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P01275

- GLUC_HUMAN

UniProt

P01275 - GLUC_HUMAN

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Protein
Glucagon
Gene
GCG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications
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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei52 – 532Cleavage; by PCSK2
Sitei83 – 842Cleavage; by PCSK1 and PCSK2
Sitei91 – 922Cleavage; by PCSK1
Sitei97 – 982Cleavage; by PCSK1
Sitei130 – 1312Cleavage; by PCSK1
Sitei145 – 1462Cleavage; by PCSK1

GO - Molecular functioni

  1. glucagon receptor binding Source: RefGenome
  2. hormone activity Source: RefGenome
  3. identical protein binding Source: IntAct
  4. protein binding Source: IntAct
  5. receptor binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
  2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RefGenome
  3. cell proliferation Source: ProtInc
  4. cellular protein metabolic process Source: Reactome
  5. cellular response to glucagon stimulus Source: Reactome
  6. energy reserve metabolic process Source: Reactome
  7. feeding behavior Source: ProtInc
  8. negative regulation of apoptotic process Source: RefGenome
  9. negative regulation of execution phase of apoptosis Source: Ensembl
  10. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  11. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  12. positive regulation of cAMP biosynthetic process Source: Ensembl
  13. positive regulation of calcium ion import Source: Ensembl
  14. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RefGenome
  15. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  16. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
  17. positive regulation of protein binding Source: Ensembl
  18. positive regulation of protein kinase activity Source: Ensembl
  19. protein kinase A signaling Source: RefGenome
  20. regulation of insulin secretion Source: Reactome
  21. response to starvation Source: RefGenome
  22. signal transduction Source: ProtInc
  23. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_1665. Glucagon signaling in metabolic regulation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18283. G alpha (q) signalling events.
REACT_18377. Glucagon-type ligand receptors.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_19327. G alpha (s) signalling events.
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

Names & Taxonomyi

Protein namesi
Recommended name:
Glucagon
Cleaved into the following 8 chains:
Oxyntomodulin
Short name:
OXM
Short name:
OXY
Glucagon-like peptide 1
Short name:
GLP-1
Alternative name(s):
Incretin hormone
Glucagon-like peptide 1(7-37)
Short name:
GLP-1(7-37)
Glucagon-like peptide 1(7-36)
Short name:
GLP-1(7-36)
Glucagon-like peptide 2
Short name:
GLP-2
Gene namesi
Name:GCG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4191. GCG.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: RefGenome
  4. plasma membrane Source: Reactome
  5. secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Available under the names Glucagon (Eli Lilly) and GlucaGen or Glucagon Novo Nordisk (Novo Nordisk). Used to treat severe hypoglycemia in insulin-dependent diabetics.

Organism-specific databases

PharmGKBiPA28606.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020
Add
BLAST
Peptidei21 – 8969Glicentin By similarity
PRO_0000011253Add
BLAST
Peptidei21 – 5030Glicentin-related polypeptide By similarity1 Publication
PRO_0000011254Add
BLAST
Peptidei53 – 8937Oxyntomodulin By similarity
PRO_0000011255Add
BLAST
Peptidei53 – 8129Glucagon1 Publication
PRO_0000011256Add
BLAST
Propeptidei84 – 896
PRO_0000011257
Peptidei92 – 12837Glucagon-like peptide 1
PRO_0000011258Add
BLAST
Peptidei98 – 12831Glucagon-like peptide 1(7-37)
PRO_0000011259Add
BLAST
Peptidei98 – 12730Glucagon-like peptide 1(7-36)1 Publication
PRO_0000011260Add
BLAST
Propeptidei131 – 14515 By similarity
PRO_0000011261Add
BLAST
Peptidei146 – 17833Glucagon-like peptide 2 By similarity
PRO_0000011262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271Arginine amide1 Publication

Post-translational modificationi

Proglucagon is post-translationally processed in a tissue-specific manner in pancreatic A cells and intestinal L cells. In pancreatic A cells, the major bioactive hormone is glucagon cleaved by PCSK2/PC2. In the intestinal L cells PCSK1/PC1 liberates GLP-1, GLP-2, glicentin and oxyntomodulin. GLP-1 is further N-terminally truncated by post-translational processing in the intestinal L cells resulting in GLP-1(7-37) GLP-1-(7-36)amide. The C-terminal amidation is neither important for the metabolism of GLP-1 nor for its effects on the endocrine pancreas.2 Publications

Keywords - PTMi

Amidation, Cleavage on pair of basic residues

Proteomic databases

PaxDbiP01275.
PRIDEiP01275.

PTM databases

PhosphoSiteiP01275.

Miscellaneous databases

PMAP-CutDBP01275.

Expressioni

Tissue specificityi

Glucagon is secreted in the A cells of the islets of Langerhans. GLP-1, GLP-2, oxyntomodulin and glicentin are secreted from enteroendocrine cells throughout the gastrointestinal tract. GLP-1 and GLP-2 are also secreted in selected neurons in the brain.

Inductioni

Glucagon release is stimulated by hypoglycemia and inhibited by hyperglycemia, insulin, and somatostatin. GLP-1 and GLP-2 are induced in response to nutrient ingestion.

Gene expression databases

BgeeiP01275.
CleanExiHS_GCG.
GenevestigatoriP01275.

Organism-specific databases

HPAiCAB000040.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7629173,EBI-7629173
DPP4P274874EBI-7629173,EBI-2871277
FAPQ128844EBI-7629173,EBI-4319803

Protein-protein interaction databases

BioGridi108911. 2 interactions.
DIPiDIP-46470N.
IntActiP01275. 4 interactions.
MINTiMINT-8090511.
STRINGi9606.ENSP00000387662.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni55 – 573
Turni59 – 624
Beta strandi63 – 653
Helixi68 – 703
Turni71 – 733
Beta strandi76 – 783
Helixi104 – 12421
Helixi150 – 1534
Helixi154 – 1563
Helixi157 – 17216
Turni173 – 1775

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BH0X-ray3.00A53-81[»]
1D0RNMR-A98-127[»]
1NAUNMR-A59-81[»]
2G49X-ray2.50C/D53-81[»]
2L63NMR-A146-178[»]
2L64NMR-A146-178[»]
2M5PNMR-X53-81[»]
2M5QNMR-X53-81[»]
3IOLX-ray2.10B98-128[»]
4APDNMR-A98-128[»]
ProteinModelPortaliP01275.
SMRiP01275. Positions 53-81, 98-127, 146-178.

Miscellaneous databases

EvolutionaryTraceiP01275.

Family & Domainsi

Sequence similaritiesi

Belongs to the glucagon family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42743.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
KOiK05259.
OMAiLNDPDQM.
OrthoDBiEOG7WMCM1.
PhylomeDBiP01275.
TreeFamiTF332333.

Family and domain databases

InterProiIPR015550. Glucagon-like.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418. PTHR11418. 1 hit.
PfamiPF00123. Hormone_2. 3 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 3 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01275-1 [UniParc]FASTAAdd to Basket

« Hide

MKSIYFVAGL FVMLVQGSWQ RSLQDTEEKS RSFSASQADP LSDPDQMNED    50
KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE 100
GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIVE ELGRRHADGS 150
FSDEMNTILD NLAARDFINW LIQTKITDRK 180
Length:180
Mass (Da):20,909
Last modified:February 6, 2007 - v3
Checksum:i7A99EEC629B2862C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151A → V.
Corresponds to variant rs5650 [ dbSNP | Ensembl ].
VAR_014596

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821K → N in CAA27627. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04040 mRNA. Translation: AAA52567.1.
X03991 Genomic DNA. Translation: CAA27627.1.
V01515 Genomic DNA. Translation: CAA24759.1.
BT006813 mRNA. Translation: AAP35459.1.
AC007750 Genomic DNA. Translation: AAY24204.1.
BC005278 mRNA. Translation: AAH05278.1.
CCDSiCCDS46439.1.
PIRiA24377. GCHU.
RefSeqiNP_002045.1. NM_002054.4.
UniGeneiHs.516494.
Hs.741174.

Genome annotation databases

EnsembliENST00000375497; ENSP00000364647; ENSG00000115263.
ENST00000418842; ENSP00000387662; ENSG00000115263.
GeneIDi2641.
KEGGihsa:2641.
UCSCiuc002ucc.4. human.

Polymorphism databases

DMDMi125987831.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Glucagon at Eli Lilly

Clinical information on Eli Lilly glucagon products

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04040 mRNA. Translation: AAA52567.1 .
X03991 Genomic DNA. Translation: CAA27627.1 .
V01515 Genomic DNA. Translation: CAA24759.1 .
BT006813 mRNA. Translation: AAP35459.1 .
AC007750 Genomic DNA. Translation: AAY24204.1 .
BC005278 mRNA. Translation: AAH05278.1 .
CCDSi CCDS46439.1.
PIRi A24377. GCHU.
RefSeqi NP_002045.1. NM_002054.4.
UniGenei Hs.516494.
Hs.741174.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BH0 X-ray 3.00 A 53-81 [» ]
1D0R NMR - A 98-127 [» ]
1NAU NMR - A 59-81 [» ]
2G49 X-ray 2.50 C/D 53-81 [» ]
2L63 NMR - A 146-178 [» ]
2L64 NMR - A 146-178 [» ]
2M5P NMR - X 53-81 [» ]
2M5Q NMR - X 53-81 [» ]
3IOL X-ray 2.10 B 98-128 [» ]
4APD NMR - A 98-128 [» ]
ProteinModelPortali P01275.
SMRi P01275. Positions 53-81, 98-127, 146-178.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108911. 2 interactions.
DIPi DIP-46470N.
IntActi P01275. 4 interactions.
MINTi MINT-8090511.
STRINGi 9606.ENSP00000387662.

Chemistry

BindingDBi P01275.
ChEMBLi CHEMBL5736.
DrugBanki DB01276. Exenatide.
DB00692. Phentolamine.

PTM databases

PhosphoSitei P01275.

Polymorphism databases

DMDMi 125987831.

Proteomic databases

PaxDbi P01275.
PRIDEi P01275.

Protocols and materials databases

DNASUi 2641.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375497 ; ENSP00000364647 ; ENSG00000115263 .
ENST00000418842 ; ENSP00000387662 ; ENSG00000115263 .
GeneIDi 2641.
KEGGi hsa:2641.
UCSCi uc002ucc.4. human.

Organism-specific databases

CTDi 2641.
GeneCardsi GC02M162963.
HGNCi HGNC:4191. GCG.
HPAi CAB000040.
MIMi 138030. gene.
neXtProti NX_P01275.
PharmGKBi PA28606.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42743.
HOGENOMi HOG000231876.
HOVERGENi HBG003010.
KOi K05259.
OMAi LNDPDQM.
OrthoDBi EOG7WMCM1.
PhylomeDBi P01275.
TreeFami TF332333.

Enzyme and pathway databases

Reactomei REACT_1665. Glucagon signaling in metabolic regulation.
REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18283. G alpha (q) signalling events.
REACT_18377. Glucagon-type ligand receptors.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_19327. G alpha (s) signalling events.
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

Miscellaneous databases

ChiTaRSi GCG. human.
EvolutionaryTracei P01275.
GeneWikii Glucagon.
GenomeRNAii 2641.
NextBioi 10412.
PMAP-CutDB P01275.
PROi P01275.
SOURCEi Search...

Gene expression databases

Bgeei P01275.
CleanExi HS_GCG.
Genevestigatori P01275.

Family and domain databases

InterProi IPR015550. Glucagon-like.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view ]
PANTHERi PTHR11418. PTHR11418. 1 hit.
Pfami PF00123. Hormone_2. 3 hits.
[Graphical view ]
PRINTSi PR00275. GLUCAGON.
SMARTi SM00070. GLUCA. 3 hits.
[Graphical view ]
PROSITEi PS00260. GLUCAGON. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Glucagon gene expression in vertebrate brain."
    Drucker D.J., Asa S.
    J. Biol. Chem. 263:13475-13478(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Exon duplication and divergence in the human preproglucagon gene."
    Bell G.I., Sanchez-Pescador R., Laybourn P.J., Najarian R.C.
    Nature 304:368-371(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  7. Cited for: PROTEIN SEQUENCE OF 53-81.
  8. "Complete sequences of glucagon-like peptide-1 from human and pig small intestine."
    Orskov C., Bersani M., Johnsen A.H., Hoejrup P., Holst J.J.
    J. Biol. Chem. 264:12826-12829(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 98-127, AMIDATION AT ARG-127.
  9. "Biological effects and metabolic rates of glucagonlike peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable."
    Orskov C., Wettergren A., Holst J.J.
    Diabetes 42:658-661(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF GLP1 BIOACTIVE FORMS.
  10. Cited for: FUNCTION OF OXYNTOMODULIN.
  11. "Postnatal and postprandial changes in plasma concentrations of glicentin in term and preterm infants."
    Tadokoro R., Shimizu T., Hosaka A., Kaneko N., Satoh Y., Yamashiro Y.
    Acta Paediatr. 92:1175-1179(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF GLICENTIN.
  12. "Role of the prohormone convertase PC2 in the processing of proglucagon to glucagon."
    Rouille Y., Bianchi M., Irminger J.C., Halban P.A.
    FEBS Lett. 413:119-123(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING BY PCSK2.
  13. "Expression, purification, and PC1-mediated processing of human proglucagon, glicentin, and major proglucagon fragment."
    Bonic A., Mackin R.B.
    Protein Expr. Purif. 28:15-24(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING BY PCSK1.
  14. "Direct and indirect mechanisms regulating secretion of glucagon-like peptide-1 and glucagon-like peptide-2."
    Brubaker P.L., Anini Y.
    Can. J. Physiol. Pharmacol. 81:1005-1012(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. "Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis."
    Drucker D.J.
    Mol. Endocrinol. 17:161-171(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Glucagon and regulation of glucose metabolism."
    Jiang G., Zhang B.B.
    Am. J. Physiol. 284:E671-E678(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. Cited for: REVIEW.
  18. Cited for: REVIEW.
  19. "Structure-function studies on positions 17, 18, and 21 replacement analogues of glucagon: the importance of charged residues and salt bridges in glucagon biological activity."
    Sturm N.S., Lin Y., Burley S.K., Krstenansky J.L., Ahn J.-M., Azizeh B.Y., Trivedi D., Hruby V.J.
    J. Med. Chem. 41:2693-2700(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 53-81.
  20. "NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer."
    Chang X., Keller D., O'Donoghue S.I., Led J.J.
    FEBS Lett. 515:165-170(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 98-127.
  21. "NMR solution structure of the glucagon antagonist [desHis1, desPhe6, Glu9]glucagon amide in the presence of perdeuterated dodecylphosphocholine micelles."
    Ying J., Ahn J.-M., Jacobsen N.E., Brown M.F., Hruby V.J.
    Biochemistry 42:2825-2835(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF GLUCAGON ANTAGONIST.

Entry informationi

Entry nameiGLUC_HUMAN
AccessioniPrimary (citable) accession number: P01275
Secondary accession number(s): A6NN65, Q53TP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In the glucagon antagonist, His-53 and Phe-58 are missing. This antagonist has been successfully utilized to reduce glucose concentration in vivo.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi