| Id: | acc4945 |
| Group: | 1sens |
| Protein: | STAT3 |
| Gene Symbol: | Stat3 |
| Protein Id: | P42227 |
| Protein Name: | STAT3_MOUSE |
| PTM: | phosphorylation |
| Site: | Tyr705 |
| Site Sequence: | EADPGSAAPYLKTKFICVTPT |
| Disease Category: | Cardiovascular and circulatory system diseases |
| Disease: | Pulmonary Hypertension |
| Disease Subtype: | |
| Disease Cellline: | |
| Disease Info: | |
| Drug: | delta-aminolevulinic acid (ALA) |
| Drug Info: | "Delta-aminolevulinic acid (ALA) is a non-proteinogenic amino acid and a key intermediate in the biosynthesis of porphyrins, heme, and chlorophyll. It plays a crucial role in various biological processes and is also used in photodynamic therapy for certain medical conditions." |
| Effect: | modulate |
| Effect Info: | "ALA inhibits ET-1-induced STAT3 phosphorylation by improving heme biosynthesis, increasing the activity of the cGMP/PKG pathway, and upregulating miR-204. Subsequently, it reduces mitochondrial oxidative stress (decreases superoxide production), restores SOD2 expression, and alleviates hypoxic pulmonary hypertension." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 25659899 |
| Sentence Index: | 25659899_7 |
| Sentence: | "Thus, a reversal of factors increasing mitochondrial superoxide and oxidant effects that potentially influence remodeling signaling related to miR204 expression and perhaps iron availability needed for the biosynthesis of heme by the ferrochelatase reaction could be factors in the beneficial actions of ALA in pulmonary hypertension." |
Sequence & Structure:
MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM
Select PDB:
No data.
Protein Tractability:
source: Open TargetsNo data.
PTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMD| Residue | Position | State | Disease | Class | PMID |
|---|---|---|---|---|---|
| Y | 705 | U | Neurofibromatosis | Phosphorylation | 23318430 |
| Y | 705 | U | Squamous cell carcinoma | Phosphorylation | 19934324 |
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.
