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P35372 (OPRM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mu-type opioid receptor

Short name=M-OR-1
Short name=MOR-1
Alternative name(s):
Mu opiate receptor
Mu opioid receptor
Short name=MOP
Short name=hMOP
Gene names
Name:OPRM1
Synonyms:MOR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extend to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling whereas morphine induces only low desensitization and endocytosis. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 12 couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16 and isoform 17 do not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. Ref.32 Ref.38

Subunit structure

Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms). Interacts with PPL; the interaction disrupts agonist-mediated G-protein activation. Interacts (via C-terminus) with DNAJB4 (via C-terminus). Interacts with calmodulin; the interaction inhibits the constitutive activity of OPRM1; it abolishes basal and attenuates agonist-stimulated G-protein coupling. Interacts with FLNA, PLD2, RANBP9 and WLS. Interacts with GPM6A, RTP4, SYP, GNAS, RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 By similarity. Ref.21 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.32 Ref.38.

Isoform 12: Cytoplasm Ref.32 Ref.38.

Tissue specificity

Expressed in brain. Isoform 16 and isoform 17 are detected in brain. Ref.32

Post-translational modification

Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by ADRBK1 in a agonist-dependent manner. Phosphorylation at Tyr-168 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-377 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway By similarity.

Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4 By similarity.

Polymorphism

Variant Asp-40 does not show altered binding affinities for most opioid peptides and alkaloids tested, but it binds beta-endorphin, an endogenous opioid that activates the mu opioid receptor, approximately 3 times more tightly than the most common allelic form.

Miscellaneous

OPRM1 is the main physiological target for most clinically important opioid analgesics. OPRM1-mediated inhibition of voltage-gated calcium channels on central presynaptic terminals of primary afferent nociceptors is thought to be one of the primary mechanisms mediating analgesia at the spinal level. Opioid-induced hyperalgesic responses are observed following both acute and chronic dosing associated with cellular excitation.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence caution

The sequence CAI20458.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAW47705.1 differs from that shown. Reason: Erroneous initiation.

Isoform 9: The sequence AAQ77392.1 differs from that shown. Reason: a polymorphism leading to premature termination of translation (position: 411:Q->Stop)

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger

Traceable author statement Ref.1. Source: ProtInc

adenylate cyclase-activating dopamine receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

behavioral response to ethanol

Inferred from mutant phenotype PubMed 21039637. Source: UniProtKB

cellular response to stress

Inferred from mutant phenotype PubMed 21039637. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of Wnt protein secretion

Inferred from mutant phenotype Ref.37. Source: UniProtKB

negative regulation of adenylate cyclase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cAMP-mediated signaling

Inferred from direct assay Ref.38. Source: UniProtKB

negative regulation of cell proliferation

Traceable author statement PubMed 2159143. Source: ProtInc

negative regulation of cytosolic calcium ion concentration

Inferred from direct assay Ref.38. Source: UniProtKB

negative regulation of nitric oxide biosynthetic process

Inferred from direct assay Ref.38. Source: UniProtKB

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from direct assay Ref.37. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay Ref.37. Source: UniProtKB

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay Ref.37. Source: UniProtKB

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of behavior

Inferred from mutant phenotype PubMed 21039637. Source: UniProtKB

sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Traceable author statement PubMed 9242668. Source: ProtInc

endoplasmic reticulum

Traceable author statement PubMed 9242668. Source: ProtInc

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionG-protein alpha-subunit binding

Inferred from direct assay Ref.37. Source: UniProtKB

beta-endorphin receptor activity

Inferred from mutant phenotype Ref.40. Source: UniProtKB

morphine receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 18 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P35372-1)

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: P35372-2)

Also known as: MOR1A; MOR-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → VRSL
Isoform 3 (identifier: P35372-3)

Also known as: MOR-1R; MOR-1X;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS
Isoform 4 (identifier: P35372-4)

Also known as: MOR-1B3;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → GPPAKFVADQLAGSS
Isoform 5 (identifier: P35372-5)

Also known as: MOR-1C; MOR-1O;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → PPLAVSMAQIFTRYPPPTHREKTCNDYMKR
Isoform 6 (identifier: P35372-6)

