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UniProtKB - P01275 (GLUC_HUMAN)

Protein

Glucagon

Gene

GCG

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

Miscellaneous

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • glucagon receptor binding Source: GO_Central
  • hormone activity Source: GO_Central
  • identical protein binding Source: IntAct
  • signaling receptor binding Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHormone

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-HSA-416476 G alpha (q) signalling events
R-HSA-418555 G alpha (s) signalling events
R-HSA-420092 Glucagon-type ligand receptors
R-HSA-422085 Synthesis, secretion, and deacylation of Ghrelin

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01275

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glucagon
Cleaved into the following 8 chains:
Glicentin
Glicentin-related polypeptide
Short name:
GRPP
Oxyntomodulin
Short name:
OXM
Short name:
OXY
Glucagon
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GCG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000115263.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:4191 GCG

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		138030 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01275

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		2641

Open Targets

More...OpenTargetsi		ENSG00000115263

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28606

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5736

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		GCG

Domain mapping of disease mutations (DMDM)

More...DMDMi		125987831

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Add BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000001125321 – 89GlicentinBy similarityAdd BLAST69
PeptideiPRO_000001125421 – 50Glicentin-related polypeptideBy similarityAdd BLAST30
PeptideiPRO_000001125553 – 89OxyntomodulinBy similarityAdd BLAST37
PeptideiPRO_000001125653 – 81GlucagonAdd BLAST29
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000001125784 – 896
PeptideiPRO_000001125892 – 128Glucagon-like peptide 1Add BLAST37
PeptideiPRO_000001125998 – 128Glucagon-like peptide 1(7-37)Add BLAST31
PeptideiPRO_000001126098 – 127Glucagon-like peptide 1(7-36)Add BLAST30
PropeptideiPRO_0000011261131 – 145By similarityAdd BLAST15
PeptideiPRO_0000011262146 – 178Glucagon-like peptide 2By similarityAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei54PhosphoserineBy similarity1
Modified residuei105PhosphoserineBy similarity1
Modified residuei108PhosphoserineBy similarity1
Modified residuei127Arginine amide1 Publication1
Modified residuei150PhosphoserineBy similarity1
Modified residuei152PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei52 – 53Cleavage; by PCSK22
Sitei83 – 84Cleavage; by PCSK1 and PCSK22
Sitei91 – 92Cleavage; by PCSK12
Sitei97 – 98Cleavage; by PCSK12
Sitei130 – 131Cleavage; by PCSK12
Sitei145 – 146Cleavage; by PCSK12

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P01275

PeptideAtlas

More...PeptideAtlasi		P01275

PRoteomics IDEntifications database

More...PRIDEi		P01275

ProteomicsDB human proteome resource

More...ProteomicsDBi		51367

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01275

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P01275

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P01275

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000115263 Expressed in 66 organ(s), highest expression level in islet of Langerhans

CleanEx database of gene expression profiles

More...CleanExi		HS_GCG

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01275 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000040
HPA036760
HPA036761

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108911, 19 interactors

Database of interacting proteins

More...DIPi		DIP-46470N

Protein interaction database and analysis system

More...IntActi		P01275, 7 interactors

Molecular INTeraction database

More...MINTi		P01275

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000387662

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P01275

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1180
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P01275

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P01275

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P01275

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glucagon family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IKZ8 Eukaryota
ENOG4111VKC LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005372

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231876

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG003010

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01275

KEGG Orthology (KO)

More...KOi		K05259

Identification of Orthologs from Complete Genome Data

More...OMAi		INWLLQT

Database of Orthologous Groups

More...OrthoDBi		EOG091G0PJK

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01275

TreeFam database of animal gene trees

More...TreeFami		TF332333

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015550 Glucagon
IPR000532 Glucagon_GIP_secretin_VIP

The PANTHER Classification System

More...PANTHERi		PTHR11418 PTHR11418, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00123 Hormone_2, 3 hits

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00275 GLUCAGON

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00070 GLUCA, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00260 GLUCAGON, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7A99EEC629B2862C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti82K → N in CAA27627 (PubMed:3725587).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014596115A → V. Corresponds to variant dbSNP:rs5650Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS46439.1

Protein sequence database of the Protein Information Resource

More...PIRi		A24377 GCHU

NCBI Reference Sequences

More...RefSeqi		NP_002045.1, NM_002054.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.516494
Hs.741174

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000375497; ENSP00000364647; ENSG00000115263
ENST00000418842; ENSP00000387662; ENSG00000115263

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2641

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2641

UCSC genome browser

More...UCSCi		uc002ucc.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
4ZGMX-ray1.80B98-128[»]
5OTUX-ray1.80B/D98-128[»]
5OTVX-ray2.00B/D98-128[»]
5OTWX-ray2.10B/D98-128[»]
5OTXX-ray2.00B/D98-128[»]
5VAIelectron microscopy4.10P98-128[»]
5YQZX-ray3.00P54-81[»]
ProteinModelPortaliP01275
SMRiP01275
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108911, 19 interactors
DIPiDIP-46470N
IntActiP01275, 7 interactors
MINTiP01275
STRINGi9606.ENSP00000387662

Chemistry databases

BindingDBiP01275
ChEMBLiCHEMBL5736

PTM databases

iPTMnetiP01275
PhosphoSitePlusiP01275

Polymorphism and mutation databases

BioMutaiGCG
DMDMi125987831

Proteomic databases

PaxDbiP01275
PeptideAtlasiP01275
PRIDEiP01275
ProteomicsDBi51367

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2641
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375497; ENSP00000364647; ENSG00000115263
ENST00000418842; ENSP00000387662; ENSG00000115263
GeneIDi2641
KEGGihsa:2641
UCSCiuc002ucc.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2641
DisGeNETi2641
EuPathDBiHostDB:ENSG00000115263.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		GCG
HGNCiHGNC:4191 GCG
HPAiCAB000040
HPA036760
HPA036761
MIMi138030 gene
neXtProtiNX_P01275
OpenTargetsiENSG00000115263
PharmGKBiPA28606

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IKZ8 Eukaryota
ENOG4111VKC LUCA
GeneTreeiENSGT00390000005372
HOGENOMiHOG000231876
HOVERGENiHBG003010
InParanoidiP01275
KOiK05259
OMAiINWLLQT
OrthoDBiEOG091G0PJK
PhylomeDBiP01275
TreeFamiTF332333

Enzyme and pathway databases

ReactomeiR-HSA-163359 Glucagon signaling in metabolic regulation
R-HSA-381676 Glucagon-like Peptide-1 (GLP1) regulates insulin secretion
R-HSA-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-HSA-416476 G alpha (q) signalling events
R-HSA-418555 G alpha (s) signalling events
R-HSA-420092 Glucagon-type ligand receptors
R-HSA-422085 Synthesis, secretion, and deacylation of Ghrelin
SIGNORiP01275

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		GCG human
EvolutionaryTraceiP01275

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Glucagon

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2641
PMAP-CutDBiP01275

Protein Ontology

More...PROi		PR:P01275

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000115263 Expressed in 66 organ(s), highest expression level in islet of Langerhans
CleanExiHS_GCG
GenevisibleiP01275 HS

Family and domain databases

InterProiView protein in InterPro
IPR015550 Glucagon
IPR000532 Glucagon_GIP_secretin_VIP
PANTHERiPTHR11418 PTHR11418, 1 hit
PfamiView protein in Pfam
PF00123 Hormone_2, 3 hits
PRINTSiPR00275 GLUCAGON
SMARTiView protein in SMART
SM00070 GLUCA, 3 hits
PROSITEiView protein in PROSITE
PS00260 GLUCAGON, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLUC_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01275
Secondary accession number(s): A6NN65, Q53TP6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: November 7, 2018
This is version 200 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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