Id: | acc2394 |
Group: | 2sens |
Protein: | STAT6 |
Gene Symbol: | STAT6 |
Protein Id: | P42226 |
Protein Name: | STAT6_HUMAN |
PTM: | phosphorylation |
Site: | Tyr641 |
Site Sequence: | EQMGKDGRGYVPATIKMTVER |
Disease Category: | Cancer |
Disease: | Breast Cancer |
Disease Subtype: | |
Disease Cellline: | EO771 |
Disease Info: | |
Drug: | emodin |
Drug Info: | "Emodin is an anthraquinone derivative that acts as an anti-SARS-CoV agent by blocking the interaction between the SARS-CoV spike protein and angiotensin-converting enzyme 2 (ACE2), inhibits casein kinase 2 (CK2), exhibits anti-inflammatory and anticancer activities, serves as a selective 11beta-HSD1 inhibitor with IC50 values of 186 nM (human) and 86 nM (mouse), and improves metabolic disorders in diet-induced obese mice. " |
Effect: | modulate |
Effect Info: | Emodin significantly inhibits the lung metastasis of breast cancer by suppressing STAT6 phosphorylation. |
Note: | |
Score: | 4.0 |
Pubmed(PMID): | 25311112 |
Sentence Index: | 25311112_9-10 |
Sentence: | "In vitro experiments demonstrated that Emodin decreased the migration of macrophages toward tumor cell-conditioned medium (TCM) and inhibited macrophage M2 polarization induced by TCM. Mechanistically, Emodin suppressed STAT6 phosphorylation and C/EBPbeta expression, two crucial signaling events in macrophage M2 polarization, in macrophages treated with IL-4 or TCM." |
Sequence & Structure:
MSLWGLVSKMPPEKVQRLYVDFPQHLRHLLGDWLESQPWEFLVGSDAFCCNLASALLSDTVQHLQASVGEQGEGSTILQHISTLESIYQRDPLKLVATFRQILQGEKKAVMEQFRHLPMPFHWKQEELKFKTGLRRLQHRVGEIHLLREALQKGAEAGQVSLHSLIETPANGTGPSEALAMLLQETTGELEAAKALVLKRIQIWKRQQQLAGNGAPFEESLAPLQERCESLVDIYSQLQQEVGAAGGELEPKTRASLTGRLDEVLRTLVTSCFLVEKQPPQVLKTQTKFQAGVRFLLGLRFLGAPAKPPLVRADMVTEKQARELSVPQGPGAGAESTGEIINNTVPLENSIPGNCCSALFKNLLLKKIKRCERKGTESVTEEKCAVLFSASFTLGPGKLPIQLQALSLPLVVIVHGNQDNNAKATILWDNAFSEMDRVPFVVAERVPWEKMCETLNLKFMAEVGTNRGLLPEHFLFLAQKIFNDNSLSMEAFQHRSVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMGKDGRGYVPATIKMTVERDQPLPTPELQMPTMVPSYDLGMAPDSSMSMQLGPDMVPQVYPPHSHSIPPYQGLSPEESVNVLSAFQEPHLQMPPSLGQMSLPFDQPHPQGLLPCQPQEHAVSSPDPLLCSDVTMVEDSCLSQPVTAFPQGTWIGEDIFPPLLPPTEQDLTKLLLEGQGESGGGSLGAQPLLQPSHYGQSGISMSHMDLRANPSW
Select PDB:
No data.
Protein Tractability:
source: Open TargetsPTM Intensity:
source: CPTACNo data.
PTM-Disease Association:
source: PTMDResidue | Position | State | Disease | Class | PMID |
---|---|---|---|---|---|
Y | 641 | U | Ductal carcinoma in situ | Phosphorylation | 23562473 |
Y | 641 | U | Lymphoma | Phosphorylation | 34388250 |
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.