| Id: | acc2392 |
| Group: | 2sens |
| Protein: | STAT5 |
| Gene Symbol: | STAT5A |
| Protein Id: | P42229 |
| Protein Name: | STA5A_HUMAN |
| PTM: | phosphorylation |
| Site: | Tyr694 |
| Site Sequence: | PVLAKAVDGYVKPQIKQVVPE |
| Disease Category: | Cancer |
| Disease: | Hepatocellular Carcinoma |
| Disease Subtype: | |
| Disease Cellline: | |
| Disease Info: | |
| Drug: | PD-1 therapy |
| Drug Info: | - |
| Effect: | inhibit |
| Effect Info: | Lenvatinib enhances the anti - PD - 1 therapy's anti - tumor immune response in patients with hepatocellular carcinoma (HCC) by targeting fibroblast growth factor receptor 4 (FGFR4) to reduce the level of programmed death - ligand 1 (PD - L1) in tumors and the infiltration of regulatory T cells (Tregs). |
| Note: | Non-conventional drugs |
| Score: | 4.5 |
| Pubmed(PMID): | 34036623 |
| Sentence Index: | 34036623_7-8 |
| Sentence: | "On the other hand, the level of IL-2 increased after anti-PD-1 treatment, but IL-2-mediated Treg differentiation was blocked by lenvatinib through targeting FGFR4 to restrain signal transducer and activator of transcription 5 (STAT5) phosphorylation. By regulating the variations in the number of Tregs and the tumor FGFR4 level in C57BL/6-forkhead box protein P3 (Foxp3DTR ) mice, we found that high levels of FGFR4 and Treg infiltration sensitized tumors to the combination treatment." |
Sequence & Structure:
MAGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPQDRAQATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQKTYDRCPLELVRCIRHILYNEQRLVREANNCSSPAGILVDAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGSNELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPERNLWNLKPFTTRDFSIRSLADRLGDLSYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVNASADAGGSSATYMDQAPSPAVCPQAPYNMYPQNPDHVLDQDGEFDLDETMDVARHVEELLRRPMDSLDSRLSPPAGLFTSARGSLS
Select PDB:
No data.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTAC| STAT5A-Tyr694 | |
|---|---|
| Cancer | Intensity |
| BRCA | -0.21 |
| COAD | 0.081 |
| HGSC | 2.396 |
| ccRCC | 0.242 |
| GBM | -0.214 |
| HNSC | 0.119 |
| LUAD | 0.595 |
| LUSC | 0.038 |
| non_ccRCC | -1.223 |
| PDAC | -0.376 |
| UCEC | -1.449 |
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| Y | 694 | D | Head and neck squamous cell carcinoma | Phosphorylation | 21281788 |
| Y | 694 | D | Sjogren's syndrome | Phosphorylation | 36072585 |
| Y | 694 | N | Large granular lymphocytic leukemia | Phosphorylation | 23596048 |
| Y | 694 | U | Glioblastoma | Phosphorylation | 22729867 |
| Y | 694 | U | Colon cancer | Phosphorylation | 23733954 |
| Y | 694 | U | Human immunodeficiency virus infectious disease | Phosphorylation | 21716071 |
State Note: Based on the distinct PTM states in diseases, PTMD classified all disease-associated PTMs into six classes, including whether the up-regulation (U) or down-regulation (D) of PTM levels, the absence (A) or presence (P) of PTMs, and the creation (C) or disruption (N) of PTM sites are associated with diseases.
PTM-Drug Perturbation Response:
source: DecryptMNo data.
Function score:
source: funscoRNo data.
