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P34972

- CNR2_HUMAN

UniProt

P34972 - CNR2_HUMAN

Protein

Cannabinoid receptor 2

Gene

CNR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis.4 Publications

    GO - Molecular functioni

    1. cannabinoid receptor activity Source: ProtInc

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
    2. immune response Source: ProtInc
    3. inflammatory response Source: UniProtKB-KW
    4. negative regulation of action potential Source: Ensembl
    5. negative regulation of inflammatory response Source: Ensembl
    6. negative regulation of mast cell activation Source: Ensembl
    7. negative regulation of nitric-oxide synthase activity Source: Ensembl
    8. negative regulation of synaptic transmission, GABAergic Source: Ensembl
    9. response to amphetamine Source: Ensembl
    10. response to lipopolysaccharide Source: Ensembl
    11. sensory perception of pain Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_14828. Class A/1 (Rhodopsin-like receptors).
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cannabinoid receptor 2
    Short name:
    CB-2
    Short name:
    CB2
    Short name:
    hCB2
    Alternative name(s):
    CX5
    Gene namesi
    Name:CNR2
    Synonyms:CB2A, CB2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2160. CNR2.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cell projectiondendrite By similarity. Perikaryon By similarity
    Note: Localizes to apical dendrite of pyramidal neurons.By similarity

    GO - Cellular componenti

    1. dendrite Source: UniProtKB-SubCell
    2. extrinsic component of cytoplasmic side of plasma membrane Source: Ensembl
    3. integral component of plasma membrane Source: ProtInc
    4. perikaryon Source: UniProtKB-SubCell
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091K → A: No effect on agonist binding. Affects cannabinoid agonist binding; when associated with G-112. 1 Publication
    Mutagenesisi109 – 1091K → R: No effect on agonist binding. 1 Publication
    Mutagenesisi112 – 1121S → G: Affects cannabinoid agonist binding; when associated with A-109. 1 Publication
    Mutagenesisi130 – 1301D → A: Loss of ligand binding. Alters agonist-induced inhibitory effect on adenylate cyclase. 1 Publication
    Mutagenesisi131 – 1311R → A: No effect on ligand binding. Alters agonist-induced inhibitory effect on adenylate cyclase. 1 Publication
    Mutagenesisi201 – 2011L → P: Abolishes ligand binding and agonist-induced inhibitory effect on adenylate cyclase. 1 Publication
    Mutagenesisi207 – 2071Y → A: Abolishes agonist-induced inhibitory effect on adenylate cyclase. No effect on ligand binding. 1 Publication
    Mutagenesisi244 – 2441A → E: Loss of ligand binding. Alters agonist-induced inhibitory effect on adenylate cyclase. 1 Publication

    Organism-specific databases

    PharmGKBiPA26682.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 360360Cannabinoid receptor 2PRO_0000069323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi11 – 111N-linked (GlcNAc...)Sequence Analysis
    Modified residuei335 – 3351PhosphoserineBy similarity
    Modified residuei336 – 3361PhosphoserineBy similarity
    Modified residuei338 – 3381PhosphothreonineBy similarity
    Modified residuei352 – 3521Phosphoserine1 Publication

    Post-translational modificationi

    Constitutively phosphorylated on Ser-352; phosphorylation increases cell internalization and desensitizes the receptor.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP34972.
    PaxDbiP34972.
    PRIDEiP34972.

    PTM databases

    PhosphoSiteiP34972.

    Expressioni

    Tissue specificityi

    Preferentially expressed in cells of the immune system with higher expression in B-cells and NK cells (at protein level). Expressed in skin in suprabasal layers and hair follicles (at protein level). Highly expressed in tonsil and to a lower extent in spleen, peripheral blood mononuclear cells, and thymus. PubMed:14657172 could not detect expression in normal brain. Expressed in brain by perivascular microglial cells and dorsal root ganglion sensory neurons (at protein level). Two isoforms are produced by alternative promoter usage and differ only in the 5' UTR: isoform CB2A is observed predominantly in testis with some expression in brain, while isoform CB2B is predominant in spleen and leukocytes.7 Publications

    Gene expression databases

    ArrayExpressiP34972.
    BgeeiP34972.
    CleanExiHS_CNR2.
    GenevestigatoriP34972.

    Organism-specific databases

    HPAiCAB009719.
    HPA028718.

    Interactioni

    Protein-protein interaction databases

    IntActiP34972. 3 interactions.
    STRINGi9606.ENSP00000363596.

    Structurei

    Secondary structure

    1
    360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi242 – 2454
    Helixi246 – 2549
    Turni255 – 2573
    Beta strandi258 – 2603
    Helixi261 – 2655
    Turni266 – 2694

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KI9NMR-A240-272[»]
    ProteinModelPortaliP34972.
    SMRiP34972. Positions 28-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP34972.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3333ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini60 – 7112CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini93 – 10412ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini130 – 14920CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini173 – 18816ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini215 – 24632CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini268 – 27912ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini302 – 36059CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei34 – 5926Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei72 – 9221Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei105 – 12925Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei150 – 17223Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei189 – 21426Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei247 – 26721Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei280 – 30122Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG276403.
    HOGENOMiHOG000049272.
    HOVERGENiHBG051045.
    InParanoidiP34972.
    KOiK04278.
    OMAiVNFHVFH.
    OrthoDBiEOG7CK36K.
    PhylomeDBiP34972.
    TreeFamiTF330052.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR001551. Canbinoid_rcpt_2.
    IPR002230. Cnbnoid_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR22750:SF11. PTHR22750:SF11. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00523. CANABINOID2R.
    PR00362. CANNABINOIDR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P34972-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEECWVTEIA NGSKDGLDSN PMKDYMILSG PQKTAVAVLC TLLGLLSALE    50
    NVAVLYLILS SHQLRRKPSY LFIGSLAGAD FLASVVFACS FVNFHVFHGV 100
    DSKAVFLLKI GSVTMTFTAS VGSLLLTAID RYLCLRYPPS YKALLTRGRA 150
    LVTLGIMWVL SALVSYLPLM GWTCCPRPCS ELFPLIPNDY LLSWLLFIAF 200
    LFSGIIYTYG HVLWKAHQHV ASLSGHQDRQ VPGMARMRLD VRLAKTLGLV 250
    LAVLLICWFP VLALMAHSLA TTLSDQVKKA FAFCSMLCLI NSMVNPVIYA 300
    LRSGEIRSSA HHCLAHWKKC VRGLGSEAKE EAPRSSVTET EADGKITPWP 350
    DSRDLDLSDC 360
    Length:360
    Mass (Da):39,681
    Last modified:February 1, 1994 - v1
    Checksum:iA7ECF68C16E7514B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731T → A in AAH95545. (PubMed:15489334)Curated
    Sequence conflicti307 – 3071R → H in AAH69722. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631Q → R High incidence in Japanese depressed subjects. 2 Publications
    Corresponds to variant rs2501432 [ dbSNP | Ensembl ].
    VAR_054310
    Natural varianti316 – 3161H → Y.3 Publications
    Corresponds to variant rs2229579 [ dbSNP | Ensembl ].
    VAR_029209

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74328 mRNA. Translation: CAA52376.1.
    EU517121 mRNA. Translation: ACD31539.1.
    AJ430063 mRNA. Translation: CAD22548.1.
    AJ430064 Genomic DNA. Translation: CAD22549.1.
    AY242132 Genomic DNA. Translation: AAO92299.1.
    AM156854 mRNA. Translation: CAJ42137.1.
    AM156855 mRNA. Translation: CAJ42138.1.
    AM156856 mRNA. Translation: CAJ42139.1.
    AL590609 Genomic DNA. Translation: CAI14799.1.
    CH471134 Genomic DNA. Translation: EAW95099.1.
    BC069722 mRNA. Translation: AAH69722.1.
    BC074767 mRNA. Translation: AAH74767.1.
    BC095545 mRNA. Translation: AAH95545.1.
    CCDSiCCDS245.1.
    PIRiS36750.
    RefSeqiNP_001832.1. NM_001841.2.
    XP_005245793.1. XM_005245736.2.
    XP_005245794.1. XM_005245737.2.
    XP_005245795.1. XM_005245738.2.
    UniGeneiHs.73037.

    Genome annotation databases

    EnsembliENST00000374472; ENSP00000363596; ENSG00000188822.
    GeneIDi1269.
    KEGGihsa:1269.
    UCSCiuc001bif.3. human.

