| Id: | acc3248 |
| Group: | 2sens |
| Protein: | beta-catenin |
| Gene Symbol: | Ctnnb1 |
| Protein Id: | Q02248 |
| Protein Name: | CTNB1_MOUSE |
| PTM: | phosphorylation |
| Site: | Ser675 |
| Site Sequence: | KPQDYKKRLSVELTSSLFRTE |
| Disease Category: | Endocrine and metabolic diseases |
| Disease: | Diabetes Mellitus |
| Disease Subtype: | STZ induced diabetic mice |
| Disease Cellline: | |
| Disease Info: | |
| Drug: | GLP–1(28–36)amide |
| Drug Info: | GLP–1(28–36)amide is a drug that belongs to the GLP - 1 peptide derivative class. It may have specific physiological functions related to GLP - 1 regulation in the body. |
| Effect: | modulate |
| Effect Info: | "GLP–1(28–36)amide stimulates the phosphorylation of β - catenin at Ser(675) in INS–1 cells and rat islet cells, increases the cAMP level and PKA activity, and enhances insulin secretion." |
| Note: | |
| Score: | 4.0 |
| Pubmed(PMID): | 23571712 |
| Sentence Index: | 23571712_2-3 |
| Sentence: | "However, the effect of this nonapeptide in pancreatic beta-cells remains largely unknown. Here, we show that in a streptozotocin-induced mouse diabetes model, GLP-1(28-36)amide improved glucose disposal and increased pancreatic beta-cell mass and beta-cell proliferation." |
Sequence & Structure:
MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
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 |
|---|---|---|---|---|---|
| S | 45 | D | Esophageal carcinoma | Phosphorylation | 31934197 |
| S | 37 | P | Acute myeloid leukemia/acute myelogenous leukemia | Phosphorylation | 21156284 |
| T | 41 | P | Acute myeloid leukemia/acute myelogenous leukemia | Phosphorylation | 21156284 |
| S | 45 | U | Esophageal carcinoma | Phosphorylation | 31934197 |
| S | 552 | U | Cowden syndrome | Phosphorylation | 17237784 |
| Y | 654 | U | Idiopathic pulmonary fibrosis | Phosphorylation | 19104148 |
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.
