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Protein

Glucagon

Gene

GCG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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.

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

  • glucagon receptor binding Source: GO_Central
  • hormone activity Source: GO_Central
  • identical protein binding Source: IntAct
  • receptor binding Source: ProtInc

GO - Biological processi

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4191. GCG.

Subcellular locationi

GO - Cellular componenti

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.

Polymorphism and mutation databases

BioMutaiGCG.
DMDMi125987831.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Peptidei21 – 8969GlicentinBy similarityPRO_0000011253Add
BLAST
Peptidei21 – 5030Glicentin-related polypeptideBy similarityPRO_0000011254Add
BLAST
Peptidei53 – 8937OxyntomodulinBy similarityPRO_0000011255Add
BLAST
Peptidei53 – 8129GlucagonPRO_0000011256Add
BLAST
Propeptidei84 – 896PRO_0000011257
Peptidei92 – 12837Glucagon-like peptide 1PRO_0000011258Add
BLAST
Peptidei98 – 12831Glucagon-like peptide 1(7-37)PRO_0000011259Add
BLAST
Peptidei98 – 12730Glucagon-like peptide 1(7-36)PRO_0000011260Add
BLAST
Propeptidei131 – 14515By similarityPRO_0000011261Add
BLAST
Peptidei146 – 17833Glucagon-like peptide 2By similarityPRO_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.3 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.
GenevisibleiP01275. HS.

Organism-specific databases

HPAiCAB000040.
HPA036760.
HPA036761.

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

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni55 – 573Combined sources
Turni59 – 624Combined sources
Beta strandi63 – 653Combined sources
Helixi68 – 703Combined sources
Turni71 – 733Combined sources
Beta strandi76 – 783Combined sources
Helixi104 – 12421Combined sources
Helixi150 – 1534Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 17216Combined sources
Turni173 – 1775Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01275.

Family & Domainsi

Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42743.
GeneTreeiENSGT00390000005372.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
InParanoidiP01275.
KOiK05259.
OMAiKMKSIYF.
OrthoDBiEOG7WMCM1.
PhylomeDBiP01275.
TreeFamiTF332333.

Family and domain databases

InterProiIPR015550. Glucagon.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418:SF0. PTHR11418:SF0. 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

        10         20         30         40         50
MKSIYFVAGL FVMLVQGSWQ RSLQDTEEKS RSFSASQADP LSDPDQMNED
60 70 80 90 100
KRHSQGTFTS DYSKYLDSRR AQDFVQWLMN TKRNRNNIAK RHDEFERHAE
110 120 130 140 150
GTFTSDVSSY LEGQAAKEFI AWLVKGRGRR DFPEEVAIVE ELGRRHADGS
160 170 180
FSDEMNTILD NLAARDFINW LIQTKITDRK
Length:180
Mass (Da):20,909
Last modified:February 6, 2007 - v3
Checksum:i7A99EEC629B2862C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821K → N in CAA27627 (PubMed:3725587).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP01275.
ChEMBLiCHEMBL5736.

PTM databases

PhosphoSiteiP01275.

Polymorphism and mutation databases

BioMutaiGCG.
DMDMi125987831.

Proteomic databases

PaxDbiP01275.
PRIDEiP01275.

Protocols and materials databases

DNASUi2641.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2641.
GeneCardsiGC02M162963.
HGNCiHGNC:4191. GCG.
HPAiCAB000040.
HPA036760.
HPA036761.
MIMi138030. gene.
neXtProtiNX_P01275.
PharmGKBiPA28606.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42743.
GeneTreeiENSGT00390000005372.
HOGENOMiHOG000231876.
HOVERGENiHBG003010.
InParanoidiP01275.
KOiK05259.
OMAiKMKSIYF.
OrthoDBiEOG7WMCM1.
PhylomeDBiP01275.
TreeFamiTF332333.

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).

Miscellaneous databases

ChiTaRSiGCG. human.
EvolutionaryTraceiP01275.
GeneWikiiGlucagon.
GenomeRNAii2641.
NextBioi10412.
PMAP-CutDBP01275.
PROiP01275.
SOURCEiSearch...

Gene expression databases

BgeeiP01275.
CleanExiHS_GCG.
GenevisibleiP01275. HS.

Family and domain databases

InterProiIPR015550. Glucagon.
IPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PANTHERiPTHR11418:SF0. PTHR11418:SF0. 1 hit.
PfamiPF00123. Hormone_2. 3 hits.
[Graphical view]
PRINTSiPR00275. GLUCAGON.
SMARTiSM00070. GLUCA. 3 hits.
[Graphical view]
PROSITEiPS00260. GLUCAGON. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: July 22, 2015
This is version 172 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.