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P28222 (5HT1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 1B

Short name=5-HT-1B
Short name=5-HT1B
Alternative name(s):
S12
Serotonin 1D beta receptor
Short name=5-HT-1D-beta
Serotonin receptor 1B
Gene names
Name:HTR1B
Synonyms:HTR1DB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). 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 activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18

Subunit structure

Homodimer. Heterodimer with HTR1D. Ref.13

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.13 Ref.17 Ref.18.

Tissue specificity

Detected in cerebral artery smooth muscle cells (at protein level). Detected in brain cortex, striatum, amygdala, medulla, hippocampus, caudate nucleus and putamen. Ref.3 Ref.6 Ref.14

Domain

Ligands are bound in a hydrophobic pocket formed by the transmembrane helices. Ref.18

Post-translational modification

Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation. Ref.12

Palmitoylated. Ref.12

Miscellaneous

A residue in the 7th transmembrane region (Thr-355 in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor internalization

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting serotonin receptor signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

bone remodeling

Inferred from electronic annotation. Source: Ensembl

cellular response to alkaloid

Inferred from direct assay Ref.1. Source: UniProtKB

cellular response to drug

Inferred from direct assay Ref.1. Source: UniProtKB

cellular response to temperature stimulus

Inferred from electronic annotation. Source: Ensembl

drinking behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP biosynthetic process

Inferred from direct assay PubMed 8882600. Source: UniProtKB

negative regulation of serotonin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of behavior

Inferred from electronic annotation. Source: InterPro

regulation of dopamine secretion

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to mineralocorticoid

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement Ref.6. Source: ProtInc

vasoconstriction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Molecular_functiondrug binding

Inferred from electronic annotation. Source: Ensembl

serotonin binding

Inferred from electronic annotation. Source: Ensembl

serotonin receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3903905-hydroxytryptamine receptor 1B
PRO_0000068916

Regions

Topological domain1 – 4949Extracellular Ref.18
Transmembrane50 – 7526Helical; Name=1
Topological domain76 – 849Cytoplasmic Ref.18
Transmembrane85 – 11026Helical; Name=2
Topological domain111 – 12313Extracellular Ref.18
Transmembrane124 – 14522Helical; Name=3
Topological domain146 – 16520Cytoplasmic Ref.18
Transmembrane166 – 18722Helical; Name=4
Topological domain188 – 20518Extracellular Ref.18
Transmembrane206 – 22823Helical; Name=5
Topological domain229 – 31587Cytoplasmic Ref.18
Transmembrane316 – 33621Helical; Name=6
Topological domain337 – 34913Extracellular Ref.18
Transmembrane350 – 37122Helical; Name=7
Topological domain372 – 39019Cytoplasmic Ref.18
Region125 – 13410Agonist binding
Region327 – 3315Agonist binding
Motif146 – 1483DRY motif; important for ligand-induced conformation changes and signaling
Motif365 – 3695NPxxY motif; important for ligand-induced conformation changes and signaling

Sites

Site3551Important for species-specific agonist sensitivity

Amino acid modifications

Lipidation3881S-palmitoyl cysteine Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation321N-linked (GlcNAc...) Potential
Disulfide bond122 ↔ 199 Ref.18

Natural variations

Natural variant1241F → C. Ref.19
Corresponds to variant rs130060 [ dbSNP | Ensembl ].
VAR_011715
Natural variant2191F → L.
Corresponds to variant rs130061 [ dbSNP | Ensembl ].
VAR_011831
Natural variant3671I → V.
Corresponds to variant rs130063 [ dbSNP | Ensembl ].
VAR_011832
Natural variant3741E → K.
Corresponds to variant rs130064 [ dbSNP | Ensembl ].
VAR_011833

Experimental info

Mutagenesis1261L → A: No effect on agonist binding. Ref.18
Mutagenesis1291D → A: Abolishes agonist binding. Ref.18
Mutagenesis1301I → A: Abolishes agonist binding. Ref.18
Mutagenesis1331C → A: Abolishes agonist binding. Ref.18
Mutagenesis1341T → A: Slightly decreases agonist binding. Ref.18
Mutagenesis2001V → A: No effect on agonist binding. Ref.18
Mutagenesis2011V → A: No effect on agonist binding. Ref.18
Mutagenesis2031T → A: No effect on agonist binding. Ref.18
Mutagenesis2091T → A: No effect on agonist binding. Ref.18
Mutagenesis2121S → A: No effect on agonist binding. Ref.18
Mutagenesis2161A → S: No effect on agonist binding. Ref.18
Mutagenesis3271W → A: Abolishes agonist binding. Ref.18
Mutagenesis3301F → A: Abolishes agonist binding. Ref.18
Mutagenesis3311F → A: No effect on agonist binding. Ref.18
Mutagenesis3341S → A: No effect on agonist binding. Ref.18
Mutagenesis3371M → A: No effect on agonist binding. Ref.18
Mutagenesis3511F → A: No effect on agonist binding. Ref.18
Mutagenesis3521D → A: No effect on agonist binding. Ref.18
Mutagenesis3551T → A: No effect on agonist binding. Ref.18
Mutagenesis3591Y → A: No effect on agonist binding. Ref.18

Secondary structure

........................... 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28222 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: CD874DC7EB44CF12

FASTA39043,568
        10         20         30         40         50         60 
MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT 

        70         80         90        100        110        120 
LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV 

       130        140        150        160        170        180 
VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI 

       190        200        210        220        230        240 
SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL 

       250        260        270        280        290        300 
KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE 

       310        320        330        340        350        360 
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL 

       370        380        390 
NSLINPIIYT MSNEDFKQAF HKLIRFKCTS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of a human 5-HT1B serotonin receptor: a homologue of the rat 5-HT1B receptor with 5-HT1D-like pharmacological specificity."
Hamblin M.W., Metcalf M.A., McGuffin R.W., Karpells S.
Biochem. Biophys. Res. Commun. 184:752-759(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Cloning and expression of the human 5-HT1B-type receptor gene."
Mochizuki D., Yuyama Y., Tsujita R., Komaki H., Sagai H.
Biochem. Biophys. Res. Commun. 185:517-523(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[3]"Characterization of the human 5-hydroxytryptamine1B receptor."
Jin H., Oksenberg D., Ashkenazi A., Peroutka S.J., Duncan A.M.V., Rozmahel R., Yang Y., Mengod G., Palacios J.M., O'Dowd B.F.
J. Biol. Chem. 267:5735-5738(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Molecular cloning of a human serotonin receptor (S12) with a pharmacological profile resembling that of the 5-HT1D subtype."
Levy F.O., Gudermann T., Perez-Reyes E., Birnbaumer M., Kaumann A.J., Birnbaumer L.
J. Biol. Chem. 267:7553-7562(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[5]"Human serotonin 1D receptor is encoded by a subfamily of two distinct genes: 5-HT1D alpha and 5-HT1D beta."
Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., Hartig P.R.
Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Tissue: Placenta.
[6]"A human serotonin 1D receptor variant (5HT1D beta) encoded by an intronless gene on chromosome 6."
Demchyshyn L., Sunahara R.K., Miller K., Teitler M., Hoffman B.J., Kennedy J.L., Seeman P., van Tol H.H.M., Niznik H.B.
Proc. Natl. Acad. Sci. U.S.A. 89:5522-5526(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"Cloning and pharmacological characterization of a novel human 5-hydroxytryptamine1D receptor subtype."
Veldman S.A., Bienkowski M.J.
Mol. Pharmacol. 42:439-444(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[8]"Human-specific amino acid changes found in 103 protein-coding genes."
Kitano T., Liu Y.-H., Ueda S., Saitou N.
Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Isolation of complete coding sequence for 5-hydroxytryptamine (serotonin) receptor 1B (HTR1B)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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].
[12]"Human serotonin1B receptor expression in Sf9 cells: phosphorylation, palmitoylation, and adenylyl cyclase inhibition."
Ng G.Y.K., George S.R., Zastawny R.L., Caron M., Bouvier M., Dennis M., O'Dowd B.F.
Biochemistry 32:11727-11733(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION, PHOSPHORYLATION, FUNCTION.
[13]"Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone and heterodimers when co-expressed."
Xie Z., Lee S.P., O'Dowd B.F., George S.R.
FEBS Lett. 456:63-67(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[14]"Triptan-induced contractile (5-HT1B receptor) responses in human cerebral and coronary arteries: relationship to clinical effect."
Edvinsson L., Uddman E., Wackenfors A., Davenport A., Longmore J., Malmsjo M.
Clin. Sci. 109:335-342(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]"Serotonin receptors."
Nichols D.E., Nichols C.D.
Chem. Rev. 108:1614-1641(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"Serotonin receptors - from molecular biology to clinical applications."
Pytliak M., Vargova V., Mechirova V., Felsoci M.
Physiol. Res. 60:15-25(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"Structural features for functional selectivity at serotonin receptors."
Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E., McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., Cherezov V., Roth B.L., Stevens R.C.
Science 340:615-619(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]"Structural basis for molecular recognition at serotonin receptors."
Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., Liu W., Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., Melcher K., Zhang C., Bai F., Yang H., Yang L. expand/collapse author list , Jiang H., Roth B.L., Cherezov V., Stevens R.C., Xu H.E.
Science 340:610-614(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-390 IN COMPLEXES WITH ERGOTAMINE AND DIHYDROERGOTAMINE, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DOMAIN, DISULFIDE BOND, MUTAGENESIS OF LEU-126; ASP-129; ILE-130; CYS-133; THR-134; VAL-200; VAL-201; THR-203; THR-209; SER-212; ALA-216; TRP-327; PHE-330; PHE-331; SER-334; MET-337; PHE-351; ASP-352; THR-355 AND TYR-359.
[19]"Identification of genetic variation in the human serotonin 1D beta receptor gene."
Nothen M.M., Erdmann J., Shimron-Abarbanell D., Propping P.
Biochem. Biophys. Res. Commun. 205:1194-1200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-124.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M89478 Genomic DNA. No translation available.
D10995 Genomic DNA. Translation: BAA01763.1.
M83180 Genomic DNA. Translation: AAA36029.1.
L09732 Genomic DNA. Translation: AAA36030.1.
M81590 mRNA. Translation: AAA60316.1.
M75128 Genomic DNA. Translation: AAA58675.1.
AB041370 Genomic DNA. Translation: BAA94455.1.
AY225227 Genomic DNA. Translation: AAO67712.1.
AL049595 Genomic DNA. Translation: CAB51537.1.
BC069065 mRNA. Translation: AAH69065.1.
BC096206 mRNA. Translation: AAH96206.1.
BC096207 mRNA. Translation: AAH96207.1.
BC096208 mRNA. Translation: AAH96208.1.
PIRJN0268.
RefSeqNP_000854.1. NM_000863.1.
UniGeneHs.123016.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G1Xmodel-A1-390[»]
4IAQX-ray2.80A33-390[»]
4IARX-ray2.70A33-390[»]
ProteinModelPortalP28222.
SMRP28222. Positions 15-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109583. 3 interactions.
IntActP28222. 1 interaction.
STRING9606.ENSP00000358963.

Chemistry

BindingDBP28222.
ChEMBLCHEMBL2096904.
DrugBankDB00918. Almotriptan.
DB01191. Dexfenfluramine.
DB00320. Dihydroergotamine.
DB00216. Eletriptan.
DB00696. Ergotamine.
DB00998. Frovatriptan.
DB00952. Naratriptan.
DB00960. Pindolol.
DB00571. Propranolol.
DB00953. Rizatriptan.
DB00669. Sumatriptan.
DB00285. Venlafaxine.
DB00315. Zolmitriptan.
GuidetoPHARMACOLOGY2.

Protein family/group databases

TCDB9.A.14.3.6. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP28222.

Polymorphism databases

DMDM112821.

Proteomic databases

PaxDbP28222.
PRIDEP28222.

Protocols and materials databases

DNASU3351.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369947; ENSP00000358963; ENSG00000135312.
GeneID3351.
KEGGhsa:3351.
UCSCuc003pil.1. human.

Organism-specific databases

CTD3351.
GeneCardsGC06M078171.
HGNCHGNC:5287. HTR1B.
HPAHPA049046.
MIM182131. gene.
neXtProtNX_P28222.
PharmGKBPA29549.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249628.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP28222.
KOK04153.
OMAIALPWKV.
OrthoDBEOG7NCV3Q.
PhylomeDBP28222.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP28222.
CleanExHS_HTR1B.
GenevestigatorP28222.

Family and domain databases

InterProIPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF16. PTHR24247:SF16. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00513. 5HT1BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWiki5-HT1B_receptor.
GenomeRNAi3351.
NextBio13252.
PROP28222.
SOURCESearch...

Entry information

Entry name5HT1B_HUMAN
AccessionPrimary (citable) accession number: P28222
Secondary accession number(s): Q4VAY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: March 19, 2014
This is version 134 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 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