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P21554 (CNR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cannabinoid receptor 1
Short name=CB-R
Short name=CB1
Alternative name(s):
CANN6
Gene names
Name:CNR1
Synonyms:CNR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cannabinoid-induced CNS effects. Acts by inhibiting adenylate cyclase. Could be a receptor for anandamide. Inhibits L-type Ca2+ channel current. Isoform 2 and isoform 3 have altered ligand binding. Ref.4

Subunit structure

Interacts (via C-terminus) with CNRIP1. Ref.13

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Widely expressed. Ref.4

Post-translational modification

Palmitoylation at Cys-415 is important for recruitment at both plasma membrane and lipid rafts. Ref.14

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMGlycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 18761332. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Compara

behavior

Traceable author statement Ref.2. Source: ProtInc

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Compara

memory

Inferred from electronic annotation. Source: Compara

negative regulation of action potential

Inferred from electronic annotation. Source: Compara

negative regulation of blood pressure

Inferred from electronic annotation. Source: Compara

negative regulation of dopamine secretion

Inferred from electronic annotation. Source: Compara

negative regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Compara

negative regulation of mast cell activation

Inferred from electronic annotation. Source: Compara

negative regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Compara

positive regulation of acute inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Compara

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Compara

positive regulation of blood pressure

Inferred from electronic annotation. Source: Compara

positive regulation of fever generation

Inferred from electronic annotation. Source: Compara

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Compara

regulation of feeding behavior

Inferred from electronic annotation. Source: Compara

regulation of insulin secretion

Inferred from electronic annotation. Source: Compara

regulation of penile erection

Inferred from electronic annotation. Source: Compara

regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Compara

regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Compara

response to cocaine

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to lipopolysaccharide

Inferred from electronic annotation. Source: Compara

response to morphine

Inferred from electronic annotation. Source: Compara

response to nicotine

Inferred from electronic annotation. Source: Compara

response to nutrient

Inferred from electronic annotation. Source: Compara

response to stress

Inferred from electronic annotation. Source: Compara

sensory perception of pain

Inferred from electronic annotation. Source: Compara

spermatogenesis

Inferred from electronic annotation. Source: Compara

   Cellular_componentintegral to plasma membrane

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functioncannabinoid receptor activity

Inferred from direct assay PubMed 18761332. Source: UniProtKB

drug binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21554-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21554-2)

Also known as: CB1a,Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MKSILDGLAD...EFYNKSLSSF → MALQIPPSAPSPLTSCTWAQMTFSTKTS
Isoform 3 (identifier: P21554-3)

Also known as: CB1b;

The sequence of this isoform differs from the canonical sequence as follows:
     22-54: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Cannabinoid receptor 1
PRO_0000069314

Regions

Topological domain1 – 116116Extracellular Potential
Transmembrane117 – 14226Helical; Name=1; Potential
Topological domain143 – 15412Cytoplasmic Potential
Transmembrane155 – 17521Helical; Name=2; Potential
Topological domain176 – 18712Extracellular Potential
Transmembrane188 – 21225Helical; Name=3; Potential
Topological domain213 – 23220Cytoplasmic Potential
Transmembrane233 – 25523Helical; Name=4; Potential
Topological domain256 – 27318Extracellular Potential
Transmembrane274 – 29926Helical; Name=5; Potential
Topological domain300 – 34445Cytoplasmic Potential
Transmembrane345 – 36521Helical; Name=6; Potential
Topological domain366 – 37712Extracellular Potential
Transmembrane378 – 39922Helical; Name=7; Potential
Topological domain400 – 47273Cytoplasmic Potential

Amino acid modifications

Lipidation4151S-palmitoyl cysteine Ref.14
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 8989MKSIL…SLSSF → MALQIPPSAPSPLTSCTWAQ MTFSTKTS in isoform 2.
VSP_001868
Alternative sequence22 – 5433Missing in isoform 3.
VSP_016529

Experimental info

Sequence conflict941E → G in AAH95513. Ref.12
Sequence conflict1031M → I in AAH95513. Ref.12
Sequence conflict1491C → R in AAH95513. Ref.12
Sequence conflict2001F → L in AAD34320. Ref.5
Sequence conflict2161I → V in AAD34320. Ref.5
Sequence conflict2461V → A in AAD34320. Ref.5
Sequence conflict2981L → P in AAH95513. Ref.12
Sequence conflict3321P → S in AAI00972. Ref.12

Secondary structure

1 .......... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 1D2E49061D12ABF2

FASTA47252,858
        10         20         30         40         50         60 
MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDIKGDMASK LGYFPQKFPL TSFRGSPFQE 

        70         80         90        100        110        120 
KMTAGDNPQL VPADQVNITE FYNKSLSSFK ENEENIQCGE NFMDIECFMV LNPSQQLAIA 

       130        140        150        160        170        180 
VLSLTLGTFT VLENLLVLCV ILHSRSLRCR PSYHFIGSLA VADLLGSVIF VYSFIDFHVF 

       190        200        210        220        230        240 
HRKDSRNVFL FKLGGVTASF TASVGSLFLT AIDRYISIHR PLAYKRIVTR PKAVVAFCLM 

       250        260        270        280        290        300 
WTIAIVIAVL PLLGWNCEKL QSVCSDIFPH IDETYLMFWI GVTSVLLLFI VYAYMYILWK 

       310        320        330        340        350        360 
AHSHAVRMIQ RGTQKSIIIH TSEDGKVQVT RPDQARMDIR LAKTLVLILV VLIICWGPLL 

       370        380        390        400        410        420 
AIMVYDVFGK MNKLIKTVFA FCSMLCLLNS TVNPIIYALR SKDLRHAFRS MFPSCEGTAQ 

       430        440        450        460        470 
PLDNSMGDSD CLHKHANNAA SVHRAAESCI KSTVKIAKVT MSVSTDTSAE AL

« Hide

Isoform 2 (CB1a,Short) [UniParc].

Checksum: E3C31ACAB4066BC1
Show »

FASTA41145,874
Isoform 3 (CB1b) [UniParc].

Checksum: C80C6B8D640412C1
Show »

FASTA43949,060

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a human cannabinoid receptor cDNA."
Gerard C., Mollereau C., Vassart G., Parmentier M.
Nucleic Acids Res. 18:7142-7142(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain stem.
[2]"Molecular cloning of a human cannabinoid receptor which is also expressed in testis."
Gerard C., Mollereau C., Vassart G., Parmentier M.
Biochem. J. 279:129-134(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain stem.
[3]"An amino-terminal variant of the central cannabinoid receptor resulting from alternative splicing."
Shire D., Carillon C., Kaghad M., Calandra B., Rinaldi-Carmona M., Le Fur G., Caput D., Ferrara P.
J. Biol. Chem. 270:3726-3731(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Lung.
[4]"Identification and characterisation of a novel splice variant of the human CB1 receptor."
Ryberg E., Vu H.K., Larsson N., Groblewski T., Hjorth S., Elebring T., Sjoegren S., Greasley P.J.
FEBS Lett. 579:259-264(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
[5]Kathmann M., Schlicker E.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[6]Bonner T.I.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]Kumar S., Gupta S., Sharma G.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain tumor.
[8]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[10]"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. expand/collapse author list , 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].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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] (ISOFORM 1).
Tissue: Lung.
[13]"CB1 cannabinoid receptor activity is modulated by the cannabinoid receptor interacting protein CRIP 1a."
Niehaus J.L., Liu Y., Wallis K.T., Egertova M., Bhartur S.G., Mukhopadhyay S., Shi S., He H., Selley D.E., Howlett A.C., Elphick M.R., Lewis D.L.
Mol. Pharmacol. 72:1557-1566(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNRIP1.
Tissue: Brain.
[14]"Effects of palmitoylation of Cys(415) in helix 8 of the CB(1) cannabinoid receptor on membrane localization and signalling."
Oddi S., Dainese E., Sandiford S., Fezza F., Lanuti M., Chiurchiu V., Totaro A., Catanzaro G., Barcaroli D., De Laurenzi V., Centonze D., Mukhopadhyay S., Selent J., Howlett A.C., Maccarrone M.
Br. J. Pharmacol. 165:2635-2651(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-415.
[15]"Cannabinoid receptor-G protein interactions: G(alphai1)-bound structures of IC3 and a mutant with altered G protein specificity."
Ulfers A.L., McMurry J.L., Miller A., Wang L., Kendall D.A., Mierke D.F.
Protein Sci. 11:2526-2531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 338-346.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X54937 mRNA. Translation: CAA38699.1.
X81120 mRNA. Translation: CAA57018.1.
X81121 mRNA. Translation: CAA57019.1.
AY766182 mRNA. Translation: AAV35030.1.
AF107262 mRNA. Translation: AAD34320.1.
U73304 Genomic DNA. Translation: AAB18200.1.
DQ067455 mRNA. Translation: AAY68486.1.
AY225225 Genomic DNA. Translation: AAO67710.1.
AL136096 Genomic DNA. Translation: CAB96726.1.
AL136096 Genomic DNA. Translation: CAI19916.1.
AK313908 mRNA. Translation: BAG36631.1.
CH471051 Genomic DNA. Translation: EAW48574.1.
CH471051 Genomic DNA. Translation: EAW48575.1.
CH471051 Genomic DNA. Translation: EAW48576.1.
BC074811 mRNA. Translation: AAH74811.1.
BC074812 mRNA. Translation: AAH74812.1.
BC095513 mRNA. Translation: AAH95513.1.
BC100968 mRNA. Translation: AAI00969.1.
BC100969 mRNA. Translation: AAI00970.1.
BC100970 mRNA. Translation: AAI00971.1.
BC100971 mRNA. Translation: AAI00972.1.
IPIIPI00009396.
IPI00215993.
IPI00655874.
PIRS17595.
RefSeqNP_001153698.1. NM_001160226.1.
NP_001153730.1. NM_001160258.1.
NP_001153731.1. NM_001160259.1.
NP_057167.2. NM_016083.4.
NP_149421.2. NM_033181.3.
UniGeneHs.75110.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVQNMR-A338-346[»]
1LVRNMR-A338-346[»]
2B0YNMR-A400-414[»]
2KOENMR-A377-414[»]
ProteinModelPortalP21554.
ModBaseSearch...

Protein-protein interaction databases

IntActP21554. 1 interaction.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP21554.

Polymorphism databases

DMDM115562.

Proteomic databases

PaxDbP21554.
PRIDEP21554.

Protocols and materials databases

DNASU1268.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369499; ENSP00000358511; ENSG00000118432.
ENST00000369501; ENSP00000358513; ENSG00000118432.
ENST00000428600; ENSP00000412192; ENSG00000118432.
ENST00000468898; ENSP00000420188; ENSG00000118432.
ENST00000535130; ENSP00000442689; ENSG00000118432.
ENST00000537554; ENSP00000441046; ENSG00000118432.
ENST00000549716; ENSP00000449549; ENSG00000118432.
ENST00000549890; ENSP00000446819; ENSG00000118432.
GeneID1268.
KEGGhsa:1268.
UCSCuc003pmq.4. human.
uc010kca.3. human.

Organism-specific databases

CTD1268.
GeneCardsGC06M088850.
H-InvDBHIX0165039.
HGNCHGNC:2159. CNR1.
HPACAB005603.
MIM114610. gene.
neXtProtNX_P21554.
PharmGKBPA26681.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148018.
HOVERGENHBG051045.
InParanoidP21554.
KOK04277.
OMAECFMILN.
OrthoDBEOG41ZF9S.
PhylomeDBP21554.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP21554.
BgeeP21554.
CleanExHS_CNR1.
GenevestigatorP21554.
GermOnlineENSG00000118432. Homo sapiens.

Family and domain databases

InterProIPR002230. Cnbnoid_rcpt.
IPR000810. Cnoid_rcpt_1.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR22750:SF10. PTHR22750:SF10. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PIRSFPIRSF037995. Cnoid_rcpt_1. 1 hit.
PRINTSPR00522. CANABINOID1R.
PR00362. CANNABINOIDR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP21554.
ChEMBLCHEMBL218.
DrugBankDB00470. Marinol.
DB00486. Nabilone.
DB06155. Rimonabant.
EvolutionaryTraceP21554.
GenomeRNAi1268.
NextBio5133.
SOURCESearch...

Entry information

Entry nameCNR1_HUMAN
AccessionPrimary (citable) accession number: P21554
Secondary accession number(s): B2R9T4 expand/collapse secondary AC list , E1P512, Q13949, Q495Z0, Q4PLI4, Q4VBM6, Q5JVL5, Q5UB37, Q9UNN0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents