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P47871

- GLR_HUMAN

UniProt

P47871 - GLR_HUMAN

Protein

Glucagon receptor

Gene

GCGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.5 Publications

    GO - Molecular functioni

    1. glucagon receptor activity Source: UniProtKB
    2. guanyl-nucleotide exchange factor activity Source: Reactome
    3. peptide hormone binding Source: Ensembl

    GO - Biological processi

    1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
    2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
    3. cellular response to glucagon stimulus Source: UniProtKB
    4. energy reserve metabolic process Source: Reactome
    5. exocytosis Source: Ensembl
    6. generation of precursor metabolites and energy Source: ProtInc
    7. glucose homeostasis Source: UniProtKB
    8. hormone-mediated signaling pathway Source: Ensembl
    9. positive regulation of GTPase activity Source: GOC
    10. regulation of blood pressure Source: ProtInc
    11. regulation of glycogen metabolic process Source: UniProtKB
    12. response to nutrient Source: ProtInc
    13. response to starvation Source: UniProtKB
    14. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_1665. Glucagon signaling in metabolic regulation.
    REACT_18283. G alpha (q) signalling events.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucagon receptor
    Short name:
    GL-R
    Gene namesi
    Name:GCGR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4192. GCGR.

    Subcellular locationi

    Cell membrane 4 Publications; Multi-pass membrane protein 4 Publications
    Note: Is rapidly internalized after ligand-binding.

    GO - Cellular componenti

    1. endosome Source: Ensembl
    2. integral component of membrane Source: ProtInc
    3. integral component of plasma membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi36 – 361W → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi63 – 631D → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi65 – 651Y → A: Strongly reduced affinity for glucagon. Increased constitutive signaling via G-proteins. 1 Publication
    Mutagenesisi113 – 1131Q → A or N: No effect on affinity for glucagon. 1 Publication
    Mutagenesisi113 – 1131Q → E: Strongly reduced affinity for glucagon. 1 Publication
    Mutagenesisi135 – 1351A → P: Abolishes glucagon binding. 1 Publication
    Mutagenesisi145 – 1451Y → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi149 – 1491Y → A: Abolishes expression at cell surface and glucagon binding. 1 Publication
    Mutagenesisi198 – 1981L → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi201 – 2011R → D: Abolishes glucagon binding. 1 Publication
    Mutagenesisi202 – 2021Y → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi208 – 2081D → Q: Abolishes glucagon binding. 1 Publication
    Mutagenesisi215 – 2151W → L: Abolishes glucagon binding. 1 Publication
    Mutagenesisi232 – 2321Q → L: Abolishes expression at cell surface and glucagon binding. 1 Publication
    Mutagenesisi233 – 2331Y → A: Abolishes glucagon binding. Strongly reduces expression at the cell surface. 1 Publication
    Mutagenesisi286 – 2861K → L: Abolishes glucagon binding. 1 Publication
    Mutagenesisi290 – 2901E → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi294 – 2941C → A or S: Abolishes glucagon binding. 1 Publication
    Mutagenesisi295 – 2951W → A or H: Abolishes glucagon binding. 1 Publication
    Mutagenesisi304 – 3041W → Q: Abolishes glucagon binding. 1 Publication
    Mutagenesisi382 – 3821L → A: Abolishes glucagon binding. 1 Publication
    Mutagenesisi386 – 3861L → F: Abolishes glucagon binding. 1 Publication

    Keywords - Diseasei

    Diabetes mellitus

    Organism-specific databases

    PharmGKBiPA28607.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 477452Glucagon receptorPRO_0000012832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi43 ↔ 67
    Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi58 ↔ 100
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Glycosylationi78 – 781N-linked (GlcNAc...)1 Publication
    Disulfide bondi81 ↔ 121

    Post-translational modificationi

    Ligand-binding promotes phosphorylation of serine residues in the C-terminal cytoplasmic domain. Phosphorylation is important for receptor endocytosis after ligand-binding.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP47871.
    PRIDEiP47871.

    PTM databases

    PhosphoSiteiP47871.

    Expressioni

    Gene expression databases

    ArrayExpressiP47871.
    BgeeiP47871.
    CleanExiHS_GCGR.
    GenevestigatoriP47871.

    Interactioni

    Protein-protein interaction databases

    BioGridi108912. 3 interactions.
    IntActiP47871. 4 interactions.
    STRINGi9606.ENSP00000383558.

    Structurei

    Secondary structure

    1
    477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi31 – 4919
    Beta strandi54 – 585
    Beta strandi64 – 685
    Beta strandi75 – 806
    Turni86 – 905
    Beta strandi95 – 1006
    Beta strandi104 – 1063
    Helixi119 – 1213
    Helixi127 – 16337
    Beta strandi164 – 1685
    Helixi173 – 1764
    Turni177 – 1793
    Helixi180 – 19718
    Helixi218 – 2214
    Turni222 – 2265
    Helixi227 – 24721
    Helixi250 – 2545
    Helixi263 – 2664
    Helixi271 – 2733
    Helixi274 – 2774
    Helixi281 – 2899
    Beta strandi293 – 2953
    Helixi301 – 3066
    Helixi308 – 32922
    Helixi331 – 3344
    Helixi343 – 3519
    Turni352 – 3543
    Helixi357 – 3615
    Turni362 – 3687
    Helixi375 – 39016
    Helixi392 – 4009
    Turni401 – 4033
    Helixi405 – 42824

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A83X-ray1.40C412-420[»]
    3CZFX-ray1.20C412-420[»]
    4ERSX-ray2.64A28-123[»]
    4L6RX-ray3.30A123-432[»]
    4LF3X-ray2.74C/F29-123[»]
    ProteinModelPortaliP47871.
    SMRiP47871. Positions 28-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47871.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 136111ExtracellularAdd
    BLAST
    Topological domaini162 – 17312CytoplasmicAdd
    BLAST
    Topological domaini199 – 22527ExtracellularAdd
    BLAST
    Topological domaini250 – 26314CytoplasmicAdd
    BLAST
    Topological domaini286 – 30318ExtracellularAdd
    BLAST
    Topological domaini327 – 35024CytoplasmicAdd
    BLAST
    Topological domaini370 – 38112ExtracellularAdd
    BLAST
    Topological domaini403 – 47775CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei137 – 16125Helical; Name=1Add
    BLAST
    Transmembranei174 – 19825Helical; Name=2Add
    BLAST
    Transmembranei226 – 24924Helical; Name=3Add
    BLAST
    Transmembranei264 – 28522Helical; Name=4Add
    BLAST
    Transmembranei304 – 32623Helical; Name=5Add
    BLAST
    Transmembranei351 – 36919Helical; Name=6Add
    BLAST
    Transmembranei382 – 40221Helical; Name=7Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG263329.
    HOGENOMiHOG000008250.
    HOVERGENiHBG008318.
    InParanoidiP47871.
    KOiK04583.
    OrthoDBiEOG7TF78W.
    PhylomeDBiP47871.
    TreeFamiTF315710.

    Family and domain databases

    InterProiIPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR003290. GPCR_2_GLP1/glucagon_rcpt.
    IPR003291. GPCR_2_glucagon_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.
    PR01354. GLUCAGONR.
    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.

    P47871-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPCQPQRPL LLLLLLLACQ PQVPSAQVMD FLFEKWKLYG DQCHHNLSLL    50
    PPPTELVCNR TFDKYSCWPD TPANTTANIS CPWYLPWHHK VQHRFVFKRC 100
    GPDGQWVRGP RGQPWRDASQ CQMDGEEIEV QKEVAKMYSS FQVMYTVGYS 150
    LSLGALLLAL AILGGLSKLH CTRNAIHANL FASFVLKASS VLVIDGLLRT 200
    RYSQKIGDDL SVSTWLSDGA VAGCRVAAVF MQYGIVANYC WLLVEGLYLH 250
    NLLGLATLPE RSFFSLYLGI GWGAPMLFVV PWAVVKCLFE NVQCWTSNDN 300
    MGFWWILRFP VFLAILINFF IFVRIVQLLV AKLRARQMHH TDYKFRLAKS 350
    TLTLIPLLGV HEVVFAFVTD EHAQGTLRSA KLFFDLFLSS FQGLLVAVLY 400
    CFLNKEVQSE LRRRWHRWRL GKVLWEERNT SNHRASSSPG HGPPSKELQF 450
    GRGGGSQDSS AETPLAGGLP RLAESPF 477
    Length:477
    Mass (Da):54,009
    Last modified:February 1, 1996 - v1
    Checksum:iADBB477C6267AE6E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401G → S.1 Publication
    Corresponds to variant rs1801483 [ dbSNP | Ensembl ].
    VAR_003581
    Natural varianti86 – 861P → S Abolishes glucagon binding. 1 Publication
    VAR_069815
    Natural varianti114 – 1141P → A.
    Corresponds to variant rs5385 [ dbSNP | Ensembl ].
    VAR_014837
    Natural varianti303 – 3031F → C.
    Corresponds to variant rs5387 [ dbSNP | Ensembl ].
    VAR_033966

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03469 mRNA. Translation: AAC52063.1.
    L20316 mRNA. Translation: AAA53628.1.
    BC104854 mRNA. Translation: AAI04855.1.
    BC112041 mRNA. Translation: AAI12042.1.
    L24751 Genomic DNA. Translation: AAA35897.1.
    CCDSiCCDS54177.1.
    PIRiJC2041.
    RefSeqiNP_000151.1. NM_000160.4.
    XP_006722340.1. XM_006722277.1.
    UniGeneiHs.208.

    Genome annotation databases

    EnsembliENST00000400723; ENSP00000383558; ENSG00000215644.
    GeneIDi2642.
    KEGGihsa:2642.
    UCSCiuc010wuw.2. human.

    Polymorphism databases

    DMDMi1346144.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03469 mRNA. Translation: AAC52063.1 .
    L20316 mRNA. Translation: AAA53628.1 .
    BC104854 mRNA. Translation: AAI04855.1 .
    BC112041 mRNA. Translation: AAI12042.1 .
    L24751 Genomic DNA. Translation: AAA35897.1 .
    CCDSi CCDS54177.1.
    PIRi JC2041.
    RefSeqi NP_000151.1. NM_000160.4.
    XP_006722340.1. XM_006722277.1.
    UniGenei Hs.208.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A83 X-ray 1.40 C 412-420 [» ]
    3CZF X-ray 1.20 C 412-420 [» ]
    4ERS X-ray 2.64 A 28-123 [» ]
    4L6R X-ray 3.30 A 123-432 [» ]
    4LF3 X-ray 2.74 C/F 29-123 [» ]
    ProteinModelPortali P47871.
    SMRi P47871. Positions 28-429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108912. 3 interactions.
    IntActi P47871. 4 interactions.
    STRINGi 9606.ENSP00000383558.

    Chemistry

    BindingDBi P47871.
    ChEMBLi CHEMBL1985.
    DrugBanki DB00040. Glucagon recombinant.
    GuidetoPHARMACOLOGYi 251.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P47871.

    Polymorphism databases

    DMDMi 1346144.

    Proteomic databases

    PaxDbi P47871.
    PRIDEi P47871.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000400723 ; ENSP00000383558 ; ENSG00000215644 .
    GeneIDi 2642.
    KEGGi hsa:2642.
    UCSCi uc010wuw.2. human.

    Organism-specific databases

    CTDi 2642.
    GeneCardsi GC17P079763.
    HGNCi HGNC:4192. GCGR.
    MIMi 138033. gene.
    neXtProti NX_P47871.
    PharmGKBi PA28607.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263329.
    HOGENOMi HOG000008250.
    HOVERGENi HBG008318.
    InParanoidi P47871.
    KOi K04583.
    OrthoDBi EOG7TF78W.
    PhylomeDBi P47871.
    TreeFami TF315710.

    Enzyme and pathway databases

    Reactomei REACT_1665. Glucagon signaling in metabolic regulation.
    REACT_18283. G alpha (q) signalling events.
    REACT_18377. Glucagon-type ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P47871.
    GeneWikii Glucagon_receptor.
    GenomeRNAii 2642.
    NextBioi 10416.
    PROi P47871.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47871.
    Bgeei P47871.
    CleanExi HS_GCGR.
    Genevestigatori P47871.

    Family and domain databases

    InterProi IPR017981. GPCR_2-like.
    IPR001879. GPCR_2_extracellular_dom.
    IPR003290. GPCR_2_GLP1/glucagon_rcpt.
    IPR003291. GPCR_2_glucagon_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.
    PR01354. GLUCAGONR.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Liver.
    2. "The human glucagon receptor encoding gene: structure, cDNA sequence and chromosomal localization."
      Lok S., Kuijper J.L., Jelinek L.J., Kramer J.M., Whitmore T.E., Sprecher C.A., Mathewes S., Grant F.J., Biggs S.H., Rosenberg G.B.
      Gene 140:203-209(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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: Liver.
    4. "Localization of the glucagon receptor gene to human chromosome band 17q25."
      Menzel S., Stoffel M., Espinosa R. III, Fernald A.A., Le Beau M.M., Bell G.I.
      Genomics 20:327-328(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-54.
      Tissue: Placenta.
    5. "Role of the glucagon receptor COOH-terminal domain in glucagon-mediated signaling and receptor internalization."
      Buggy J.J., Heurich R.O., MacDougall M., Kelley K.A., Livingston J.N., Yoo-Warren H., Rossomando A.J.
      Diabetes 46:1400-1405(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    6. "Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype."
      Ruckert C., Fiorillo M.T., Loll B., Moretti R., Biesiadka J., Saenger W., Ziegler A., Sorrentino R., Uchanska-Ziegler B.
      J. Biol. Chem. 281:2306-2316(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 412-420 IN COMPLEX WITH CLASS I MHC.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 28-123, FUNCTION, MUTAGENESIS OF TYR-65 AND GLN-113, DISULFIDE BONDS, GLYCOSYLATION AT ASN-74 AND ASN-78.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 123-432, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, MEMBRANE TOPOLOGY, MUTAGENESIS OF TRP-36; ASP-63; ALA-135; TYR-145; TYR-149; LEU-198; ARG-201; TYR-202; ASP-208; TRP-215; GLN-232; TYR-233; LYS-286; GLU-290; CYS-294; TRP-295; TRP-304; LEU-382 AND LEU-386, CHARACTERIZATION OF VARIANT SER-86.
    9. "A mutation in the glucagon receptor gene (Gly40Ser): heterogeneity in the association with diabetes mellitus."
      Fujisawa T., Ikegami H., Yamato E., Takekawa K., Nakagawa Y., Hamada Y., Ueda H., Fukuda M., Ogihara T.
      Diabetologia 38:983-985(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-40.
    10. "Homozygous P86S mutation of the human glucagon receptor is associated with hyperglucagonemia, alpha cell hyperplasia, and islet cell tumor."
      Zhou C., Dhall D., Nissen N.N., Chen C.R., Yu R.
      Pancreas 38:941-946(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-86, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SER-86.

    Entry informationi

    Entry nameiGLR_HUMAN
    AccessioniPrimary (citable) accession number: P47871
    Secondary accession number(s): Q2M3M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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 17
      Human chromosome 17: 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