    Polymorphism databases

    DMDMi461697.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74328 mRNA. Translation: CAA52376.1 .
    EU517121 mRNA. Translation: ACD31539.1 .
    AJ430063 mRNA. Translation: CAD22548.1 .
    AJ430064 Genomic DNA. Translation: CAD22549.1 .
    AY242132 Genomic DNA. Translation: AAO92299.1 .
    AM156854 mRNA. Translation: CAJ42137.1 .
    AM156855 mRNA. Translation: CAJ42138.1 .
    AM156856 mRNA. Translation: CAJ42139.1 .
    AL590609 Genomic DNA. Translation: CAI14799.1 .
    CH471134 Genomic DNA. Translation: EAW95099.1 .
    BC069722 mRNA. Translation: AAH69722.1 .
    BC074767 mRNA. Translation: AAH74767.1 .
    BC095545 mRNA. Translation: AAH95545.1 .
    CCDSi CCDS245.1.
    PIRi S36750.
    RefSeqi NP_001832.1. NM_001841.2.
    XP_005245793.1. XM_005245736.2.
    XP_005245794.1. XM_005245737.2.
    XP_005245795.1. XM_005245738.2.
    UniGenei Hs.73037.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KI9 NMR - A 240-272 [» ]
    ProteinModelPortali P34972.
    SMRi P34972. Positions 28-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P34972. 3 interactions.
    STRINGi 9606.ENSP00000363596.

    Chemistry

    BindingDBi P34972.
    ChEMBLi CHEMBL253.
    DrugBanki DB00486. Nabilone.
    GuidetoPHARMACOLOGYi 57.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P34972.

    Polymorphism databases

    DMDMi 461697.

    Proteomic databases

    MaxQBi P34972.
    PaxDbi P34972.
    PRIDEi P34972.

    Protocols and materials databases

    DNASUi 1269.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374472 ; ENSP00000363596 ; ENSG00000188822 .
    GeneIDi 1269.
    KEGGi hsa:1269.
    UCSCi uc001bif.3. human.

    Organism-specific databases

    CTDi 1269.
    GeneCardsi GC01M024197.
    H-InvDB HIX0160038.
    HGNCi HGNC:2160. CNR2.
    HPAi CAB009719.
    HPA028718.
    MIMi 605051. gene.
    neXtProti NX_P34972.
    PharmGKBi PA26682.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276403.
    HOGENOMi HOG000049272.
    HOVERGENi HBG051045.
    InParanoidi P34972.
    KOi K04278.
    OMAi VNFHVFH.
    OrthoDBi EOG7CK36K.
    PhylomeDBi P34972.
    TreeFami TF330052.

    Enzyme and pathway databases

    Reactomei REACT_14828. Class A/1 (Rhodopsin-like receptors).
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P34972.
    GeneWikii Cannabinoid_receptor_type_2.
    GenomeRNAii 1269.
    NextBioi 5139.
    PROi P34972.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P34972.
    Bgeei P34972.
    CleanExi HS_CNR2.
    Genevestigatori P34972.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR001551. Canbinoid_rcpt_2.
    IPR002230. Cnbnoid_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR22750:SF11. PTHR22750:SF11. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00523. CANABINOID2R.
    PR00362. CANNABINOIDR.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a peripheral receptor for cannabinoids."
      Munro S., Thomas K.L., Abu-Shaar M.
      Nature 365:61-65(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Species differences in cannabinoid receptor 2 (CNR2 gene): identification of novel human and rodent CB2 isoforms, differential tissue expression and regulation by cannabinoid receptor ligands."
      Liu Q.-R., Pan C.H., Hishimoto A., Li C.Y., Xi Z.X., Llorente-Berzal A., Viveros M.P., Ishiguro H., Arinami T., Onaivi E.S., Uhl G.R.
      Genes Brain Behav. 8:519-530(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Spleen.
    3. "Cannabinoid receptors and their genes."
      Bruess M., Boenisch H.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Blood.
    4. "Isolation of complete coding sequence for cannabinoid receptor 2 (CNR2)."
      Warren C.N., Aronstam R.S., Sharma S.V.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Amplification and cloning of human cannabinoid receptor 2 gene from Asiatic origin."
      Saravanan T., Chugh A., Kant R.
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-316.
      Tissue: Blood.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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], VARIANTS ARG-63 AND TYR-316.
      Tissue: Brain.
    9. "Expression of central and peripheral cannabinoid receptors in human immune tissues and leukocyte subpopulations."
      Galiegue S., Mary S., Marchand J., Dussossoy D., Carriere D., Carayon P., Bouaboula M., Shire D., Le Fur G., Casellas P.
      Eur. J. Biochem. 232:54-61(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Regulation of peripheral cannabinoid receptor CB2 phosphorylation by the inverse agonist SR 144528. Implications for receptor biological responses."
      Bouaboula M., Dussossoy D., Casellas P.
      J. Biol. Chem. 274:20397-20405(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-352, SUBCELLULAR LOCATION.
    11. "Role of a conserved lysine residue in the peripheral cannabinoid receptor (CB2): evidence for subtype specificity."
      Tao Q., McAllister S.D., Andreassi J., Nowell K.W., Cabral G.A., Hurst D.P., Bachtel K., Ekman M.C., Reggio P.H., Abood M.E.
      Mol. Pharmacol. 55:605-613(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-109 AND SER-112.
    12. "Evidence that 2-arachidonoylglycerol but not N-palmitoylethanolamine or anandamide is the physiological ligand for the cannabinoid CB2 receptor. Comparison of the agonistic activities of various cannabinoid receptor ligands in HL-60 cells."
      Sugiura T., Kondo S., Kishimoto S., Miyashita T., Nakane S., Kodaka T., Suhara Y., Takayama H., Waku K.
      J. Biol. Chem. 275:605-612(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF 2-ARACHIDONOYLGLYCEROL AS AN ENDOGENOUS LIGAND.
    13. "Presence and regulation of the endocannabinoid system in human dendritic cells."
      Matias I., Pochard P., Orlando P., Salzet M., Pestel J., Di Marzo V.
      Eur. J. Biochem. 269:3771-3778(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Absence of a conserved proline and presence of a conserved tyrosine in the CB2 cannabinoid receptor are crucial for its function."
      Song Z.H., Feng W.
      FEBS Lett. 531:290-294(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-201 AND TYR-207.
    15. "Effects of D3.49A, R3.50A, and A6.34E mutations on ligand binding and activation of the cannabinoid-2 (CB2) receptor."
      Feng W., Song Z.H.
      Biochem. Pharmacol. 65:1077-1085(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-130; ARG-131 AND ALA-244.
    16. "2-arachidonoylglycerol induces the migration of HL-60 cells differentiated into macrophage-like cells and human peripheral blood monocytes through the cannabinoid CB2 receptor-dependent mechanism."
      Kishimoto S., Gokoh M., Oka S., Muramatsu M., Kajiwara T., Waku K., Sugiura T.
      J. Biol. Chem. 278:24469-24475(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Inhibition of skin tumor growth and angiogenesis in vivo by activation of cannabinoid receptors."
      Casanova M.L., Blazquez C., Martinez-Palacio J., Villanueva C., Fernandez-Acenero M.J., Huffman J.W., Jorcano J.L., Guzman M.
      J. Clin. Invest. 111:43-50(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    18. "Cannabinoid CB2 receptors and fatty acid amide hydrolase are selectively overexpressed in neuritic plaque-associated glia in Alzheimer's disease brains."
      Benito C., Nunez E., Tolon R.M., Carrier E.J., Rabano A., Hillard C.J., Romero J.
      J. Neurosci. 23:11136-11141(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    19. "Cannabinoid CB2 receptors are expressed by perivascular microglial cells in the human brain: an immunohistochemical study."
      Nunez E., Benito C., Pazos M.R., Barbachano A., Fajardo O., Gonzalez S., Tolon R.M., Romero J.
      Synapse 53:208-213(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    20. "Cannabinoid receptor CB2 localisation and agonist-mediated inhibition of capsaicin responses in human sensory neurons."
      Anand U., Otto W.R., Sanchez-Herrera D., Facer P., Yiangou Y., Korchev Y., Birch R., Benham C., Bountra C., Chessell I.P., Anand P.
      Pain 138:667-680(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    21. "Structural biology of human cannabinoid receptor-2 helix 6 in membrane-mimetic environments."
      Tiburu E.K., Tyukhtenko S., Deshmukh L., Vinogradova O., Janero D.R., Makriyannis A.
      Biochem. Biophys. Res. Commun. 384:243-248(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 240-272.
    22. Cited for: VARIANTS ARG-63 AND TYR-316.

    Entry informationi

    Entry nameiCNR2_HUMAN
    AccessioniPrimary (citable) accession number: P34972
    Secondary accession number(s): C6ES44
    , Q4VBK8, Q5JRH7, Q6B0G7, Q6NSY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 131 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 1
      Human chromosome 1: 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