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O75899 (GABR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid type B receptor subunit 2

Short name=GABA-B receptor 2
Short name=GABA-B-R2
Short name=GABA-BR2
Short name=GABABR2
Short name=Gb2
Alternative name(s):
G-protein coupled receptor 51
HG20
Gene names
Name:GABBR2
Synonyms:GPR51, GPRC3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length941 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Ref.1 Ref.3 Ref.12 Ref.13 Ref.14

Subunit structure

Heterodimer of GABBR1 and GABBR2. Homodimers may form, but are inactive. Interacts with ATF4 via its C-terminal region. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Note: Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. In contrast, GABBR2 does not depend on GABBR1 for transport to the cell membrane. Ref.1 Ref.3 Ref.11

Tissue specificity

Highly expressed in brain, especially in cerebral cortex, thalamus, hippocampus, frontal, occipital and temporal lobe, occipital pole and cerebellum, followed by corpus callosum, caudate nucleus, spinal cord, amygdala and medulla. Weakly expressed in heart, testis and skeletal muscle. Ref.2 Ref.3 Ref.4

Domain

Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR1.

Sequence similarities

Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily.

Sequence caution

The sequence AAH35071.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

gamma-aminobutyric acid signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of adenylate cyclase activity

Traceable author statement Ref.3. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentG-protein coupled receptor heterodimeric complex

Inferred from physical interaction Ref.1. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled GABA receptor activity

Traceable author statement Ref.3. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NSFP464594EBI-715469,EBI-712251

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 941900Gamma-aminobutyric acid type B receptor subunit 2
PRO_0000012952

Regions

Topological domain42 – 483442Extracellular Potential
Transmembrane484 – 50421Helical; Name=1; Potential
Topological domain505 – 52218Cytoplasmic Potential
Transmembrane523 – 54321Helical; Name=2; Potential
Topological domain544 – 5518Extracellular Potential
Transmembrane552 – 57221Helical; Name=3; Potential
Topological domain573 – 59725Cytoplasmic Potential
Transmembrane598 – 61821Helical; Name=4; Potential
Topological domain619 – 65436Extracellular Potential
Transmembrane655 – 67521Helical; Name=5; Potential
Topological domain676 – 69116Cytoplasmic Potential
Transmembrane692 – 71221Helical; Name=6; Potential
Topological domain713 – 7208Extracellular Potential
Transmembrane721 – 74121Helical; Name=7; Potential
Topological domain742 – 941200Cytoplasmic Potential
Coiled coil781 – 81939 Potential

Amino acid modifications

Modified residue8841Phosphoserine By similarity
Glycosylation901N-linked (GlcNAc...) Ref.13
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Ref.13
Glycosylation4041N-linked (GlcNAc...) Ref.13 Ref.14
Glycosylation4531N-linked (GlcNAc...) Ref.13
Disulfide bond108 ↔ 135 Ref.13 Ref.14
Disulfide bond237 ↔ 266 Ref.13 Ref.14
Disulfide bond265 ↔ 302 Ref.13 Ref.14

Natural variations

Natural variant1631L → P.
Corresponds to variant rs35449008 [ dbSNP | Ensembl ].
VAR_049280
Natural variant6281Y → F. Ref.3
VAR_010148
Natural variant8691T → A. Ref.3
Corresponds to variant rs10985765 [ dbSNP | Ensembl ].
VAR_010149

Experimental info

Mutagenesis1181Y → A: Impairs interaction with GABBR1. Decreases signaling via G-proteins. Ref.13
Sequence conflict61S → R in AAC99345. Ref.2
Sequence conflict121P → R in AAC99345. Ref.2
Sequence conflict4241G → E in AAD30389. Ref.5
Sequence conflict7971R → H in AAH35071. Ref.8

Secondary structure

......................................................................... 941
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75899 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 09F1773DB0673C5D

FASTA941105,821
        10         20         30         40         50         60 
MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP PSSPPLSIMG 

        70         80         90        100        110        120 
LMPLTKEVAK GSIGRGVLPA VELAIEQIRN ESLLRPYFLD LRLYDTECDN AKGLKAFYDA 

       130        140        150        160        170        180 
IKYGPNHLMV FGGVCPSVTS IIAESLQGWN LVQLSFAATT PVLADKKKYP YFFRTVPSDN 

       190        200        210        220        230        240 
AVNPAILKLL KHYQWKRVGT LTQDVQRFSE VRNDLTGVLY GEDIEISDTE SFSNDPCTSV 

       250        260        270        280        290        300 
KKLKGNDVRI ILGQFDQNMA AKVFCCAYEE NMYGSKYQWI IPGWYEPSWW EQVHTEANSS 

       310        320        330        340        350        360 
RCLRKNLLAA MEGYIGVDFE PLSSKQIKTI SGKTPQQYER EYNNKRSGVG PSKFHGYAYD 

       370        380        390        400        410        420 
GIWVIAKTLQ RAMETLHASS RHQRIQDFNY TDHTLGRIIL NAMNETNFFG VTGQVVFRNG 

       430        440        450        460        470        480 
ERMGTIKFTQ FQDSREVKVG EYNAVADTLE IINDTIRFQG SEPPKDKTII LEQLRKISLP 

       490        500        510        520        530        540 
LYSILSALTI LGMIMASAFL FFNIKNRNQK LIKMSSPYMN NLIILGGMLS YASIFLFGLD 

       550        560        570        580        590        600 
GSFVSEKTFE TLCTVRTWIL TVGYTTAFGA MFAKTWRVHA IFKNVKMKKK IIKDQKLLVI 

       610        620        630        640        650        660 
VGGMLLIDLC ILICWQAVDP LRRTVEKYSM EPDPAGRDIS IRPLLEHCEN THMTIWLGIV 

       670        680        690        700        710        720 
YAYKGLLMLF GCFLAWETRN VSIPALNDSK YIGMSVYNVG IMCIIGAAVS FLTRDQPNVQ 

       730        740        750        760        770        780 
FCIVALVIIF CSTITLCLVF VPKLITLRTN PDAATQNRRF QFTQNQKKED SKTSTSVTSV 

       790        800        810        820        830        840 
NQASTSRLEG LQSENHRLRM KITELDKDLE EVTMQLQDTP EKTTYIKQNH YQELNDILNL 

       850        860        870        880        890        900 
GNFTESTDGG KAILKNHLDQ NPQLQWNTTE PSRTCKDPIE DINSPEHIQR RLSLQLPILH 

       910        920        930        940 
HAYLPSIGGV DASCVSPCVS PTASPRHRHV PPSFRVMVSG L 

« Hide

References

« Hide 'large scale' references
[1]"Heterodimerization is required for the formation of a functional GABA(B) receptor."
White J.H., Wise A., Main M.J., Green A., Fraser N.J., Disney G.H., Barnes A.A., Emson P., Foord S.M., Marshall F.H.
Nature 396:679-682(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH GABBR1, SUBCELLULAR LOCATION.
Tissue: Cerebellum.
[2]"Cloning of a novel G-protein-coupled receptor GPR 51 resembling GABAB receptors expressed predominantly in nervous tissues and mapped proximal to the hereditary sensory neuropathy type 1 locus on chromosome 9."
Ng G.Y.K., McDonald T., Bonnert T., Rigby M., Heavens R., Whiting P., Chateauneuf A., Coulombe N., Kargman S., Caskey T., Evans J.F., O'Neill G.P., Liu Q.
Genomics 56:288-295(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal brain.
[3]"Molecular identification of the human GABABR2: cell surface expression and coupling to adenylyl cyclase in the absence of GABABR1."
Martin S.C., Russek S.J., Farb D.H.
Mol. Cell. Neurosci. 13:180-191(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PHE-628 AND ALA-869.
Tissue: Brain.
[4]"Distribution of the GABA(B) receptor subunit gb2 in rat CNS."
Clark J.A., Mezey E., Lam A.S., Bonner T.I.
Brain Res. 860:41-52(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain.
[5]"Cloning and characterization of a novel human GABA-B receptor subtype with high affinity for GABA and low affinity for baclofen."
Liu M., Parker R., McCrea K., Watson J., Baker E., Sutherland G., Herzog H.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]Borowsky B., Laz T., Gerald C.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hippocampus.
[7]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-941.
Tissue: Hippocampus.
[9]"Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity."
Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R., Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P., Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F., Bonner T.I., O'Neill G.P.
J. Biol. Chem. 274:7607-7610(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABBR1.
[10]"Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B)) receptors with truncated receptors and metabotropic glutamate receptor 4 supports the GABA(B) heterodimer as the functional receptor."
Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr., Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K., Abramovitz M., O'Neill G.P., Ng G.Y.K.
J. Pharmacol. Exp. Ther. 293:460-467(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABBR1.
[11]"Subcellular distribution of GABA(B) receptor homo- and hetero-dimers."
Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S., Bouvier M.
Biochem. J. 388:47-55(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[12]"Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor."
Nomura R., Suzuki Y., Kakizuka A., Jingami H.
J. Biol. Chem. 283:4665-4673(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH GABBR1.
[13]"Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2."
Geng Y., Xiong D., Mosyak L., Malito D.L., Kniazeff J., Chen Y., Burmakina S., Quick M., Bush M., Javitch J.A., Pin J.P., Fan Q.R.
Nat. Neurosci. 15:970-978(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 42-466, PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH GABBR1, MUTAGENESIS OF TYR-118, GLYCOSYLATION AT ASN-90; ASN-389; ASN-404 AND ASN-453, DISULFIDE BONDS.
[14]"Structural mechanism of ligand activation in human GABA(B) receptor."
Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.
Nature 504:254-259(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-466 IN COMPLEXES WITH GABBR1; AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-404, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ012188 mRNA. Translation: CAA09942.1.
AF069755 mRNA. Translation: AAC99345.1.
AF099033 mRNA. Translation: AAD45867.1.
AF056085 mRNA. Translation: AAC63228.1.
AF095784 mRNA. Translation: AAD30389.1.
AF074483 mRNA. Translation: AAD03336.1.
AL445495 expand/collapse EMBL AC list , AL353782, AL356282, AL591502 Genomic DNA. Translation: CAD13322.2.
AL353782 expand/collapse EMBL AC list , AL356282, AL445495, AL591502 Genomic DNA. Translation: CAH71298.1.
AL356282 expand/collapse EMBL AC list , AL353782, AL445495, AL591502 Genomic DNA. Translation: CAH72233.1.
AL591502 expand/collapse EMBL AC list , AL353782, AL356282, AL445495 Genomic DNA. Translation: CAI12581.1.
BC035071 mRNA. Translation: AAH35071.2. Different initiation.
RefSeqNP_005449.5. NM_005458.7.
UniGeneHs.198612.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F11X-ray2.38A42-466[»]
4F12X-ray3.02A42-466[»]
4MQEX-ray2.35B42-466[»]
4MQFX-ray2.22B42-466[»]
4MR7X-ray2.15B42-466[»]
4MR8X-ray2.15B42-466[»]
4MR9X-ray2.35B42-466[»]
4MRMX-ray2.86B42-466[»]
4MS1X-ray2.25B42-466[»]
4MS3X-ray2.50B42-466[»]
4MS4X-ray1.90B42-466[»]
ProteinModelPortalO75899.
SMRO75899. Positions 52-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114938. 5 interactions.
DIPDIP-42851N.
IntActO75899. 6 interactions.
MINTMINT-1398863.
STRING9606.ENSP00000259455.

Chemistry

BindingDBO75899.
ChEMBLCHEMBL2111463.
DrugBankDB00181. Baclofen.

Protein family/group databases

TCDB9.A.14.15.1. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteO75899.

Proteomic databases

PaxDbO75899.
PRIDEO75899.

Protocols and materials databases

DNASU9568.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259455; ENSP00000259455; ENSG00000136928.
GeneID9568.
KEGGhsa:9568.
UCSCuc004ays.3. human.

Organism-specific databases

CTD9568.
GeneCardsGC09M101050.
HGNCHGNC:4507. GABBR2.
HPAHPA013820.
HPA031684.
MIM607340. gene.
neXtProtNX_O75899.
PharmGKBPA28896.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273984.
HOVERGENHBG080355.
InParanoidO75899.
KOK04615.
OMAHENIDDV.
OrthoDBEOG7D2FCV.
PhylomeDBO75899.
TreeFamTF313965.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressO75899.
BgeeO75899.
CleanExHS_GABBR2.
GenevestigatorO75899.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR000337. GPCR_3.
IPR017978. GPCR_3_C.
IPR017979. GPCR_3_CS.
IPR002455. GPCR_3_GABA_rcpt_B.
IPR002457. GPCR_3_GABA_rcpt_B2.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
[Graphical view]
PRINTSPR01178. GABAB2RECPTR.
PR01176. GABABRECEPTR.
PR00248. GPCRMGR.
SUPFAMSSF53822. SSF53822. 1 hit.
PROSITEPS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGABBR2. human.
GeneWikiGABBR2.
GenomeRNAi9568.
NextBio35881.
PROO75899.
SOURCESearch...

Entry information

Entry nameGABR2_HUMAN
AccessionPrimary (citable) accession number: O75899
Secondary accession number(s): O75974 expand/collapse secondary AC list , O75975, Q5VXZ2, Q8WX04, Q9P1R2, Q9UNR1, Q9UNS9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

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 9

Human chromosome 9: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries