| + |
B3GNT3 | up-regulates activity 
glycosylation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275389 |
Asn192 |
KREEKLFNVTSTLRI |
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 29438695 |
These results further suggested that B3GNT3 mediates PD-L1 and PD-1 interaction through N-linked glycosylation instead of O-linked glycosylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275390 |
Asn200 |
VTSTLRINTTTNEIF |
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 29438695 |
These results further suggested that B3GNT3 mediates PD-L1 and PD-1 interaction through N-linked glycosylation instead of O-linked glycosylation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization 
phosphorylation
|
CD274 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277275 |
Ser184 |
GKTTTTNsKREEKLF |
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 27572267 |
We show that glycogen synthase kinase 3β (GSK3β) interacts with PD-L1 and induces phosphorylation-dependent proteasome degradation of PD-L1 by β-TrCP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277276 |
Thr180 |
QVLSGKTtTTNSKRE |
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 27572267 |
We show that glycogen synthase kinase 3β (GSK3β) interacts with PD-L1 and induces phosphorylation-dependent proteasome degradation of PD-L1 by β-TrCP. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277552 |
Ser279 |
CGIQDTNsKKQSDTH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 33879767 |
We find EGFR inhibitors promote PD-L1 ubiquitination and proteasomal degradation following GSK3α-mediated phosphorylation of Ser279/Ser283. We identify ARIH1 as the E3 ubiquitin ligase responsible for targeting PD-L1 to degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK2 | up-regulates quantity by stabilization
phosphorylation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277315 |
Thr194 |
EEKLFNVtSTLRINT |
Mus musculus |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 34315872 |
NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277314 |
Thr210 |
TNEIFYCtFRRLDPE |
Mus musculus |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 34315872 |
NEK2 interacts with PD-L1, phosphorylating the T194/T210 residues and preventing ubiquitin-proteasome pathway-mediated degradation of PD-L1 in ER lumen. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
COPS5 | up-regulates quantity by stabilization
deubiquitination
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274977 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27866850 |
The results suggested that TNF-α upregulates expression of CSN5, which interacts and deubiquitinates PD-L1 for protein stabilization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXP3 | up-regulates quantity by expression
transcriptional regulation
|
CD274 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277728 |
|
|
Homo sapiens |
Pancreatic Cancer Cell |
| pmid |
sentence |
| 38339310 |
FOXP3 expression additionally increased programmed death ligand 1 (PD-L1) expression, which, when inhibited with CCL5, decreased the tumor burden and Treg infiltration in orthotopic murine, Pan-02 PDAC tumors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITCH | down-regulates quantity by destabilization
ubiquitination
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278815 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35638972 |
ITCH Ubiquitinates and Down-Regulates Tumor-Surface PD-L1.|The current study supports a model (Fig. 7) in which the E3 ligase ITCH mediates poly-ubiquitination of PD-L1 and down-regulates tumor cell-surface PD-L1 levels (via ubiquitin-directed lysosomal degradation) in MAPKi-adapted melanoma cells and in potentially other biologic contexts such quasi-mesenchymal tumor cell-states that contribute to therapy resistance and metastatic potential. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARIH1 | down-regulates quantity by destabilization
ubiquitination, polyubiquitination
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278582 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33879767 |
E3 ubiquitin ligase ARIH1 directly ubiquitinates PD-L1 and targets it for proteasomal degradation, following EGFR inhibition. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277553 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 33879767 |
We find EGFR inhibitors promote PD-L1 ubiquitination and proteasomal degradation following GSK3α-mediated phosphorylation of Ser279/Ser283. We identify ARIH1 as the E3 ubiquitin ligase responsible for targeting PD-L1 to degradation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
destabilization
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274979 |
|
|
Homo sapiens |
A-375 Cell |
| pmid |
sentence |
| 28813410 |
Deletion of STUB1 resulted in a more profound increase in PD-L1 levels in CMTM6 deficient than in CMTM6 proficient cells, identifying STUB1 as an E3 ligase that causes destabilization of PD-L1 (Fig. 4f,g), either by direct modification of one of the lysines in the PD-L1 cytoplasmic domain or indirectly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPOP | down-regulates quantity
ubiquitination
|
CD274 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274978 |
|
|
Homo sapiens |
LNCaP-C4-2 Cell |
| pmid |
sentence |
| 29160310 |
Loss-of-function mutations in SPOP compromise ubiquitination-mediated PD-L1 degradation, leading to increased PD-L1 levels and reduced numbers of tumor-infiltrating lymphocytes (TILs) in mouse tumors and in primary human prostate cancer specimens. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CD274 | up-regulates
binding
|
PDCD1 |
0.936 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82604 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11015443 |
Pd-l1, was found to bind pd-1 specifically. The functional significance of this interaction has been demonstrated in t cell assays, in which engagement of pd-1 by pd-l1 leads to the inhibition of tcr-mediated lymphocyte proliferation and cytokine secretion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STT3B | up-regulates quantity by stabilization
glycosylation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274976 |
|
|
Homo sapiens |
MCF-10A Cell |
| pmid |
sentence |
| 29765039 |
Together, these results support a notion that the two STT3 isoforms regulate EMT-mediated PD-L1 induction through PD-L1 protein N-glycosylation and stabilization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-betaTRCP | down-regulates quantity by destabilization
polyubiquitination
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277277 |
|
|
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 27572267 |
We show that glycogen synthase kinase 3β (GSK3β) interacts with PD-L1 and induces phosphorylation-dependent proteasome degradation of PD-L1 by β-TrCP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SIGMAR1 | up-regulates quantity by stabilization
stabilization
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274974 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 29117944 |
We propose that Sigma1 is a ligand-operated scaffolding protein that promotes the stability, processing, assembly, and trafficking of specific proteins in the secretory pathway of cancer cells. In support of this hypothesis, we found that siRNA-mediated knockdown of Sigma1 resulted in a significant decrease in PD-L1 protein levels in triple-negative MDA-MB-231 breast cancer and androgen-independent PC3 prostate cancer cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KMT2C | up-regulates quantity by expression
transcriptional regulation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260040 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30385408 |
MLL3 enhances the transcription of PD-L1 and regulates anti-tumor immunity. We found that MLL3 bound to the enhancer of PD-L1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity
phosphorylation
|
CD274 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279047 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27572267 |
Together, the results suggest that GSK3\u03b2 binds and phosphorylates the non-glycosylated PD-L1.|We show that glycogen synthase kinase 3\u03b2 (GSK3\u03b2) interacts with PD-L1 and induces phosphorylation-dependent proteasome degradation of PD-L1 by \u03b2-TrCP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CMTM4 | up-regulates quantity by stabilization
stabilization
|
CD274 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274981 |
|
|
Homo sapiens |
A-375 Cell |
| pmid |
sentence |
| 28813410 |
Furthermore, the observations that (i) CMTM6 affects PD-L1 protein stability at late time points after biosynthesis; (ii) CMTM6, CMTM4 and PD-L1 interact, as shown by co-immunoprecipitation; and that (iii) CMTM6 is largely located at the cell surface, collectively suggest a model in which CMTM6 interacts with PD-L1 at the tumour cell surface and thereby protects it from degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CMTM6 | up-regulates quantity by stabilization
stabilization
|
CD274 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274980 |
|
|
Homo sapiens |
A-375 Cell |
| pmid |
sentence |
| 28813410 |
Furthermore, the observations that (i) CMTM6 affects PD-L1 protein stability at late time points after biosynthesis; (ii) CMTM6, CMTM4 and PD-L1 interact, as shown by co-immunoprecipitation; and that (iii) CMTM6 is largely located at the cell surface, collectively suggest a model in which CMTM6 interacts with PD-L1 at the tumour cell surface and thereby protects it from degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STT3A | up-regulates quantity by stabilization
glycosylation
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274975 |
|
|
Homo sapiens |
MCF-10A Cell |
| pmid |
sentence |
| 29765039 |
Together, these results support a notion that the two STT3 isoforms regulate EMT-mediated PD-L1 induction through PD-L1 protein N-glycosylation and stabilization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FKBP5 | up-regulates quantity by expression
catalytic activity
|
CD274 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274973 |
|
|
Homo sapiens |
U-251MG Cell |
| pmid |
sentence |
| 28978117 |
FKBP51s upregulated PD-L1 expression on the plasma membrane by catalysing the protein folding required for subsequent glycosylation. Inhibition of FKBP51s isomerase activity by SAFit decreased PD-L1 levels |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIF1A | up-regulates quantity by expression 
transcriptional regulation
|
CD274 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27141364 |
STAT3 and HIF-1α cooperatively enhance PD-L1 expression in EML4-ALK-translocated pADC cells under hypoxia. Taken together, these findings suggest that EML4-ALK might increase HIF-1α expression under hypoxia by enhancing transcription and inhibiting ubiquitination of HIF-1α, resulting in the stabilization of HIF-1α, consequently contributing to HIF-1α-mediated upregulation of PD-L1 under hypoxia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT3 | up-regulates quantity by expression
transcriptional regulation
|
CD274 |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259188 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27141364 |
STAT3 and HIF-1α cooperatively enhance PD-L1 expression in EML4-ALK-translocated pADC cells under hypoxia.The protein-DNA binding assay revealed that pSTAT3 was bound to the PD-L1 promoter region in H23 cells transfected with EML4-ALK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CD274
- 
- 