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P43220

- GLP1R_HUMAN

UniProt

P43220 - GLP1R_HUMAN

Protein

Glucagon-like peptide 1 receptor

Gene

GLP1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

    GO - Molecular functioni

    1. glucagon receptor activity Source: InterPro
    2. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: ProtInc
    2. cAMP-mediated signaling Source: UniProtKB
    3. energy reserve metabolic process Source: Reactome
    4. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    5. regulation of insulin secretion Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Protein family/group databases

    TCDBi9.A.14.4.6. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucagon-like peptide 1 receptor
    Short name:
    GLP-1 receptor
    Short name:
    GLP-1-R
    Short name:
    GLP-1R
    Gene namesi
    Name:GLP1R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4324. GLP1R.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: ProtInc
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 463440Glucagon-like peptide 1 receptorPRO_0000012835Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 71
    Disulfide bondi62 ↔ 104
    Glycosylationi63 – 631N-linked (GlcNAc...)1 Publication
    Glycosylationi82 – 821N-linked (GlcNAc...)1 Publication
    Disulfide bondi85 ↔ 126
    Glycosylationi115 – 1151N-linked (GlcNAc...)1 Publication
    Disulfide bondi226 ↔ 296
    Modified residuei341 – 3411ADP-ribosylcysteine1 Publication
    Modified residuei348 – 3481ADP-ribosylarginine1 Publication

    Post-translational modificationi

    N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP43220.
    PRIDEiP43220.

    PTM databases

    PhosphoSiteiP43220.

    Expressioni

    Gene expression databases

    BgeeiP43220.
    CleanExiHS_GLP1R.
    GenevestigatoriP43220.

    Interactioni

    Subunit structurei

    May form homodimers and heterodimers with GIPR.2 Publications

    Protein-protein interaction databases

    BioGridi109002. 43 interactions.
    DIPiDIP-29980N.
    MINTiMINT-1217566.
    STRINGi9606.ENSP00000362353.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 5221
    Beta strandi57 – 593
    Beta strandi79 – 846
    Helixi92 – 943
    Beta strandi99 – 1046
    Beta strandi108 – 1103
    Beta strandi114 – 1174
    Helixi124 – 1263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3C59X-ray2.30A24-145[»]
    3C5TX-ray2.10A24-145[»]
    3IOLX-ray2.10A24-145[»]
    ProteinModelPortaliP43220.
    SMRiP43220. Positions 28-412.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43220.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 139116ExtracellularBy similarityAdd
    BLAST
    Topological domaini165 – 17612CytoplasmicBy similarityAdd
    BLAST
    Topological domaini202 – 22726ExtracellularBy similarityAdd
    BLAST
    Topological domaini252 – 26514CytoplasmicBy similarityAdd
    BLAST
    Topological domaini288 – 30518ExtracellularBy similarityAdd
    BLAST
    Topological domaini329 – 35224CytoplasmicBy similarityAdd
    BLAST
    Topological domaini372 – 38312ExtracellularBy similarityAdd
    BLAST
    Topological domaini405 – 46359CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei140 – 16425Helical; Name=1By similarityAdd
    BLAST
    Transmembranei177 – 20125Helical; Name=2By similarityAdd
    BLAST
    Transmembranei228 – 25124Helical; Name=3By similarityAdd
    BLAST
    Transmembranei266 – 28722Helical; Name=4By similarityAdd
    BLAST
    Transmembranei306 – 32823Helical; Name=5By similarityAdd
    BLAST
    Transmembranei353 – 37119Helical; Name=6By similarityAdd
    BLAST
    Transmembranei384 – 40421Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG263329.
    HOGENOMiHOG000008250.
    HOVERGENiHBG008318.
    InParanoidiP43220.
    KOiK04581.
    OMAiCIVVSKL.
    OrthoDBiEOG7TF78W.
    PhylomeDBiP43220.
    TreeFamiTF315710.

    Family and domain databases

    InterProiIPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR003290. GPCR_2_GLP1/glucagon_rcpt.
    IPR003292. GPCR_2_GLP1_rcpt.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    [Graphical view]
    PfamiPF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view]
    PRINTSiPR01353. GLUCAGNFAMLY.
    PR01355. GLUCAGNLIKER.
    PR00249. GPCRSECRETIN.
    SMARTiSM00008. HormR. 1 hit.
    [Graphical view]
    PROSITEiPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P43220-1 [UniParc]FASTAAdd to Basket

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    MAGAPGPLRL ALLLLGMVGR AGPRPQGATV SLWETVQKWR EYRRQCQRSL    50
    TEDPPPATDL FCNRTFDEYA CWPDGEPGSF VNVSCPWYLP WASSVPQGHV 100
    YRFCTAEGLW LQKDNSSLPW RDLSECEESK RGERSSPEEQ LLFLYIIYTV 150
    GYALSFSALV IASAILLGFR HLHCTRNYIH LNLFASFILR ALSVFIKDAA 200
    LKWMYSTAAQ QHQWDGLLSY QDSLSCRLVF LLMQYCVAAN YYWLLVEGVY 250
    LYTLLAFSVL SEQWIFRLYV SIGWGVPLLF VVPWGIVKYL YEDEGCWTRN 300
    SNMNYWLIIR LPILFAIGVN FLIFVRVICI VVSKLKANLM CKTDIKCRLA 350
    KSTLTLIPLL GTHEVIFAFV MDEHARGTLR FIKLFTELSF TSFQGLMVAI 400
    LYCFVNNEVQ LEFRKSWERW RLEHLHIQRD SSMKPLKCPT SSLSSGATAG 450
    SSMYTATCQA SCS 463
    Length:463
    Mass (Da):53,026
    Last modified:November 2, 2010 - v2
    Checksum:iEE7C0EAE29931F5D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121L → V in AAA03614. (PubMed:8405712)Curated
    Sequence conflicti12 – 121L → V no nucleotide entry (PubMed:7517895)Curated
    Sequence conflicti12 – 121L → V in AAB64013. (PubMed:9213353)Curated
    Sequence conflicti136 – 1372SP → WG in AAA03614. (PubMed:8405712)Curated
    Sequence conflicti137 – 1371P → R no nucleotide entry (PubMed:7517895)Curated
    Sequence conflicti151 – 1511G → A in AAA03614. (PubMed:8405712)Curated
    Sequence conflicti221 – 2211Q → L in AAA63787. (PubMed:7843404)Curated
    Sequence conflicti289 – 2891Y → I in AAA03614. (PubMed:8405712)Curated
    Sequence conflicti316 – 3161A → G in AAA62471. (PubMed:8404634)Curated
    Sequence conflicti316 – 3161A → G in AAC50050. (PubMed:8404634)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71P → L.1 Publication
    Corresponds to variant rs10305420 [ dbSNP | Ensembl ].
    VAR_018924
    Natural varianti20 – 201R → K.1 Publication
    Corresponds to variant rs10305421 [ dbSNP | Ensembl ].
    VAR_018925
    Natural varianti44 – 441R → H.1 Publication
    Corresponds to variant rs2295006 [ dbSNP | Ensembl ].
    VAR_018926
    Natural varianti131 – 1311R → Q.1 Publication
    Corresponds to variant rs3765467 [ dbSNP | Ensembl ].
    VAR_018927
    Natural varianti168 – 1681G → S.1 Publication
    Corresponds to variant rs6923761 [ dbSNP | Ensembl ].
    VAR_018928
    Natural varianti260 – 2601L → F.6 Publications
    Corresponds to variant rs1042044 [ dbSNP | Ensembl ].
    VAR_015098
    Natural varianti316 – 3161A → T.1 Publication
    Corresponds to variant rs10305492 [ dbSNP | Ensembl ].
    VAR_018929
    Natural varianti333 – 3331S → C.1 Publication
    Corresponds to variant rs10305493 [ dbSNP | Ensembl ].
    VAR_018930
    Natural varianti421 – 4211R → Q.1 Publication
    Corresponds to variant rs10305510 [ dbSNP | Ensembl ].
    VAR_018931

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01104 mRNA. Translation: AAA03614.1.
    U01157 mRNA. Translation: AAA62471.1.
    U01156 mRNA. Translation: AAC50050.1.
    L23503 mRNA. Translation: AAA17021.1.
    U10037 mRNA. Translation: AAA63787.1.
    AB065685 Genomic DNA. Translation: BAC05908.1.
    AY439112 Genomic DNA. Translation: AAR05444.1.
    AL035690 Genomic DNA. Translation: CAB71177.1.
    BC112126 mRNA. Translation: AAI12127.1.
    BC113493 mRNA. Translation: AAI13494.1.
    U66062 Genomic DNA. Translation: AAB64013.1.
    CCDSiCCDS4839.1.
    PIRiI84494.
    S71624.
    RefSeqiNP_002053.3. NM_002062.3.
    XP_006715128.1. XM_006715065.1.
    UniGeneiHs.389103.

    Genome annotation databases

    EnsembliENST00000373256; ENSP00000362353; ENSG00000112164.
    GeneIDi2740.
    KEGGihsa:2740.
    UCSCiuc003ooj.4. human.

    Polymorphism databases

    DMDMi311033387.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Glucagon-like peptide 1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01104 mRNA. Translation: AAA03614.1 .
    U01157 mRNA. Translation: AAA62471.1 .
    U01156 mRNA. Translation: AAC50050.1 .
    L23503 mRNA. Translation: AAA17021.1 .
    U10037 mRNA. Translation: AAA63787.1 .
    AB065685 Genomic DNA. Translation: BAC05908.1 .
    AY439112 Genomic DNA. Translation: AAR05444.1 .
    AL035690 Genomic DNA. Translation: CAB71177.1 .
    BC112126 mRNA. Translation: AAI12127.1 .
    BC113493 mRNA. Translation: AAI13494.1 .
    U66062 Genomic DNA. Translation: AAB64013.1 .
    CCDSi CCDS4839.1.
    PIRi I84494.
    S71624.
    RefSeqi NP_002053.3. NM_002062.3.
    XP_006715128.1. XM_006715065.1.
    UniGenei Hs.389103.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3C59 X-ray 2.30 A 24-145 [» ]
    3C5T X-ray 2.10 A 24-145 [» ]
    3IOL X-ray 2.10 A 24-145 [» ]
    ProteinModelPortali P43220.
    SMRi P43220. Positions 28-412.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109002. 43 interactions.
    DIPi DIP-29980N.
    MINTi MINT-1217566.
    STRINGi 9606.ENSP00000362353.

    Chemistry

    BindingDBi P43220.
    ChEMBLi CHEMBL1784.
    DrugBanki DB01276. Exenatide.
    DB00040. Glucagon recombinant.
    GuidetoPHARMACOLOGYi 249.

    Protein family/group databases

    TCDBi 9.A.14.4.6. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei P43220.

    Polymorphism databases

    DMDMi 311033387.

    Proteomic databases

    PaxDbi P43220.
    PRIDEi P43220.

    Protocols and materials databases

    DNASUi 2740.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373256 ; ENSP00000362353 ; ENSG00000112164 .
    GeneIDi 2740.
    KEGGi hsa:2740.
    UCSCi uc003ooj.4. human.

    Organism-specific databases

    CTDi 2740.
    GeneCardsi GC06P039063.
    H-InvDB HIX0095000.
    HIX0200932.
    HGNCi HGNC:4324. GLP1R.
    MIMi 138032. gene.
    neXtProti NX_P43220.
    PharmGKBi PA28725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263329.
    HOGENOMi HOG000008250.
    HOVERGENi HBG008318.
    InParanoidi P43220.
    KOi K04581.
    OMAi CIVVSKL.
    OrthoDBi EOG7TF78W.
    PhylomeDBi P43220.
    TreeFami TF315710.

    Enzyme and pathway databases

    Reactomei REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P43220.
    GeneWikii Glucagon-like_peptide_1_receptor.
    GenomeRNAii 2740.
    NextBioi 10800.
    PROi P43220.
    SOURCEi Search...

    Gene expression databases

    Bgeei P43220.
    CleanExi HS_GLP1R.
    Genevestigatori P43220.

    Family and domain databases

    InterProi IPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR003290. GPCR_2_GLP1/glucagon_rcpt.
    IPR003292. GPCR_2_GLP1_rcpt.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    [Graphical view ]
    Pfami PF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view ]
    PRINTSi PR01353. GLUCAGNFAMLY.
    PR01355. GLUCAGNLIKER.
    PR00249. GPCRSECRETIN.
    SMARTi SM00008. HormR. 1 hit.
    [Graphical view ]
    PROSITEi PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and functional expression of the human islet GLP-1 receptor. Demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist of the receptor."
      Thorens B., Porret A., Buehler L., Deng S., Morel P., Widmann C.
      Diabetes 42:1678-1682(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-260.
      Tissue: Pancreatic islet.
    2. "Cloning and functional expression of the human glucagon-like peptide-1 (GLP-1) receptor."
      Dillon J.S., Tanizawa Y., Wheeler M.B., Leng X., Ligon B.B., Rabin D.U., Yoo-Warren H., Permutt M., Boyd A.E.
      Endocrinology 133:1907-1910(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-260.
      Tissue: Pancreas.
    3. "Cloning and functional expression of a human glucagon-like peptide-1 receptor."
      Graziano M.P., Hey P.J., Borkowski D., Chicchi G.C., Strader C.D.
      Biochem. Biophys. Res. Commun. 196:141-146(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-260.
      Tissue: Gastric carcinoma.
    4. "Signal transduction of the GLP-1-receptor cloned from a human insulinoma."
      van Eyll B., Lankat-Buttgereit B., Bode H.P., Goeke R., Goeke B.
      FEBS Lett. 348:7-13(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Insulinoma.
    5. "Tissue-specific expression of the human receptor for glucagon-like peptide-I: brain, heart and pancreatic forms have the same deduced amino acid sequences."
      Wei Y., Mojsov S.
      FEBS Lett. 358:219-224(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-260.
      Tissue: Pancreas.
    6. "Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
      Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-7; LYS-20; HIS-44; GLN-131; SER-168; PHE-260; THR-316; CYS-333 AND GLN-421.
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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], VARIANT PHE-260.
    10. "Cloning and characterization of the 5' flanking sequences (promoter region) of the human GLP-1 receptor gene."
      Lankat-Buttgereit B., Goeke B.
      Peptides 18:617-624(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
      Tissue: Placenta.
    11. "Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to the activation pocket."
      Mann R.J., Al-Sabah S., de Maturana R.L., Sinfield J.K., Donnelly D.
      Peptides 31:2289-2293(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    12. "Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase."
      Dezelak M., Bavec A.
      Mol. Biol. Rep. 39:4375-4381(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION AT CYS-341 AND ARG-348.
    13. "Regulation of GIP and GLP1 receptor cell surface expression by N-glycosylation and receptor heteromerization."
      Whitaker G.M., Lynn F.C., McIntosh C.H., Accili E.A.
      PLoS ONE 7:E32675-E32675(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-63; ASN-82 AND ASN-115, SUBUNIT.
    14. "Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain."
      Runge S., Thogersen H., Madsen K., Lau J., Rudolph R.
      J. Biol. Chem. 283:11340-11347(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-145 IN COMPLEX WITH ANTAGONIST EXENDIN-4, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGLP1R_HUMAN
    AccessioniPrimary (citable) accession number: P43220
    Secondary accession number(s): Q2M229, Q99669
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3