| + |
MAPK8 | up-regulates quantity by stabilization 
phosphorylation
|
PIN1 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277562 |
Ser115 |
SQFSDCSsAKARGDL |
Homo sapiens |
Cholangiocarcinoma Cell Line |
| pmid |
sentence |
| 34048060 |
Mechanistically, the JNK kinases directly bind to and phosphorylate PIN1 at Ser115, and this phosphorylation prevents PIN1 mono-ubiquitination at Lys117 and its proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK9 | up-regulates quantity by stabilization
phosphorylation
|
PIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277563 |
Ser115 |
SQFSDCSsAKARGDL |
Homo sapiens |
Cholangiocarcinoma Cell Line |
| pmid |
sentence |
| 34048060 |
Mechanistically, the JNK kinases directly bind to and phosphorylate PIN1 at Ser115, and this phosphorylation prevents PIN1 mono-ubiquitination at Lys117 and its proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAP3K11 | up-regulates
phosphorylation
|
PIN1 |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205586 |
Ser138 |
QKPFEDAsFALRTGE |
Homo sapiens |
|
| pmid |
sentence |
| 25519816 |
Here we demonstrate that mixed-lineage kinase 3 (mlk3), a map3k family member, phosphorylates pin1 on a ser138 site to increase its catalytic activity and nuclear translocation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity 
phosphorylation
|
PIN1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202487 |
Ser16 |
PGWEKRMsRSSGRVY |
Homo sapiens |
|
| pmid |
sentence |
| 23970419 |
Here, we found that aurora a can interact with and phosphorylate pin1 at ser16, which suppresses the g2/m function of pin1 by disrupting its binding ability and mitotic entry. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates activity
phosphorylation
|
PIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112164 |
Ser16 |
PGWEKRMsRSSGRVY |
Homo sapiens |
|
| pmid |
sentence |
| 11723108 |
Pka and pkc readily phosphorylated pin1 and its ww domain in summary, we have demonstrated that phosphorylation of the pin1 ww domain on ser16 regulates its ability to function as a pser/thr-binding module. |To examine the importance of Ser16 of Pin1, it was mutated to Glu to mimic pSer, and the mutant Pin1S16E failed to bind mitotic phosphoproteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
PIN1 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139919 |
Ser65 |
SHLLVKHsQSRRPSS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16118204 |
Here we demonstrate that ser-65 in pin1 is the major site for plk1-specific phosphorylation, and the polo-box domain of plk1 is required for this phosphorylation. Interestingly, the phosphorylation of pin1 by plk1 does not affect its isomerase activity but rather is linked to its protein stability. pin1 is ubiquitinated in hela s3 cells, and substitution of glu for ser-65 reduces the ubiquitination of pin1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
all-trans-retinoic acid | down-regulates activity
chemical inhibition
|
PIN1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259925 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30093655 |
ATRA inhibits leukemia, breast, and liver cancer by targeting isomerase Pin1, a master regulator of oncogenic signaling networks. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | down-regulates quantity by destabilization
binding
|
KLF10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276503 |
|
|
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 23994618 |
RAF1 phosphorylates the Thr93 site of KLF10 in vivo. Since the phosphorylation of Thr93 enables KLF10 and PIN1 to bind, it seems likely that RAF-1 will have an effect on KLF10 stability that is similar to that of PIN1.PIN1 facilitates KLF10 protein degradation. ( |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | up-regulates activity
isomerization
|
IRS1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265757 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 23720771 |
In this study, the association of Par14 with insulin receptor substrate 1 (IRS-1) was demonstrated in HepG2 cells|Therefore, although Pin1 and Par14 associate with different portions of IRS-1, the prolyl cis/trans isomerization in multiple sites of IRS-1 by these isomerases appears to be critical for efficient insulin receptor-induced IRS-1 phosphorylation|Par14 overexpression in HepG2 markedly enhanced insulin-induced IRS-1 phosphorylation and its downstream events |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | down-regulates quantity by destabilization
binding
|
IRF3 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252256 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16699525 |
Here we report that activation of IRF3 is negatively regulated by the peptidyl-prolyl isomerase Pin1. After stimulation by double-stranded RNA, induced phosphorylation of the Ser339–Pro340 motif of IRF3 led to its interaction with Pin1 and finally polyubiquitination and then proteasome-dependent degradation of IRF3. Suppression of Pin1 by RNA interference or genetic deletion resulted in enhanced IRF-3-dependent production of interferon-beta, with consequent reduction of virus replication. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STIL | up-regulates
binding
|
PIN1 |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138677 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 16024801 |
Cell cycle-dependent phosphorylation of sil is required for its interaction with pin1, a regulator of mitosis. Point mutation of the seven (s/t)p sites between amino acids 567 and 760 reduces mitotic phosphorylation of sil, pin1 binding, and spindle checkpoint duration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH | up-regulates quantity by expression 
transcriptional regulation
|
PIN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254342 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19151708 |
Previously, we have shown that commitment of the C2C12 cells to the osteoblastic lineage occurs around 24h after BMP treatment, when the osteoblast specific transcription factor Cbfa1 and the novel osteoblast related genes Tcf7 and Hey1 become regulated |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
diarsenic trioxide | down-regulates activity
chemical inhibition
|
PIN1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259923 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30093655 |
Here we show that ATO targets Pin1 and cooperates with ATRA to exert potent anticancer activity. ATO inhibits and degrades Pin1, and suppresses its oncogenic function by noncovalent binding to Pin1’s active site |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | down-regulates activity
isomerization
|
XPO5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263015 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27846390 |
Here we show that ERK suppresses pre-miRNA export from the nucleus through phosphorylation of exportin-5 (XPO5) at T345/S416/S497. After phosphorylation by ERK, conformation of XPO5 is altered by prolyl isomerase Pin1, resulting in reduction of pre-miRNA loading. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH1 | up-regulates quantity by expression
transcriptional regulation
|
PIN1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183458 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19151708 |
Notch1 directly induces transcription of pin1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | down-regulates quantity by repression
transcriptional regulation
|
IFNB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252289 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16699525 |
To investigate the temporal regulation of IRF3-dependent transcription by Pin1, we used a rapid-response luciferase reporter gene. Real-time reporter gene assays showed that suppression of endogenous Pin1 expression substantially prolonged both IRF3-dependent transcription and IFN-beta promoter activation after poly(I)dotpoly(C) stimulation (Fig. 4c,d). Consistent with the inhibitory effects of Pin1 on the IFN-beta promoter |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | up-regulates
binding
|
MYC |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202134 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 23716601 |
Pin1 prolyl isomerase enhances recruitment of serine 62-phosphorylated myc and its coactivators to select promoters during gene activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIN1 | up-regulates
binding
|
NOTCH1 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183461 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19151708 |
Prolyl-isomerase pin1 interacts with notch1 and affects notch1 activation. Pin1 potentiates notch1 cleavage by gamma-secretase, leading to an increased release of the active intracellular domain and ultimately enhancing notch1. pin1 potentiates notch1 cleavage by gamma-secretase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PIN1
- 
- 