+ |
CSNK1E | down-regulates activity
phosphorylation
|
PER3 |
0.734 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250815 |
Ser622 |
ILSTAMLsLGSGISQ |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250816 |
Ser625 |
TAMLSLGsGISQCGY |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250817 |
Ser628 |
LSLGSGIsQCGYSST |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250818 |
Ser633 |
GISQCGYsSTIVHVP |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250819 |
Ser634 |
ISQCGYSsTIVHVPP |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250820 |
Thr635 |
SQCGYSStIVHVPPP |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11865049 |
The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. Moreover, CKIepsilon and CKIdelta are able to induce nuclear translocation of mPer3, which requires its nuclear localization signal. The mutation in potential phosphorylation sites on mPer3 decreased the extent of both nuclear translocation and degradation of mPer3 that are stimulated by CKIepsilon. | In mut7 in which all of the conserved serine and threonine residues in this region were mutated, the ratio of the shifted band was greatly reduced reproducibly. |
|
Publications: |
6 |
Organism: |
Chlorocebus Aethiops |
Pathways: | Circadian clock |
+ |
CLOCK | up-regulates quantity by expression
transcriptional regulation
|
PER3 |
0.586 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253635 |
|
|
|
|
pmid |
sentence |
22750052 |
Mammalian clocks are primarily based on a transcription and translation feedback loop in which a heterodimeric complex of the transcription factors CLOCK (circadian locomotor output cycles kaput) and BMAL1 (brain and muscle Arnt-like protein 1) activates the expression of its own repressors, the period (PER1-3) and cryptochrome (CRY1,2) proteins. |
|
Publications: |
1 |
Pathways: | Circadian clock |
+ |
ARNTL | up-regulates quantity by expression
transcriptional regulation
|
PER3 |
0.587 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253630 |
|
|
|
|
pmid |
sentence |
22750052 |
Mammalian clocks are primarily based on a transcription and translation feedback loop in which a heterodimeric complex of the transcription factors CLOCK (circadian locomotor output cycles kaput) and BMAL1 (brain and muscle Arnt-like protein 1) activates the expression of its own repressors, the period (PER1-3) and cryptochrome (CRY1,2) proteins. |
|
Publications: |
1 |
Pathways: | Circadian clock |
+ |
CLOCK/BMAL1 | up-regulates quantity by expression
transcriptional regulation
|
PER3 |
0.587 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253683 |
|
|
|
|
pmid |
sentence |
22750052 |
Mammalian clocks are primarily based on a transcription and translation feedback loop in which a heterodimeric complex of the transcription factors CLOCK (circadian locomotor output cycles kaput) and BMAL1 (brain and muscle Arnt-like protein 1) activates the expression of its own repressors, the period (PER1-3) and cryptochrome (CRY1,2) proteins. |
|
Publications: |
1 |
Pathways: | Circadian clock |
+ |
RAI1 | up-regulates quantity by expression
transcriptional regulation
|
PER3 |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266841 |
|
|
Mus musculus |
|
pmid |
sentence |
22578325 |
Data further show that haploinsufficiency of RAI1 and Rai1 in SMS fibroblasts and the mouse hypothalamus, respectively, results in the transcriptional dysregulation of the circadian clock and causes altered expression and regulation of multiple circadian genes, including PER2, PER3, CRY1, BMAL1, and others. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Hypothalamus |
Pathways: | Circadian clock |
+ |
CSNK1D | down-regulates quantity by destabilization
phosphorylation
|
PER3 |
0.712 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267998 |
|
|
Mus musculus |
|
pmid |
sentence |
11865049 |
We show here that mPer proteins, negative limbs of the autoregulatory loop, are specific substrates for CKIepsilon and CKIdelta. The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Circadian clock |
+ |
CSNK1E | down-regulates quantity by destabilization
phosphorylation
|
PER3 |
0.734 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267996 |
|
|
Mus musculus |
|
pmid |
sentence |
11865049 |
We show here that mPer proteins, negative limbs of the autoregulatory loop, are specific substrates for CKIepsilon and CKIdelta. The CKI phosphorylation of mPer1 and mPer3 proteins results in their rapid degradation, which is dependent on the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Circadian clock |