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Q13255 (GRM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metabotropic glutamate receptor 1

Short name=mGluR1
Gene names
Name:GRM1
Synonyms:GPRC1A, MGLUR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. Ref.1

Subunit structure

Homodimer; disulfide-linked. The PPXXF motif binds HOMER1, HOMER2 and HOMER3. Interacts with SIAH1, RYR1, RYR2, ITPR1, SHANK1, SHANK3 and GRASP By similarity. Ref.5 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Detected in brain.

Involvement in disease

Spinocerebellar ataxia, autosomal recessive, 13 (SCAR13) [MIM:614831]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR13 is characterized by delayed psychomotor development beginning in infancy. Affected individuals show mild to profound mental retardation with poor or absent speech as well as gait and stance ataxia and hyperreflexia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Belongs to the G-protein coupled receptor 3 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseNeurodegeneration
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

activation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

regulation of sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentG-protein coupled receptor homodimeric complex

Inferred from physical interaction Ref.5. Source: FlyBase

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled receptor activity

Traceable author statement Ref.1. Source: UniProtKB

glutamate receptor activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KPNA1P522942EBI-8527352,EBI-358383

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q13255-1)

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 Beta (identifier: Q13255-2)

The sequence of this isoform differs from the canonical sequence as follows:
     887-906: NSNGKSVSWSEPGGGQVPKG → KKRQPEFSPTSQCPSAHVQL
     907-1194: Missing.
Note: Ref.1 (AAA87844) sequence is in conflict in positions: 896:T->S and 904:V->A.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11941176Metabotropic glutamate receptor 1
PRO_0000012922

Regions

Topological domain19 – 592574Extracellular Potential
Transmembrane593 – 61523Helical; Name=1; Potential
Topological domain616 – 62914Cytoplasmic Potential
Transmembrane630 – 65021Helical; Name=2; Potential
Topological domain651 – 66111Extracellular Potential
Transmembrane662 – 68019Helical; Name=3; Potential
Topological domain681 – 70626Cytoplasmic Potential
Transmembrane707 – 72721Helical; Name=4; Potential
Topological domain728 – 75023Extracellular Potential
Transmembrane751 – 77222Helical; Name=5; Potential
Topological domain773 – 78513Cytoplasmic Potential
Transmembrane786 – 80823Helical; Name=6; Potential
Topological domain809 – 8146Extracellular Potential
Transmembrane815 – 84026Helical; Name=7; Potential
Topological domain841 – 1194354Cytoplasmic Potential
Region186 – 1883Glutamate binding By similarity
Compositional bias1014 – 103522Gln/Pro-rich
Compositional bias1067 – 108115Gln/Pro-rich
Compositional bias1095 – 113036Asp/Glu-rich (acidic)
Compositional bias1142 – 119453Ser-rich

Sites

Binding site741Glutamate By similarity
Binding site1651Glutamate By similarity
Binding site2361Glutamate By similarity
Binding site3181Glutamate By similarity
Binding site4091Glutamate By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Ref.7
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 109 Ref.5 Ref.7
Disulfide bond140Interchain Ref.5 Ref.7
Disulfide bond289 ↔ 291 By similarity
Disulfide bond378 ↔ 394 Ref.5 Ref.7
Disulfide bond432 ↔ 439 Ref.5 Ref.7

Natural variations

Alternative sequence887 – 90620NSNGK…QVPKG → KKRQPEFSPTSQCPSAHVQL in isoform Beta.
VSP_002024
Alternative sequence907 – 1194288Missing in isoform Beta.
VSP_002025
Natural variant341S → Y.
Corresponds to variant rs12190109 [ dbSNP | Ensembl ].
VAR_028184
Natural variant2851R → K.
Corresponds to variant rs7760248 [ dbSNP | Ensembl ].
VAR_028185
Natural variant5931S → P. Ref.1
Corresponds to variant rs1047005 [ dbSNP | Ensembl ].
VAR_055875
Natural variant6961R → W in a colorectal cancer sample; somatic mutation. Ref.8
VAR_036194
Natural variant7411E → D.
Corresponds to variant rs3025919 [ dbSNP | Ensembl ].
VAR_028186
Natural variant8841G → E.
Corresponds to variant rs362936 [ dbSNP | Ensembl ].
VAR_028187
Natural variant9291V → I.
Corresponds to variant rs2941 [ dbSNP | Ensembl ].
VAR_024482
Natural variant9931S → P. Ref.1 Ref.2
Corresponds to variant rs6923492 [ dbSNP | Ensembl ].
VAR_028188

Secondary structure

.................................................................................. 1194
Helix Strand Turn

Details...

Sequences

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

Last modified November 2, 2010. Version 3.
Checksum: 0A633505F6D51909

FASTA1,194132,357
        10         20         30         40         50         60 
MVGLLLFFFP AIFLEVSLLP RSPGRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE 

        70         80         90        100        110        120 
KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI 

       130        140        150        160        170        180 
EFIRDSLISI RDEKDGINRC LPDGQSLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI 

       190        200        210        220        230        240 
PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG 

       250        260        270        280        290        300 
MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL 

       310        320        330        340        350        360 
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD 

       370        380        390        400        410        420 
TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KRICTGNESL EENYVQDSKM GFVINAIYAM 

       430        440        450        460        470        480 
AHGLQNMHHA LCPGHVGLCD AMKPIDGSKL LDFLIKSSFI GVSGEEVWFD EKGDAPGRYD 

       490        500        510        520        530        540 
IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGVV RSVCSEPCLK GQIKVIRKGE 

       550        560        570        580        590        600 
VSCCWICTAC KENEYVQDEF TCKACDLGWW PNADLTGCEP IPVRYLEWSN IESIIAIAFS 

       610        620        630        640        650        660 
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ 

       670        680        690        700        710        720 
RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL 

       730        740        750        760        770        780 
VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPLGYN GLLIMSCTYY AFKTRNVPAN 

       790        800        810        820        830        840 
FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA 

       850        860        870        880        890        900 
KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK AGAGNANSNG KSVSWSEPGG 

       910        920        930        940        950        960 
GQVPKGQHMW HRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDTS TKTLYNVEEE 

       970        980        990       1000       1010       1020 
EDAQPIRFSP PGSPSMVVHR RVPSAATTPP LPSHLTAEET PLFLAEPALP KGLPPPLQQQ 

      1030       1040       1050       1060       1070       1080 
QQPPPQQKSL MDQLQGVVSN FSTAIPDFHA VLAGPGGPGN GLRSLYPPPP PPQHLQMLPL 

      1090       1100       1110       1120       1130       1140 
QLSTFGEELV SPPADDDDDS ERFKLLQEYV YEHEREGNTE EDELEEEEED LQAASKLTPD 

      1150       1160       1170       1180       1190 
DSPALTPPSP FRDSVASGSS VPSSPVSESV LCTPPNVSYA SVILRDYKQS SSTL 

« Hide

Isoform Beta [UniParc].

Checksum: D63470CF9A15361E
Show »

FASTA906101,323

References

« Hide 'large scale' references
[1]"Cloning and expression of a human metabotropic glutamate receptor 1 alpha: enhanced coupling on co-transfection with a glutamate transporter."
Desai M.A., Burnett J.P., Mayne N.G., Schoepp D.D.
Mol. Pharmacol. 48:648-657(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), FUNCTION, VARIANTS PRO-593 AND PRO-993.
[2]"Human metabotropic glutamate receptor 1: mRNA distribution, chromosome localization and functional expression of two splice variants."
Stephan D., Bon C., Holzwarth J.A., Galvan M., Pruss R.M.
Neuropharmacology 35:1649-1660(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), VARIANT PRO-993.
[3]"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].
[4]"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 ALPHA).
Tissue: Testis.
[5]"Cys-140 is critical for metabotropic glutamate receptor-1 dimerization."
Ray K., Hauschild B.C.
J. Biol. Chem. 275:34245-34251(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN DISULFIDE BOND.
[6]"Autosomal-recessive congenital cerebellar ataxia is caused by mutations in metabotropic glutamate receptor 1."
Guergueltcheva V., Azmanov D.N., Angelicheva D., Smith K.R., Chamova T., Florez L., Bynevelt M., Nguyen T., Cherninkova S., Bojinova V., Kaprelyan A., Angelova L., Morar B., Chandler D., Kaneva R., Bahlo M., Tournev I., Kalaydjieva L.
Am. J. Hum. Genet. 91:553-564(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCAR13.
[7]"Metabotropic glutamate receptor mGluR1 complexed with LY341495 antagonist."
Structural genomics consortium (SGC)
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 28-518 IN COMPLEX WITH ANTAGONIST LY341495, GLYCOSYLATION AT ASN-223, DISULFIDE BONDS.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-696.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31215 mRNA. Translation: AAA87843.1.
U31216 mRNA. Translation: AAA87844.1.
L76627 mRNA. Translation: AAB05337.1.
L76631 mRNA. Translation: AAB05338.1.
AL592423, AL035698, AL096867 Genomic DNA. Translation: CAH71181.1.
AL592423, AL035698, AL096867 Genomic DNA. Translation: CAH71182.1.
AL096867, AL592423, AL035698 Genomic DNA. Translation: CAI20335.1.
AL096867, AL035698, AL592423 Genomic DNA. Translation: CAI20336.1.
AL035698, AL096867, AL592423 Genomic DNA. Translation: CAI22468.1.
AL035698, AL096867, AL592423 Genomic DNA. Translation: CAI22469.1.
BC136280 mRNA. Translation: AAI36281.1.
RefSeqNP_001264993.1. NM_001278064.1.
NP_001264994.1. NM_001278065.1.
NP_001264995.1. NM_001278066.1.
NP_001264996.1. NM_001278067.1.
UniGeneHs.32945.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KS9X-ray1.90A/B28-518[»]
ProteinModelPortalQ13255.
SMRQ13255. Positions 35-582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109168. 6 interactions.
IntActQ13255. 2 interactions.
MINTMINT-2806316.

Chemistry

BindingDBQ13255.
ChEMBLCHEMBL3772.
DrugBankDB00659. Acamprosate.
DB00142. L-Glutamic Acid.
GuidetoPHARMACOLOGY289.

Protein family/group databases

TCDB9.A.14.7.1. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteQ13255.

Polymorphism databases

DMDM311033443.

Proteomic databases

PaxDbQ13255.
PRIDEQ13255.

Protocols and materials databases

DNASU2911.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282753; ENSP00000282753; ENSG00000152822. [Q13255-1]
ENST00000361719; ENSP00000354896; ENSG00000152822. [Q13255-1]
ENST00000392299; ENSP00000376119; ENSG00000152822. [Q13255-2]
ENST00000492807; ENSP00000424095; ENSG00000152822. [Q13255-2]
ENST00000507907; ENSP00000425599; ENSG00000152822. [Q13255-2]
GeneID2911.
KEGGhsa:2911.
UCSCuc003qll.3. human. [Q13255-2]
uc010khw.2. human. [Q13255-1]

Organism-specific databases

CTD2911.
GeneCardsGC06P146390.
HGNCHGNC:4593. GRM1.
HPAHPA015701.
MIM604473. gene.
614831. phenotype.
neXtProtNX_Q13255.
Orphanet324262. Autosomal recessive congenital cerebellar ataxia due to MGLUR1 deficiency.
PharmGKBPA28990.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295200.
HOVERGENHBG107965.
InParanoidQ13255.
KOK04603.
OMAKTNETAC.
OrthoDBEOG7Z0JXG.
PhylomeDBQ13255.
TreeFamTF313240.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ13255.

Gene expression databases

ArrayExpressQ13255.
BgeeQ13255.
GenevestigatorQ13255.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR000337. GPCR_3.
IPR011500. GPCR_3_9-Cys_dom.
IPR017978. GPCR_3_C.
IPR017979. GPCR_3_CS.
IPR000162. GPCR_3_mtglu_rcpt.
IPR001256. GPCR_3_mtglu_rcpt_1.
IPR019588. Metabotropic_Glu_rcpt_Homer-bd.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF10606. GluR_Homer-bdg. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view]
PRINTSPR00248. GPCRMGR.
PR01051. MTABOTROPC1R.
PR00593. MTABOTROPICR.
SUPFAMSSF53822. SSF53822. 1 hit.
PROSITEPS00979. G_PROTEIN_RECEP_F3_1. 1 hit.
PS00980. G_PROTEIN_RECEP_F3_2. 1 hit.
PS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13255.
GeneWikiMetabotropic_glutamate_receptor_1.
GenomeRNAi2911.
NextBio11539.
PROQ13255.
SOURCESearch...

Entry information

Entry nameGRM1_HUMAN
AccessionPrimary (citable) accession number: Q13255
Secondary accession number(s): B9EG79 expand/collapse secondary AC list , Q13256, Q14757, Q14758, Q5VTF7, Q5VTF8, Q9NU10, Q9UGS9, Q9UGT0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 134 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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