GLUC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GLUC_HUMAN
• UniProt AC: P01275
• Protein Name: Glucagon
• Gene Name: GCG
• Organism: Homo sapiens (Human).
• Sequence Length: 180
• Subcellular Localization: Secreted.
• Protein Description: Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.; GLP-1 is a potent stimulator of glucose-dependent insulin release. Play important roles on gastric motility and the suppression of plasma glucagon levels. May be involved in the suppression of satiety and stimulation of glucose disposal in peripheral tissues, independent of the actions of insulin. Have growth-promoting activities on intestinal epithelium. May also regulate the hypothalamic pituitary axis (HPA) via effects on LH, TSH, CRH, oxytocin, and vasopressin secretion. Increases islet mass through stimulation of islet neogenesis and pancreatic beta cell proliferation. Inhibits beta cell apoptosis.; GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. The gastrointestinal tract, from the stomach to the colon is the principal target for GLP-2 action. Plays a key role in nutrient homeostasis, enhancing nutrient assimilation through enhanced gastrointestinal function, as well as increasing nutrient disposal. Stimulates intestinal glucose transport and decreases mucosal permeability.; Oxyntomodulin significantly reduces food intake. Inhibits gastric emptying in humans. Suppression of gastric emptying may lead to increased gastric distension, which may contribute to satiety by causing a sensation of fullness.; Glicentin may modulate gastric acid secretion and the gastro-pyloro-duodenal activity. May play an important role in intestinal mucosal growth in the early period of life..
• Protein Sequence: MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	Phosphorylation	WQRSLQDTEEKSRSF HHHHCCCHHHHHHCC	32.84	-
30	Phosphorylation	LQDTEEKSRSFSASQ CCCHHHHHHCCCHHH	36.11	23312004
32	Phosphorylation	DTEEKSRSFSASQAD CHHHHHHCCCHHHCC	30.55	23312004
34	Phosphorylation	EEKSRSFSASQADPL HHHHHCCCHHHCCCC	28.40	26657352
36	Phosphorylation	KSRSFSASQADPLSD HHHCCCHHHCCCCCC	25.38	26657352
42	Phosphorylation	ASQADPLSDPDQMNE HHHCCCCCCHHHCCC	53.11	23312004
54	Phosphorylation	MNEDKRHSQGTFTSD CCCCHHHCCCCCCHH	34.05	25072903
57	Phosphorylation	DKRHSQGTFTSDYSK CHHHCCCCCCHHHHH	18.99	25072903
59	Phosphorylation	RHSQGTFTSDYSKYL HHCCCCCCHHHHHHH	22.11	25072903
59	O-linked_Glycosylation	RHSQGTFTSDYSKYL HHCCCCCCHHHHHHH	22.11	OGP
60	Phosphorylation	HSQGTFTSDYSKYLD HCCCCCCHHHHHHHH	30.29	25072903
62	Phosphorylation	QGTFTSDYSKYLDSR CCCCCHHHHHHHHHH	13.56	23312004
63	Phosphorylation	GTFTSDYSKYLDSRR CCCCHHHHHHHHHHH	21.58	25072903
68	Phosphorylation	DYSKYLDSRRAQDFV HHHHHHHHHHHHHHH	22.52	-
105	Phosphorylation	HAEGTFTSDVSSYLE HCCCCCCHHHHHHHC	31.65	-
108	Phosphorylation	GTFTSDVSSYLEGQA CCCCHHHHHHHCHHH	20.46	-
127	Amidation	IAWLVKGRGRRDFPE HHHHHHCCCCCCCCH	29.72	2753890
127	Arginine amide	IAWLVKGRGRRDFPE HHHHHHCCCCCCCCH	29.72	-
150	Phosphorylation	GRRHADGSFSDEMNT HHHCCCCCCCHHHHH	23.32	24670416
152	Phosphorylation	RHADGSFSDEMNTIL HCCCCCCCHHHHHHH	34.07	24670416
157	Phosphorylation	SFSDEMNTILDNLAA CCCHHHHHHHHHHHH	22.93	22617229

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of GLUC_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GLUC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GLUC_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of GLUC_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Amidation

"Complete sequences of glucagon-like peptide-1 from human and pigsmall intestine.";
Orskov C., Bersani M., Johnsen A.H., Hoejrup P., Holst J.J.;
J. Biol. Chem. 264:12826-12829(1989).
Cited for: PROTEIN SEQUENCE OF 98-127, AND AMIDATION AT ARG-127.
PubMed: 2753890