Also known as: MOR-1V; MOR-1Y; MOR-1Y2; MOR-1Y3;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → IRDPISNLPRVSVF
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 7 (identifier: P35372-7)

Also known as: MOR-1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → KIDLFQKSSLLNCEHTKG
Isoform 8 (identifier: P35372-8)

Also known as: MOR-1B2;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → RERRQKSDW
Isoform 9 (identifier: P35372-9)

Also known as: MOR-1B5;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV
Isoform 10 (identifier: P35372-10)

Also known as: MOR-1i;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCLHRRVPSE...SGARPAVSTM
Isoform 11 (identifier: P35372-11)

Also known as: MOR-1B4;

The sequence of this isoform differs from the canonical sequence as follows:
     389-400: LENLEAETAPLP → S
Isoform 12 (identifier: P35372-12)

Also known as: MOR-1G1; MOR-1K;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
Isoform 13 (identifier: P35372-13)

Also known as: MOR-1G2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: MDSSAAPTNA...GNFLVMYVIV → MMRAKSISTKAGKPS
Isoform 14 (identifier: P35372-14)

Also known as: Mu3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     389-400: LENLEAETAPLP → NYYIIHRCCCNTPLISQKPVLLWFCD
Isoform 15 (identifier: P35372-15)

Also known as: MOR-1W;

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
     389-400: LENLEAETAPLP → VRSL
Isoform 16 (identifier: P35372-16)

Also known as: SV1;

The sequence of this isoform differs from the canonical sequence as follows:
     98-400: YTKMKTATNI...NLEAETAPLP → YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG
Isoform 17 (identifier: P35372-17)

Also known as: SV2;

The sequence of this isoform differs from the canonical sequence as follows:
     97-400: RYTKMKTATN...NLEAETAPLP → SSSWF
Isoform 18 (identifier: P35372-18)

Also known as: hMOR-1Z;

The sequence of this isoform differs from the canonical sequence as follows:
     98-186: YTKMKTATNI...ALDFRTPRNA → FHRLYTNILS...LDSHSHLRHH
     187-400: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Mu-type opioid receptor
PRO_0000069972

Regions

Topological domain1 – 6868Extracellular By similarity
Transmembrane69 – 9325Helical; Name=1; By similarity
Topological domain94 – 10613Cytoplasmic By similarity
Transmembrane107 – 13125Helical; Name=2; By similarity
Topological domain132 – 14211Extracellular By similarity
Transmembrane143 – 16523Helical; Name=3; By similarity
Topological domain166 – 18520Cytoplasmic By similarity
Transmembrane186 – 20722Helical; Name=4; By similarity
Topological domain208 – 23023Extracellular By similarity
Transmembrane231 – 25525Helical; Name=5; By similarity
Topological domain256 – 28328Cytoplasmic By similarity
Transmembrane284 – 30724Helical; Name=6; By similarity
Topological domain308 – 3147Extracellular By similarity
Transmembrane315 – 33824Helical; Name=7; By similarity
Topological domain339 – 40062Cytoplasmic By similarity

Amino acid modifications

Modified residue1681Phosphotyrosine By similarity
Modified residue3651Phosphoserine By similarity
Modified residue3721Phosphothreonine By similarity
Modified residue3771Phosphoserine By similarity
Lipidation3531S-palmitoyl cysteine Potential
Glycosylation91N-linked (GlcNAc...) Potential
Glycosylation121N-linked (GlcNAc...) Potential
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation481N-linked (GlcNAc...) Potential
Disulfide bond142 ↔ 219 By similarity

Natural variations

Alternative sequence1 – 100100Missing in isoform 12, isoform 14 and isoform 15.
VSP_042327
Alternative sequence1 – 9696MDSSA…MYVIV → MMRAKSISTKAGKPS in isoform 13.
VSP_042328
Alternative sequence11M → MCLHRRVPSEETYSLDRFAQ NPPLFPPPSLPASESRMAHA PLLQRCGAARTGFCKKQQEL WQRRKEAAEALGTRKVSVLL ATSHSGARPAVSTM in isoform 10.
VSP_037693
Alternative sequence97 – 400304RYTKM…TAPLP → SSSWF in isoform 17.
VSP_042329
Alternative sequence98 – 400303YTKMK…TAPLP → YSWFVIGGPEGRRKQRRLGE DKRARGCGEKG in isoform 16.
VSP_042330
Alternative sequence98 – 18689YTKMK…TPRNA → FHRLYTNILSSNLVLGKPAE DLCFHLRLHYASAHHYRVLW TDDLAPQECPHALWLQRKGQ ESSKDHQDGAGGGGCVHRLL DSHSHLRHH in isoform 18.
VSP_047577
Alternative sequence187 – 400214Missing in isoform 18.
VSP_047578
Alternative sequence389 – 40012LENLE…TAPLP → S in isoform 11.
VSP_037694
Alternative sequence389 – 40012LENLE…TAPLP → NYYIIHRCCCNTPLISQKPV LLWFCD in isoform 14.
VSP_042331
Alternative sequence389 – 40012LENLE…TAPLP → VRSL in isoform 2 and isoform 15.
VSP_001896
Alternative sequence389 – 40012LENLE…TAPLP → CLPIPSLSCWALEQGCLVVY PGPLQGPLVRYDLPAILHSS CLRGNTAPSPSGGAFLLS in isoform 3.
VSP_037695
Alternative sequence389 – 40012LENLE…TAPLP → GPPAKFVADQLAGSS in isoform 4.
VSP_037696
Alternative sequence389 – 40012LENLE…TAPLP → PPLAVSMAQIFTRYPPPTHR EKTCNDYMKR in isoform 5.
VSP_037697
Alternative sequence389 – 40012LENLE…TAPLP → IRDPISNLPRVSVF in isoform 6.
VSP_037698
Alternative sequence389 – 40012LENLE…TAPLP → KIDLFQKSSLLNCEHTKG in isoform 7.
VSP_037699
Alternative sequence389 – 40012LENLE…TAPLP → RERRQKSDW in isoform 8.
VSP_037700
Alternative sequence389 – 40012LENLE…TAPLP → VELNLDCHCENAKPWPLSYN AGQSPFPFPGRV in isoform 9.
VSP_037701
Natural variant61A → V. Ref.13 Ref.18 Ref.39 Ref.40
Corresponds to variant rs1799972 [ dbSNP | Ensembl ].
VAR_009525
Natural variant401N → D in 10% of the population. Ref.2 Ref.13 Ref.39 Ref.40
Corresponds to variant rs1799971 [ dbSNP | Ensembl ].
VAR_009524
Natural variant631G → V.
Corresponds to variant rs9282817 [ dbSNP | Ensembl ].
VAR_049426
Natural variant661S → F.
Corresponds to variant rs9282819 [ dbSNP | Ensembl ].
VAR_049427
Natural variant1471S → C Rare polymorphism. Ref.13 Ref.39
Corresponds to variant rs17174794 [ dbSNP | Ensembl ].
VAR_009526
Natural variant1521N → D. Ref.13
Corresponds to variant rs17174801 [ dbSNP | Ensembl ].
VAR_019252
Natural variant2601R → H Rare polymorphism. Ref.40
Corresponds to variant rs1799974 [ dbSNP | Ensembl ].
VAR_009527
Natural variant2651R → C. Ref.13
Corresponds to variant rs17174822 [ dbSNP | Ensembl ].
VAR_019253
Natural variant2741D → N. Ref.13
Corresponds to variant rs17174829 [ dbSNP | Ensembl ].
VAR_019254

Experimental info

Mutagenesis1421C → A or S: Abolishes ligand binding; when associated with A-219 or S-219. Ref.22
Mutagenesis2191C → A or S: Abolishes ligand binding; when associated with A-142 or S-142. Ref.22
Mutagenesis2731K → A: Impairs interaction with calmodulin. Ref.23 Ref.25
Mutagenesis2751R → A: Impairs interaction with calmodulin. Ref.25
Sequence conflict261P → L in BAG36624. Ref.11
Sequence conflict511D → N in AAA20580. Ref.1
Sequence conflict1091I → V in AAQ77391. Ref.6
Sequence conflict2071M → I in AAB60354. Ref.2
Sequence conflict2341L → V in AAA20580. Ref.1
Isoform 3:
Sequence conflict4021Q → H in AAK74189. Ref.4

Sequences

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

Last modified July 15, 1998. Version 2.
Checksum: 1DABEBEC9AFF6F66

FASTA40044,779
        10         20         30         40         50         60 
MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP 

        70         80         90        100        110        120 
PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALAT 

       130        140        150        160        170        180 
STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF 

       190        200        210        220        230        240 
RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI 

       250        260        270        280        290        300 
FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 

       310        320        330        340        350        360 
YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI 

       370        380        390        400 
EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP 

« Hide

Isoform 2 (MOR1A) (MOR-1A) [UniParc].

Checksum: 14184C69F06AFCBE
Show »

FASTA39243,957
Isoform 3 (MOR-1R) (MOR-1X) [UniParc].

Checksum: 42DC76968E6352A8
Show »

FASTA44649,520
Isoform 4 (MOR-1B3) [UniParc].

Checksum: B3FFA10F7B1C5311
Show »

FASTA40344,928
Isoform 5 (MOR-1C) (MOR-1O) [UniParc].

Checksum: 51B9E7B131122196
Show »

FASTA41847,032
Isoform 6 (MOR-1V) (MOR-1Y) (MOR-1Y2) (MOR-1Y3) [UniParc].

Checksum: 5BC8380AB8196D70
Show »

FASTA40245,096
Isoform 7 (MOR-1B1) [UniParc].

Checksum: 1A0330578A82B183
Show »

FASTA40645,544
Isoform 8 (MOR-1B2) [UniParc].

Checksum: 3BC7E1C19B9739E3
Show »

FASTA39744,743
Isoform 9 (MOR-1B5) [UniParc].

Checksum: 63301322222198DE
Show »

FASTA42047,070
Isoform 10 (MOR-1i) [UniParc].

Checksum: 14A90F782A013067
Show »

FASTA49355,045
Isoform 11 (MOR-1B4) [UniParc].

Checksum: 7E806AFCBE572CD5
Show »

FASTA38943,588
Isoform 12 (MOR-1G1) (MOR-1K) [UniParc].

Checksum: 03FE8402349A629C
Show »

FASTA30034,393
Isoform 13 (MOR-1G2) [UniParc].

Checksum: 6373C1D800FF5E53
Show »

FASTA31936,516
Isoform 14 (Mu3) [UniParc].

Checksum: 7346DB61E594896E
Show »

FASTA31436,240
Isoform 15 (MOR-1W) [UniParc].

Checksum: 62A80E8005705E4C
Show »

FASTA29233,570
Isoform 16 (SV1) [UniParc].

Checksum: 1E780EE294726795
Show »

FASTA12813,544
Isoform 17 (SV2) [UniParc].

Checksum: E6590D98EDF64171
Show »

FASTA10110,451
Isoform 18 (hMOR-1Z) [UniParc].

Checksum: 2A80DD5FADA6B83B
Show »

FASTA18620,188

References

« Hide 'large scale' references
[1]"Human mu opiate receptor. cDNA and genomic clones, pharmacologic characterization and chromosomal assignment."
Wang J.-B., Johnson P.S., Persico A.M., Hawkins A.L., Griffin C.A., Uhl G.R.
FEBS Lett. 338:217-222(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Expression of two variants of the human mu opioid receptor mRNA in SK-N-SH cells and human brain."
Bare L.A., Mansson E., Yang D.
FEBS Lett. 354:213-216(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-40.
Tissue: Brain.
[3]"The human mu opioid receptor: modulation of functional desensitization by calcium/calmodulin-dependent protein kinase and protein kinase C."
Mestek A. Jr., Hurley J.H., Bye L.S., Campbell A.D., Chen Y., Tian M., Liu J., Schulman H., Yu L.
J. Neurosci. 15:2396-2406(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Identification and characterization of two new human mu opioid receptor splice variants, hMOR-1O and hMOR-1X."
Pan Y.X., Xu J., Mahurter L., Xu M., Gilbert A.K., Pasternak G.W.
Biochem. Biophys. Res. Commun. 301:1057-1061(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
[5]"Molecular identification and functional expression of mu 3, a novel alternatively spliced variant of the human mu opiate receptor gene."
Cadet P., Mantione K.J., Stefano G.B.
J. Immunol. 170:5118-5123(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
[6]"Identification and characterization of six new alternatively spliced variants of the human mu opioid receptor gene, Oprm."
Pan L., Xu J., Yu R., Xu M.-M., Pan Y.-X., Pasternak G.W.
Neuroscience 133:209-220(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6; 7; 8; 9 AND 11).
[7]"Isolation and characterization of new exon 11-associated N-terminal splice variants of the human mu opioid receptor gene."
Xu J., Xu M., Hurd Y.L., Pasternak G.W., Pan Y.X.
J. Neurochem. 108:962-972(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 12 AND 13).
[8]"Novel variants of the human mu opioid receptor are generated by alternative splicing and transcription from different positions in the OPRM1 gene."
Baar C., Kvam T.-M., Rakvag T.T., Kaasa S., Skorpen F.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 15).
Tissue: Brain.
[9]"Isolation and expression of alternatively spliced variants encoding proteins with single transmembrane domain in mu opioid receptor genes."
Xu J., Pasternak G.W., Pan Y.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
[10]"Expansion of the human mu-opioid receptor gene architecture: novel functional variants."
Shabalina S.A., Zaykin D.V., Gris P., Ogurtsov A.Y., Gauthier J., Shibata K., Tchivileva I.E., Belfer I., Mishra B., Kiselycznyk C., Wallace M.R., Staud R., Spiridonov N.A., Max M.B., Goldman D., Fillingim R.B., Maixner W., Diatchenko L.
Hum. Mol. Genet. 18:1037-1051(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
Tissue: Brain.
[11]"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: Brain.
[12]"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-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[13]NIEHS SNPs program
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ASP-40; CYS-147; ASP-152; CYS-265 AND ASN-274.
[14]"Isolation and characterization of two alternatively spliced variants from the human mu opioid receptor, OPRM1, gene."
Xu J., Xu M., Pasternak G.W., Pan Y.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 10).
[15]"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].
[16]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].
[17]"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).
[18]"An homozygous Ala 6 Val (GCC->GTC) mutation was detected on human mu opioid receptor gene of an African American individual with sickle cell anemia."
Metha S., Glendenning M., Kutlar A., Kutlar F.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, VARIANT VAL-6.
Tissue: Blood.
[19]"The mu opiate receptor as a candidate gene for pain: polymorphisms, variations in expression, nociception, and opiate responses."
Uhl G.R., Sora I., Wang Z.
Proc. Natl. Acad. Sci. U.S.A. 96:7752-7755(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
[20]"Mu opioid receptor gene expression in immune cells."
Chuang T.K., Killam K.F. Jr., Chuang L.F., Kung H.F., Sheng W.S., Chao C.C., Yu L., Chuang R.Y.
Biochem. Biophys. Res. Commun. 216:922-930(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-374.
[21]"ADP-ribosylation factor-dependent phospholipase D2 activation is required for agonist-induced mu-opioid receptor endocytosis."
Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V.
J. Biol. Chem. 278:9979-9985(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLD2.
[22]"Mutation of human mu opioid receptor extracellular 'disulfide cysteine' residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane."
Zhang P., Johnson P.S., Zollner C., Wang W., Wang Z., Montes A.E., Seidleck B.K., Blaschak C.J., Surratt C.K.
Brain Res. Mol. Brain Res. 72:195-204(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-142 AND CYS-219.
[23]"Calmodulin binding to G protein-coupling domain of opioid receptors."
Wang D., Sadee W., Quillan J.M.
J. Biol. Chem. 274:22081-22088(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273.
[24]"Molecular mechanisms and regulation of opioid receptor signaling."
Law P.Y., Wong Y.H., Loh H.H.
Annu. Rev. Pharmacol. Toxicol. 40:389-430(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[25]"Calmodulin regulation of basal and agonist-stimulated G protein coupling by the mu-opioid receptor (OP(3)) in morphine-pretreated cell."
Wang D., Surratt C.K., Sadee W.
J. Neurochem. 75:763-771(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273 AND ARG-275.
[26]"Interactions of opioid and chemokine receptors: oligomerization of mu, kappa, and delta with CCR5 on immune cells."
Suzuki S., Chuang L.F., Yau P., Doi R.H., Chuang R.Y.
Exp. Cell Res. 280:192-200(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH CCR5.
[27]"Agonists activate Gi1 alpha or Gi2 alpha fused to the human mu opioid receptor differently."
Massotte D., Brillet K., Kieffer B., Milligan G.
J. Neurochem. 81:1372-1382(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COUPLING TO GNAI1 AND GNAI2.
[28]"Selective interactions between helix VIII of the human mu-opioid receptors and the C terminus of periplakin disrupt G protein activation."
Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G.
J. Biol. Chem. 278:33400-33407(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPL.
[29]"Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking."
Onoprishvili I., Andria M.L., Kramer H.K., Ancevska-Taneva N., Hiller J.M., Simon E.J.
Mol. Pharmacol. 64:1092-1100(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNA.
[30]"Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer."
Wang D., Sun X., Bohn L.M., Sadee W.
Mol. Pharmacol. 67:2173-2184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOOLIGOMERIZATION, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1 AND OPRK1.
[31]"Functional complementation and the analysis of opioid receptor homodimerization."
Pascal G., Milligan G.
Mol. Pharmacol. 68:905-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOOLIGOMERIZATION.
[32]"The opioid ligand binding of human mu-opioid receptor is modulated by novel splice variants of the receptor."
Choi H.S., Kim C.S., Hwang C.K., Song K.Y., Wang W., Qiu Y., Law P.Y., Wei L.N., Loh H.H.
Biochem. Biophys. Res. Commun. 343:1132-1140(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 16 AND 17), FUNCTION (ISOFORMS 16 AND 17), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
[33]"A member of the heat shock protein 40 family, hlj1, binds to the carboxyl tail of the human mu opioid receptor."
Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., Simon E.J.
Brain Res. 1081:28-33(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJB4.
[34]"Physical association between neuropeptide FF and micro-opioid receptors as a possible molecular basis for anti-opioid activity."
Roumy M., Lorenzo C., Mazeres S., Bouchet S., Zajac J.M., Mollereau C.
J. Biol. Chem. 282:8332-8342(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH NPFFR2.
[35]"Membrane functional organisation and dynamic of mu-opioid receptors."
Lopez A., Salome L.
Cell. Mol. Life Sci. 66:2093-2108(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[36]"Regulation of mu opioid receptor internalization by the scaffold protein RanBPM."
Talbot J.N., Skifter D.A., Bianchi E., Monaghan D.T., Toews M.L., Murrin L.C.
Neurosci. Lett. 466:154-158(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[37]"Interaction of the mu-opioid receptor with GPR177 (Wntless) inhibits Wnt secretion: potential implications for opioid dependence."
Jin J., Kittanakom S., Wong V., Reyes B.A., Van Bockstaele E.J., Stagljar I., Berrettini W., Levenson R.
BMC Neurosci. 11:33-33(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WLS.
[38]"A novel alternatively spliced isoform of the mu-opioid receptor: functional antagonism."
Gris P., Gauthier J., Cheng P., Gibson D.G., Gris D., Laur O., Pierson J., Wentworth S., Nackley A.G., Maixner W., Diatchenko L.
Mol. Pain 6:33-33(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 12), SUBCELLULAR LOCATION (ISOFORM 12).
[39]"Mu opioid receptor gene variants: lack of association with alcohol dependence."
Bergen A.W., Kokoszka J., Peterson R., Long J.C., Virkkunen M., Linnoila M., Goldman D.
Mol. Psychiatry 2:490-494(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-6; ASP-40 AND CYS-147.
[40]"Single-nucleotide polymorphism in the human mu opioid receptor gene alters beta-endorphin binding and activity: possible implications for opiate addiction."
Bond C., LaForge K.S., Tian M., Melia D., Zhang S., Borg L., Gong J., Schluger J., Strong J.A., Leal S.M., Tischfield J.A., Kreek M.J., Yu L.
Proc. Natl. Acad. Sci. U.S.A. 95:9608-9613(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-6; ASP-40 AND HIS-260.
+Additional computationally mapped references.

Web resources

Wikipedia

Mu opioid receptor entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25119 mRNA. Translation: AAA20580.1.
U12569 mRNA. Translation: AAB60354.1.
L29301 mRNA. Translation: AAA73958.1.
AY036622 mRNA. Translation: AAK74189.1.
AY036623 mRNA. Translation: AAK74190.1.
AY195733 mRNA. Translation: AAO21305.1.
AY225404 mRNA. Translation: AAP44727.1.
AY309001 mRNA. Translation: AAQ77385.1.
AY309005 mRNA. Translation: AAQ77389.1.
AY309006 mRNA. Translation: AAQ77390.1.
AY309007 mRNA. Translation: AAQ77391.1.
AY309008 mRNA. Translation: AAQ77392.1.
AY309009 mRNA. Translation: AAQ77393.1.
EU340241 mRNA. Translation: ACA49726.1.
EU340242 mRNA. Translation: ACA49727.1.
EU340243 mRNA. Translation: ACA49728.1.
AY364230 mRNA. Translation: AAR12887.1.
AY364890 mRNA. Translation: AAR11568.1.
HQ699462 mRNA. Translation: AET97615.1.
EU360599 mRNA. Translation: ABY61366.1.
EU362990 mRNA. Translation: ABY66530.1.
AK313901 mRNA. Translation: BAG36624.1.
AY521028 mRNA. Translation: AAS00462.1.
AY587764 Genomic DNA. Translation: AAS83107.1.
FJ041292 mRNA. Translation: ACM90350.1.
FJ041293 mRNA. Translation: ACM90351.1.
FJ041294 mRNA. Translation: ACM90352.1.
AL132774, AL136444 Genomic DNA. Translation: CAI20458.1. Different initiation.
AL445220 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW47705.1. Different initiation.
BC074927 mRNA. Translation: AAH74927.1.
AY292290 Genomic DNA. Translation: AAP44409.1.
AY292291 Genomic DNA. Translation: AAP44410.1.
AF153500 Genomic DNA. Translation: AAD44318.1.
PIRI56553.
S65693.
RefSeqNP_000905.3. NM_000914.4.
NP_001008503.2. NM_001008503.2.
NP_001008504.2. NM_001008504.3.
NP_001008505.2. NM_001008505.2.
NP_001138751.1. NM_001145279.3.
NP_001138752.1. NM_001145280.3.
NP_001138753.1. NM_001145281.2.
NP_001138754.1. NM_001145282.2.
NP_001138755.1. NM_001145283.2.
NP_001138756.1. NM_001145284.3.
NP_001138757.1. NM_001145285.2.
NP_001138758.1. NM_001145286.2.
NP_001138759.1. NM_001145287.2.
NP_001272452.1. NM_001285523.1.
NP_001272453.1. NM_001285524.1.
NP_001272455.1. NM_001285526.1.
NP_001272456.1. NM_001285527.1.
NP_001272457.1. NM_001285528.1.
UniGeneHs.2353.

3D structure databases

DisProtDP00272.
ProteinModelPortalP35372.
SMRP35372. Positions 67-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111033. 7 interactions.
IntActP35372. 15 interactions.
MINTMINT-100121.

Chemistry

BindingDBP35372.
ChEMBLCHEMBL2095149.
DrugBankDB00802. Alfentanil.
DB00913. Anileridine.
DB00921. Buprenorphine.
DB00611. Butorphanol.
DB00318. Codeine.
DB01209. Dezocine.
DB01081. Diphenoxylate.
DB00813. Fentanyl.
DB00956. Hydrocodone.
DB00327. Hydromorphone.
DB00504. Levallorphan.
DB01227. Levomethadyl Acetate.
DB00854. Levorphanol.
DB00836. Loperamide.
DB00333. Methadone.
DB01433. Methadyl Acetate.
DB00295. Morphine.
DB00844. Nalbuphine.
DB01183. Naloxone.
DB00704. Naltrexone.
DB00497. Oxycodone.
DB01192. Oxymorphone.
DB00652. Pentazocine.
DB00647. Propoxyphene.
DB00899. Remifentanil.
DB00708. Sufentanil.
DB00193. Tramadol.
GuidetoPHARMACOLOGY319.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35372.

Polymorphism databases

DMDM2851402.

Proteomic databases

PaxDbP35372.
PRIDEP35372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000229768; ENSP00000229768; ENSG00000112038. [P35372-3]
ENST00000330432; ENSP00000328264; ENSG00000112038. [P35372-1]
ENST00000337049; ENSP00000338381; ENSG00000112038. [P35372-5]
ENST00000360422; ENSP00000353598; ENSG00000112038. [P35372-6]
ENST00000414028; ENSP00000399359; ENSG00000112038. [P35372-4]
ENST00000419506; ENSP00000403549; ENSG00000112038. [P35372-9]
ENST00000428397; ENSP00000411903; ENSG00000112038. [P35372-2]
ENST00000434900; ENSP00000394624; ENSG00000112038. [P35372-10]
ENST00000435918; ENSP00000413752; ENSG00000112038. [P35372-8]
ENST00000452687; ENSP00000410497; ENSG00000112038. [P35372-7]
ENST00000518759; ENSP00000430260; ENSG00000112038. [P35372-13]
ENST00000519083; ENSP00000431048; ENSG00000112038. [P35372-6]
ENST00000520708; ENSP00000430876; ENSG00000112038. [P35372-12]
ENST00000522236; ENSP00000429373; ENSG00000112038. [P35372-12]
ENST00000522555; ENSP00000429719; ENSG00000112038. [P35372-12]
ENST00000522739; ENSP00000428018; ENSG00000112038. [P35372-6]
ENST00000524150; ENSP00000430575; ENSG00000112038. [P35372-18]
ENST00000524163; ENSP00000430097; ENSG00000112038. [P35372-11]
GeneID4988.
KEGGhsa:4988.
UCSCuc003qpn.2. human. [P35372-2]
uc003qpo.1. human. [P35372-3]
uc003qpq.1. human. [P35372-7]
uc003qpr.2. human. [P35372-1]
uc003qpt.1. human. [P35372-5]
uc003qpu.2. human. [P35372-15]
uc011efb.2. human. [P35372-10]
uc011efc.1. human. [P35372-13]
uc011eff.1. human. [P35372-9]
uc011efg.1. human. [P35372-11]
uc011efh.1. human. [P35372-8]
uc011efi.2. human. [P35372-4]

Organism-specific databases

CTD4988.
GeneCardsGC06P154391.
HGNCHGNC:8156. OPRM1.
HPAHPA014509.
MIM600018. gene.
neXtProtNX_P35372.
PharmGKBPA31945.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279457.
HOGENOMHOG000230486.
HOVERGENHBG106919.
InParanoidP35372.
KOK04215.
OMANSTRVRQ.
TreeFamTF315737.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP35372.
BgeeP35372.
CleanExHS_OPRM1.
GenevestigatorP35372.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWiki%CE%9C-opioid_receptor.
GenomeRNAi4988.
NextBio19206.
PROP35372.
SOURCESearch...

Entry information

Entry nameOPRM_HUMAN
AccessionPrimary (citable) accession number: P35372
Secondary accession number(s): B0FXJ1 expand/collapse secondary AC list , B2R9S7, B8Q1L7, B8Q1L8, B8Q1L9, E7EWZ3, G8XRH6, G8XRH8, Q12930, Q4VWM1, Q4VWM2, Q4VWM3, Q4VWM4, Q4VWM6, Q4VWX6, Q5TDA1, Q6UPP1, Q6UQ80, Q7Z2D8, Q86V80, Q8IWW3, Q8IWW4, Q9UCZ4, Q9UN57
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: March 19, 2014
This is version 142 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries