+ |
CSNK2A1 | down-regulates
phosphorylation
|
IKZF1 |
0.294 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174820 |
Ser101 |
GSHRDQGsSALSGVG |
Homo sapiens |
|
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174824 |
Ser13 |
GQDMSQVsGKESPPV |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174828 |
Ser295 |
LSDTPYDsSASYEKE |
Homo sapiens |
|
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174832 |
Ser63 |
NVKVETQsDEENGRA |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174836 |
Thr23 |
ESPPVSDtPDEGDEP |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
CSNK2B | down-regulates
phosphorylation
|
IKZF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174840 |
Ser101 |
GSHRDQGsSALSGVG |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174844 |
Ser13 |
GQDMSQVsGKESPPV |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174848 |
Ser295 |
LSDTPYDsSASYEKE |
Homo sapiens |
|
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174852 |
Ser63 |
NVKVETQsDEENGRA |
Homo sapiens |
|
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway / these results suggest that ck2 kinase directly phosphorylates amino acids 13, 23, 63, 101 and 294 in vivo |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174856 |
Thr23 |
ESPPVSDtPDEGDEP |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
We identified four novelikarosphosphorylation sites that are phosphorylated by ck2 kinase. / ck2-mediated phosphorylation inhibits ikaros' localization to pc-hc / hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
SYK | up-regulates
phosphorylation
|
IKZF1 |
0.414 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199096 |
Ser361 |
LAEGTPRsNHSAQDS |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
23071339 |
Syk phoshorylatesikarosat unique c-terminal serine phosphorylation sites s358 and s361, thereby augmenting its nuclear localization and sequence-specific dna binding activity. Mechanistically, we establish that syk-inducedikarosactivation is essential for its nuclear localization and optimal transcription factor function. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199100 |
Ser364 |
GTPRSNHsAQDSAVE |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
23071339 |
Syk phoshorylatesikarosat unique c-terminal serine phosphorylation sites s358 and s361, thereby augmenting its nuclear localization and sequence-specific dna binding activity. Mechanistically, we establish that syk-inducedikarosactivation is essential for its nuclear localization and optimal transcription factor function. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PPP1CB | up-regulates
dephosphorylation
|
IKZF1 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174862 |
|
|
Homo sapiens |
|
pmid |
sentence |
21750978 |
Ikarosis dephosphorylated by protein phosphatase 1 (pp1) via interaction at a consensus pp1-binding motif/ hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IKZF1 | up-regulates activity
|
Lymphopoiesis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259958 |
|
|
Homo sapiens |
Hematopoietic Stem Cell |
pmid |
sentence |
25085254 |
The Ikaros family of DNA binding proteins are critical regulators of lymphocyte differentiation. In multipotent hematopoietic progenitors, Ikaros supports transcriptional priming of genes promoting lymphocyte differentiation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | up-regulates
dephosphorylation
|
IKZF1 |
0.282 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174859 |
|
|
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
21750978 |
Ikarosis dephosphorylated by protein phosphatase 1 (pp1) via interaction at a consensus pp1-binding motif/ hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin4-RBX1-DDB1 | down-regulates quantity by destabilization
polyubiquitination
|
IKZF1 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272083 |
|
|
Homo sapiens |
MM1-S Cell |
pmid |
sentence |
24292625 |
We found that lenalidomide causes selective ubiquitination and degradation of two lymphoid transcription factors, IKZF1 and IKZF3, by the CRBN-CRL4 ubiquitin ligase. IKZF1 and IKZF3 are essential transcription factors in multiple myeloma. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IKZF1 | up-regulates quantity by expression
transcriptional regulation
|
LNPEP |
0.279 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255403 |
|
|
Homo sapiens |
Trophoblast Cell Line |
pmid |
sentence |
15894523 |
Activator protein-2 (AP-2) and Ikaros transcription factors play significant roles in exerting high promoter activity of P-LAP/OTase in the trophoblastic cells. Moreover, P-LAP/OTase is transcriptionally regulated in a trophoblast-differentiation-dependent fashion via up-regulation of AP-2, putatively AP-2alpha. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
lenalidomide | down-regulates quantity by destabilization
chemical inhibition
|
IKZF1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236910 |
|
|
Homo sapiens |
|
pmid |
sentence |
24328678 |
Members of the Ikaros family of transcription factors, specifically Ikaros and Aiolos (encoded by the genes IKZF1 and IKZF3 respectively), are recruited as protein substrates for CRL4CRBN in T cells in response to lenalidomide or pomalidomide treatment. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PP1 | up-regulates
dephosphorylation
|
IKZF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264663 |
|
|
Homo sapiens |
|
pmid |
sentence |
21750978 |
Ikarosis dephosphorylated by protein phosphatase 1 (pp1) via interaction at a consensus pp1-binding motif/ hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CC | up-regulates
dephosphorylation
|
IKZF1 |
0.336 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174865 |
|
|
Homo sapiens |
|
pmid |
sentence |
21750978 |
Ikarosis dephosphorylated by protein phosphatase 1 (pp1) via interaction at a consensus pp1-binding motif/ hyperphosphorylation of ikaros promotes its degradation by the ubiquitin/proteasome pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |