| + |
CSNK2A1 |
phosphorylation
|
HCLS1 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250885 |
Thr16 |
DVSVSVEtQGDDWDT |
Homo sapiens |
|
| pmid |
sentence |
| 10806407 |
The in vivo Ser/Thr phosphorylation of HS1 is enhanced by okadaic acid and reduced by specific inhibitors of casein kinase (CK)2. In vitro, HS1 is an excellent substrate for either CK2 alpha subunit alone (Km = 47 nM) or CK2 holoenzyme | It is likely therefore that Thr16 and/or Thr23 account for the phosphate incorporated into HS1 threonyl residue(s) upon incubation with CK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250886 |
Thr23 |
TQGDDWDtDPDFVND |
Homo sapiens |
|
| pmid |
sentence |
| 10806407 |
The in vivo Ser/Thr phosphorylation of HS1 is enhanced by okadaic acid and reduced by specific inhibitors of casein kinase (CK)2. In vitro, HS1 is an excellent substrate for either CK2 alpha subunit alone (Km = 47 nM) or CK2 holoenzyme | It is likely therefore that Thr16 and/or Thr23 account for the phosphate incorporated into HS1 threonyl residue(s) upon incubation with CK2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FGR |
phosphorylation
|
HCLS1 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251144 |
Tyr222 |
MEAPTTAyKKTTPIE |
in vitro |
|
| pmid |
sentence |
| 10066823 |
We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn. this interaction is weakened by phosphorylation of Tyr-222, through an allosteric mechanism that ultimately causes the detachment of fully phosphorylated HS1 from c-Fgr. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN |
phosphorylation
|
HCLS1 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251399 |
Tyr222 |
MEAPTTAyKKTTPIE |
in vitro |
|
| pmid |
sentence |
| 10066823 |
HS1 was shown to undergo a process of sequential phosphorylation both in vitro and in vivo, which is synergistically mediated by Syk and Src family protein-tyrosine kinases and essential for B cell antigen receptor-mediated apoptosis. We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SYK | up-regulates 
phosphorylation
|
HCLS1 |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47338 |
Tyr378 |
EPEPENDyEDVEEMD |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Here, we show that bcr-associated tyrosine kinases lyn and syk synergistically phosphorylate hs1, and that tyr-378 and tyr-397 of hs1 are the critical residues for its bcr-induced phosphorylation. once the two tyrosine residues are both phosphorylated, processive phosphorylation of hs1 by lyn and the other src family kinases would take place, producing hyperphosphorylated form of hs1. Finally, it is this hyperphosphorylated form of hs1 that translocates to the nucleus and activates b cell apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47342 |
Tyr397 |
EDEPEGDyEEVLEPE |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9104825 |
Here, we show that bcr-associated tyrosine kinases lyn and syk synergistically phosphorylate hs1, and that tyr-378 and tyr-397 of hs1 are the critical residues for its bcr-induced phosphorylation. once the two tyrosine residues are both phosphorylated, processive phosphorylation of hs1 by lyn and the other src family kinases would take place, producing hyperphosphorylated form of hs1. Finally, it is this hyperphosphorylated form of hs1 that translocates to the nucleus and activates b cell apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
HCLS1 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251400 |
Tyr378 |
EPEPENDyEDVEEMD |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Lyn and Syk synergistically phosphorylate HS1, and that Tyr-378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis. PMID: 9104825 PMCID: PMC2196252 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251401 |
Tyr397 |
EDEPEGDyEEVLEPE |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Lyn and Syk synergistically phosphorylate HS1, and that Tyr-378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis. PMID: 9104825 PMCID: PMC2196252 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates quantity by expression 
transcriptional regulation
|
HCLS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260052 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11494141 |
Defects in PTEN, a tumor suppressor, have been found in cancers arising in a variety of human tissues. To elucidate the tumor-suppressive function of this gene, we have been analysing expression profiles of cancer cells after introduction of exogenous PTEN. Those experiments identified 99 candidate genes that were transcriptionally transactivated. Among them, we report here the further analyses of eight genes, EGR2/Krox-20, BPOZ, APS, HCLS1/HS1, DUSP1/MKP1, NDRG1/Drg1/RTP, NFIL3/E4BP4, and a novel gene (PINK1, PTEN-induced putative kinase). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
HCLS1
- 
- 