed to phosphorylate plcgamma2, btk, and syk, purified btk had much greater ability to phosphorylate recombinant plcgamma2 in vitro, whereas syk efficiently phosphorylated adapter protein blnk. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
PI3K | up-regulates activity
phosphorylation
|
BTK |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252709 |
|
|
Mus musculus |
Myeloma Cell Line |
| pmid |
sentence |
| 10201980 |
Activation of Btk occurs by transphosphorylation of tyrosine 551 in the catalytic domain, resulting in a dramatic increase in the catalytic activity of the kinase (11, 12, 13). This allows for autophosphorylation at tyrosine 223 in the SH3 domain (14). Both Lyn and Syk have been demonstrated to be involved in BCR-mediated Btk activation (11), but processes that drive colocalization of these kinases are ill-defined. Recently, it was suggested that phosphatidylinositol 3-kinase (PI3-K) is also involved in Btk activation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | B-cell activation |
| + |
PIK3CA | up-regulates activity
phosphorylation
|
BTK |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249610 |
|
|
Mus musculus |
Myeloma Cell Line |
| pmid |
sentence |
| 10201980 |
Activation of Btk occurs by transphosphorylation of tyrosine 551 in the catalytic domain, resulting in a dramatic increase in the catalytic activity of the kinase (11, 12, 13). This allows for autophosphorylation at tyrosine 223 in the SH3 domain (14). Both Lyn and Syk have been demonstrated to be involved in BCR-mediated Btk activation (11), but processes that drive colocalization of these kinases are ill-defined. Recently, it was suggested that phosphatidylinositol 3-kinase (PI3-K) is also involved in Btk activation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ibrutinib | down-regulates
chemical inhibition
|
BTK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189641 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
9-(1-Methyl-4-pyrazolyl)-1-[1-(1-oxoprop-2-enyl)-2,3-dihydroindol-6-yl]-2-benzo[h][1,6]naphthyridinone | down-regulates activity
chemical inhibition
|
BTK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262238 |
|
|
in vitro |
|
| pmid |
sentence |
| 24556163 |
BTK is a member of the TEC family of non-receptor tyrosine kinases whose deregulation has been implicated in a variety of B-cell-related diseases. We have used structure-based drug design in conjunction with kinome profiling and cellular assays to develop a potent, selective, and irreversible BTK kinase inhibitor, QL47, which covalently modifies Cys481. QL47 inhibits BTK kinase activity with an IC50 of 7 nM, inhibits autophosphorylation of BTK on Tyr223 in cells with an EC50 of 475 nM, and inhibits phosphorylation of a downstream effector PLCγ2 (Tyr759) with an EC50 of 318 nM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BTK | up-regulates
phosphorylation
|
GTF2I |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46060 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9012831 |
We now describe a protein, bap-135, that is associated with btk in b cells and is a substrate for phosphorylation by btk.Taken together, these observations suggest that bap-135 may reside downstream of btk in a signaling pathway originating at the bcr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BTK
- 
- 