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Q13255

- GRM1_HUMAN

UniProt

Q13255 - GRM1_HUMAN

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Protein

Metabotropic glutamate receptor 1

Gene

GRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Enzyme regulationi

Signaling is inhibited by the antagonist LY341495. The LY341495 binding site partially overlaps with the glutamate binding site. Signaling is also inhibited by synthetic allosteric regulators, such as FITM (4-fluoro-N-(4-(6-(isopropylamino)pyrimidin-4-yl)thiazol-2-yl)-N-methylbenzamide) that bind in a pocket between the transmembrane helices.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei74 – 741GlutamateCurated
Binding sitei165 – 1651GlutamateCurated
Binding sitei236 – 2361GlutamateBy similarity
Binding sitei318 – 3181GlutamateBy similarity
Binding sitei409 – 4091GlutamateBy similarity

GO - Molecular functioni

  1. glutamate receptor activity Source: UniProtKB
  2. G-protein coupled receptor activity Source: UniProtKB

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. activation of MAPKK activity Source: Ensembl
  3. cell death Source: UniProtKB-KW
  4. cellular response to electrical stimulus Source: Ensembl
  5. dimeric G-protein coupled receptor signaling pathway Source: UniProtKB
  6. G-protein coupled glutamate receptor signaling pathway Source: UniProtKB
  7. G-protein coupled receptor signaling pathway Source: UniProtKB
  8. locomotory behavior Source: Ensembl
  9. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
  10. protein kinase C-activating G-protein coupled receptor signaling pathway Source: RefGenome
  11. regulation of sensory perception of pain Source: Ensembl
  12. regulation of synaptic transmission, glutamatergic Source: RefGenome
  13. sensory perception of pain Source: Ensembl
  14. synaptic transmission Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
SignaLinkiQ13255.

Protein family/group databases

TCDBi9.A.14.7.1. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Metabotropic glutamate receptor 1
Short name:
mGluR1
Gene namesi
Name:GRM1
Synonyms:GPRC1A, MGLUR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4593. GRM1.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. dendrite Source: Ensembl
  2. G-protein coupled receptor dimeric complex Source: UniProtKB
  3. G-protein coupled receptor homodimeric complex Source: FlyBase
  4. integral component of plasma membrane Source: UniProtKB
  5. nucleus Source: Ensembl
  6. plasma membrane Source: Reactome
  7. postsynaptic density Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Neurodegeneration

Organism-specific databases

MIMi614831. phenotype.
Orphaneti324262. Autosomal recessive congenital cerebellar ataxia due to MGLUR1 deficiency.
404507. Chondromyxoid fibroma.
PharmGKBiPA28990.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 11941176Metabotropic glutamate receptor 1PRO_0000012922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 109
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi140 – 140Interchain
Glycosylationi223 – 2231N-linked (GlcNAc...)1 Publication
Disulfide bondi289 ↔ 291By similarity
Disulfide bondi378 ↔ 394
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi432 ↔ 439
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi657 ↔ 746

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ13255.
PRIDEiQ13255.

PTM databases

PhosphoSiteiQ13255.

Expressioni

Tissue specificityi

Detected in brain.

Gene expression databases

BgeeiQ13255.
ExpressionAtlasiQ13255. baseline and differential.
GenevestigatoriQ13255.

Organism-specific databases

HPAiHPA015701.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA1P522942EBI-8527352,EBI-358383

Protein-protein interaction databases

BioGridi109168. 6 interactions.
IntActiQ13255. 2 interactions.
MINTiMINT-2806316.

Structurei

Secondary structure

1
1194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413
Beta strandi44 – 518
Helixi59 – 613
Turni62 – 654
Turni72 – 754
Helixi76 – 9015
Beta strandi93 – 964
Beta strandi101 – 1077
Helixi112 – 12312
Beta strandi156 – 1605
Helixi165 – 17511
Helixi176 – 1783
Beta strandi182 – 1865
Helixi190 – 1934
Turni195 – 1973
Beta strandi201 – 2055
Helixi209 – 22113
Beta strandi226 – 2349
Helixi235 – 25016
Beta strandi254 – 2618
Helixi267 – 27812
Turni279 – 2846
Beta strandi286 – 2905
Helixi293 – 30614
Beta strandi313 – 3164
Turni318 – 3225
Helixi324 – 3274
Helixi331 – 3344
Beta strandi338 – 3425
Helixi348 – 3547
Turni359 – 3613
Helixi368 – 3758
Beta strandi391 – 3933
Turni400 – 4034
Helixi410 – 43122
Helixi440 – 4423
Helixi447 – 4559
Beta strandi458 – 4603
Beta strandi466 – 4683
Beta strandi478 – 4869
Beta strandi492 – 50110
Beta strandi504 – 5074
Turni509 – 5113
Helixi591 – 61626
Beta strandi618 – 6203
Helixi621 – 6244
Helixi628 – 64922
Helixi654 – 68532
Helixi703 – 72725
Beta strandi732 – 7354
Beta strandi738 – 7403
Beta strandi742 – 7465
Helixi750 – 77324
Turni774 – 7763
Helixi779 – 80729
Helixi811 – 83929

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KS9X-ray1.90A/B28-518[»]
4OR2X-ray2.80A/B581-860[»]
ProteinModelPortaliQ13255.
SMRiQ13255. Positions 35-846.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13255.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 592574Extracellular1 PublicationAdd
BLAST
Topological domaini616 – 62914Cytoplasmic1 PublicationAdd
BLAST
Topological domaini651 – 6588Extracellular1 Publication
Topological domaini681 – 70323Cytoplasmic1 PublicationAdd
BLAST
Topological domaini728 – 75023Extracellular1 PublicationAdd
BLAST
Topological domaini773 – 78513Cytoplasmic1 PublicationAdd
BLAST
Topological domaini808 – 8158Extracellular1 Publication
Topological domaini841 – 1194354Cytoplasmic1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei593 – 61523Helical; Name=1Add
BLAST
Transmembranei630 – 65021Helical; Name=2Add
BLAST
Transmembranei659 – 68022Helical; Name=3Add
BLAST
Transmembranei704 – 72724Helical; Name=4Add
BLAST
Transmembranei751 – 77222Helical; Name=5Add
BLAST
Transmembranei786 – 80722Helical; Name=6Add
BLAST
Transmembranei816 – 84025Helical; Name=7Add
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 1883Glutamate bindingCurated

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1014 – 103522Gln/Pro-richAdd
BLAST
Compositional biasi1067 – 108115Gln/Pro-richAdd
BLAST
Compositional biasi1095 – 113036Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi1142 – 119453Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295200.
GeneTreeiENSGT00760000118884.
HOVERGENiHBG107965.
InParanoidiQ13255.
KOiK04603.
OMAiKTNETAC.
OrthoDBiEOG7Z0JXG.
PhylomeDBiQ13255.
TreeFamiTF313240.

Family and domain databases

InterProiIPR001828. 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]
PfamiPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF10606. GluR_Homer-bdg. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view]
PRINTSiPR00248. GPCRMGR.
PR01051. MTABOTROPC1R.
PR00593. MTABOTROPICR.
SUPFAMiSSF53822. SSF53822. 1 hit.
PROSITEiPS00979. 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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q13255-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVGLLLFFFP AIFLEVSLLP RSPGRKVLLA GASSQRSVAR MDGDVIIGAL
60 70 80 90 100
FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT
110 120 130 140 150
LGSEIRDSCW HSSVALEQSI EFIRDSLISI RDEKDGINRC LPDGQSLPPG
160 170 180 190 200
RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI PQIAYSATSI DLSDKTLYKY
210 220 230 240 250
FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG MDAFKELAAQ
260 270 280 290 300
EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
310 320 330 340 350
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF
360 370 380 390 400
DDYFLKLRLD TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KRICTGNESL
410 420 430 440 450
EENYVQDSKM GFVINAIYAM AHGLQNMHHA LCPGHVGLCD AMKPIDGSKL
460 470 480 490 500
LDFLIKSSFI GVSGEEVWFD EKGDAPGRYD IMNLQYTEAN RYDYVHVGTW
510 520 530 540 550
HEGVLNIDDY KIQMNKSGVV RSVCSEPCLK GQIKVIRKGE VSCCWICTAC
560 570 580 590 600
KENEYVQDEF TCKACDLGWW PNADLTGCEP IPVRYLEWSN IESIIAIAFS
610 620 630 640 650
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA
660 670 680 690 700
KPTTTSCYLQ RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF
710 720 730 740 750
MSAWAQVIIA SILISVQLTL VVTLIIMEPP MPILSYPSIK EVYLICNTSN
760 770 780 790 800
LGVVAPLGYN GLLIMSCTYY AFKTRNVPAN FNEAKYIAFT MYTTCIIWLA
810 820 830 840 850
FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA KPERNVRSAF
860 870 880 890 900
TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK AGAGNANSNG KSVSWSEPGG
910 920 930 940 950
GQVPKGQHMW HRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDTS
960 970 980 990 1000
TKTLYNVEEE EDAQPIRFSP PGSPSMVVHR RVPSAATTPP LPSHLTAEET
1010 1020 1030 1040 1050
PLFLAEPALP KGLPPPLQQQ QQPPPQQKSL MDQLQGVVSN FSTAIPDFHA
1060 1070 1080 1090 1100
VLAGPGGPGN GLRSLYPPPP PPQHLQMLPL QLSTFGEELV SPPADDDDDS
1110 1120 1130 1140 1150
ERFKLLQEYV YEHEREGNTE EDELEEEEED LQAASKLTPD DSPALTPPSP
1160 1170 1180 1190
FRDSVASGSS VPSSPVSESV LCTPPNVSYA SVILRDYKQS SSTL
Length:1,194
Mass (Da):132,357
Last modified:November 2, 2010 - v3
Checksum:i0A633505F6D51909
GO
Isoform Beta (identifier: Q13255-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     887-906: NSNGKSVSWSEPGGGQVPKG → KKRQPEFSPTSQCPSAHVQL
     907-1194: Missing.

Show »
Length:906
Mass (Da):101,323
Checksum:iD63470CF9A15361E
GO
Isoform 3 (identifier: Q13255-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     887-908: NSNGKSVSWSEPGGGQVPKGQH → KWRTGAQGTAYVAPPLCAREDQ
     909-1194: Missing.

Note: No experimental confirmation available.

Show »
Length:908
Mass (Da):101,473
Checksum:i214EC733A9D585B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform Beta (identifier: Q13255-2)
Sequence conflicti896 – 8961T → S in AAA87844. (PubMed:7476890)Curated
Sequence conflicti904 – 9041V → A in AAA87844. (PubMed:7476890)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341S → Y.
Corresponds to variant rs12190109 [ dbSNP | Ensembl ].
VAR_028184
Natural varianti285 – 2851R → K.
Corresponds to variant rs7760248 [ dbSNP | Ensembl ].
VAR_028185
Natural varianti593 – 5931S → P.1 Publication
Corresponds to variant rs1047005 [ dbSNP | Ensembl ].
VAR_055875
Natural varianti696 – 6961R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036194
Natural varianti741 – 7411E → D.
Corresponds to variant rs3025919 [ dbSNP | Ensembl ].
VAR_028186
Natural varianti884 – 8841G → E.
Corresponds to variant rs362936 [ dbSNP | Ensembl ].
VAR_028187
Natural varianti929 – 9291V → I.
Corresponds to variant rs2941 [ dbSNP | Ensembl ].
VAR_024482
Natural varianti993 – 9931S → P.2 Publications
Corresponds to variant rs6923492 [ dbSNP | Ensembl ].
VAR_028188

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei887 – 90822NSNGK…PKGQH → KWRTGAQGTAYVAPPLCARE DQ in isoform 3. 1 PublicationVSP_055127Add
BLAST
Alternative sequencei887 – 90620NSNGK…QVPKG → KKRQPEFSPTSQCPSAHVQL in isoform Beta. 2 PublicationsVSP_002024Add
BLAST
Alternative sequencei907 – 1194288Missing in isoform Beta. 2 PublicationsVSP_002025Add
BLAST
Alternative sequencei909 – 1194286Missing in isoform 3. 1 PublicationVSP_055128Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31215 mRNA. Translation: AAA87843.1.
U31216 mRNA. Translation: AAA87844.1.
L76627 mRNA. Translation: AAB05337.1.
L76631 mRNA. Translation: AAB05338.1.
AL031769 Genomic DNA. No translation available.
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.
BC143779 mRNA. No translation available.
CCDSiCCDS47497.1. [Q13255-2]
CCDS5209.1. [Q13255-1]
CCDS64548.1. [Q13255-3]
RefSeqiNP_001264993.1. NM_001278064.1. [Q13255-1]
NP_001264994.1. NM_001278065.1. [Q13255-2]
NP_001264995.1. NM_001278066.1. [Q13255-2]
NP_001264996.1. NM_001278067.1. [Q13255-3]
XP_006715530.1. XM_006715467.1. [Q13255-2]
UniGeneiHs.32945.

Genome annotation databases

EnsembliENST00000282753; ENSP00000282753; ENSG00000152822. [Q13255-1]
ENST00000355289; ENSP00000347437; ENSG00000152822. [Q13255-3]
ENST00000361719; ENSP00000354896; ENSG00000152822. [Q13255-1]
ENST00000492807; ENSP00000424095; ENSG00000152822. [Q13255-2]
ENST00000507907; ENSP00000425599; ENSG00000152822. [Q13255-2]
GeneIDi2911.
KEGGihsa:2911.
UCSCiuc003qll.3. human. [Q13255-2]
uc010khw.2. human. [Q13255-1]

Polymorphism databases

DMDMi311033443.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31215 mRNA. Translation: AAA87843.1 .
U31216 mRNA. Translation: AAA87844.1 .
L76627 mRNA. Translation: AAB05337.1 .
L76631 mRNA. Translation: AAB05338.1 .
AL031769 Genomic DNA. No translation available.
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 .
BC143779 mRNA. No translation available.
CCDSi CCDS47497.1. [Q13255-2 ]
CCDS5209.1. [Q13255-1 ]
CCDS64548.1. [Q13255-3 ]
RefSeqi NP_001264993.1. NM_001278064.1. [Q13255-1 ]
NP_001264994.1. NM_001278065.1. [Q13255-2 ]
NP_001264995.1. NM_001278066.1. [Q13255-2 ]
NP_001264996.1. NM_001278067.1. [Q13255-3 ]
XP_006715530.1. XM_006715467.1. [Q13255-2 ]
UniGenei Hs.32945.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3KS9 X-ray 1.90 A/B 28-518 [» ]
4OR2 X-ray 2.80 A/B 581-860 [» ]
ProteinModelPortali Q13255.
SMRi Q13255. Positions 35-846.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109168. 6 interactions.
IntActi Q13255. 2 interactions.
MINTi MINT-2806316.

Chemistry

BindingDBi Q13255.
ChEMBLi CHEMBL3772.
GuidetoPHARMACOLOGYi 289.

Protein family/group databases

TCDBi 9.A.14.7.1. the g-protein-coupled receptor (gpcr) family.
GPCRDBi Search...

PTM databases

PhosphoSitei Q13255.

Polymorphism databases

DMDMi 311033443.

Proteomic databases

PaxDbi Q13255.
PRIDEi Q13255.

Protocols and materials databases

DNASUi 2911.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282753 ; ENSP00000282753 ; ENSG00000152822 . [Q13255-1 ]
ENST00000355289 ; ENSP00000347437 ; ENSG00000152822 . [Q13255-3 ]
ENST00000361719 ; ENSP00000354896 ; ENSG00000152822 . [Q13255-1 ]
ENST00000492807 ; ENSP00000424095 ; ENSG00000152822 . [Q13255-2 ]
ENST00000507907 ; ENSP00000425599 ; ENSG00000152822 . [Q13255-2 ]
GeneIDi 2911.
KEGGi hsa:2911.
UCSCi uc003qll.3. human. [Q13255-2 ]
uc010khw.2. human. [Q13255-1 ]

Organism-specific databases

CTDi 2911.
GeneCardsi GC06P146390.
HGNCi HGNC:4593. GRM1.
HPAi HPA015701.
MIMi 604473. gene.
614831. phenotype.
neXtProti NX_Q13255.
Orphaneti 324262. Autosomal recessive congenital cerebellar ataxia due to MGLUR1 deficiency.
404507. Chondromyxoid fibroma.
PharmGKBi PA28990.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295200.
GeneTreei ENSGT00760000118884.
HOVERGENi HBG107965.
InParanoidi Q13255.
KOi K04603.
OMAi KTNETAC.
OrthoDBi EOG7Z0JXG.
PhylomeDBi Q13255.
TreeFami TF313240.

Enzyme and pathway databases

Reactomei REACT_18283. G alpha (q) signalling events.
REACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
SignaLinki Q13255.

Miscellaneous databases

EvolutionaryTracei Q13255.
GeneWikii Metabotropic_glutamate_receptor_1.
GenomeRNAii 2911.
NextBioi 11539.
PROi Q13255.
SOURCEi Search...

Gene expression databases

Bgeei Q13255.
ExpressionAtlasi Q13255. baseline and differential.
Genevestigatori Q13255.

Family and domain databases

InterProi IPR001828. 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 ]
Pfami PF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF10606. GluR_Homer-bdg. 1 hit.
PF07562. NCD3G. 1 hit.
[Graphical view ]
PRINTSi PR00248. GPCRMGR.
PR01051. MTABOTROPC1R.
PR00593. MTABOTROPICR.
SUPFAMi SSF53822. SSF53822. 1 hit.
PROSITEi PS00979. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] (ISOFORMS ALPHA AND 3).
    Tissue: Testis.
  5. Cited for: INVOLVEMENT IN SCAR13.
  6. "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.
  7. "Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator."
    Wu H., Wang C., Gregory K.J., Han G.W., Cho H.P., Xia Y., Niswender C.M., Katritch V., Meiler J., Cherezov V., Conn P.J., Stevens R.C.
    Science 344:58-64(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 581-860 IN COMPLEX WITH ALLOSTERIC ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BOND, ENZYME REGULATION.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-696.

Entry informationi

Entry nameiGRM1_HUMAN
AccessioniPrimary (citable) accession number: Q13255
Secondary accession number(s): B9EG79
, F8W805, Q13256, Q14757, Q14758, Q5VTF7, Q5VTF8, Q9NU10, Q9UGS9, Q9UGT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 140 of the entry and version 3 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 6
    Human chromosome 6: 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