UniProtKB - P28222 (5HT1B_HUMAN)
(max 400 entries)x
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P28222|5HT1B_HUMAN 5-hydroxytryptamine receptor 1B OS=Homo sapiens OX=9606 GN=HTR1B PE=1 SV=1 MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALIT LATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQV VCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISI SLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRIL KQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLE KKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYL NSLINPIIYTMSNEDFKQAFHKLIRFKCTS
- Align
- Format
- Add to basketAdded to basket
- History
- Other tutorials and videos
- Help video
- Feedback
Protein
5-hydroxytryptamine receptor 1B
Gene
HTR1B
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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.12 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. , 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.
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.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 355 | Important for species-specific agonist sensitivity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- drug binding Source: Ensembl
- G-protein coupled serotonin receptor activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neurotransmitter receptor activity Source: GO_Central
- serotonin binding Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- adenylate cyclase-inhibiting serotonin receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- bone remodeling Source: Ensembl
- cellular response to alkaloid Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to drug Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular response to temperature stimulus Source: Ensembl
- chemical synaptic transmission Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- drinking behavior Source: Ensembl
- G-protein coupled receptor internalization Source: Ensembl
- G-protein coupled receptor signaling pathway Source: Reactome
- G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- negative regulation of serotonin secretion Source: UniProtKB
- negative regulation of synaptic transmission, GABAergic Source: Ensembl
- negative regulation of synaptic transmission, glutamatergic Source: Ensembl
- positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
- regulation of behavior Source: InterPro
- regulation of dopamine secretion Source: Ensembl
- response to cocaine Source: Ensembl
- response to ethanol Source: Ensembl
- response to mineralocorticoid Source: Ensembl
- vasoconstriction Source: InterPro
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | G-protein coupled receptor, Receptor, Transducer |
| Biological process | Behavior |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-390666 Serotonin receptors R-HSA-418594 G alpha (i) signalling events |
Protein family/group databases
Transport Classification Database More...TCDBi | 9.A.14.3.6 the g-protein-coupled receptor (gpcr) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 5-hydroxytryptamine receptor 1BShort 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 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:HTR1B Synonyms:HTR1DB |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135312.5 |
Human Gene Nomenclature Database More...HGNCi | HGNC:5287 HTR1B |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 182131 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P28222 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane 10 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. , 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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. - Ref.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. , 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.
- Cell membrane 10 Publications
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- plasma membrane Source: HPA
Other locations
- cytoplasm Source: Ensembl
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 49 | ExtracellularAdd BLAST | 49 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 50 – 75 | Helical; Name=1Add BLAST | 26 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 76 – 84 | Cytoplasmic | 9 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 85 – 110 | Helical; Name=2Add BLAST | 26 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 111 – 123 | ExtracellularAdd BLAST | 13 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 124 – 145 | Helical; Name=3Add BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 146 – 165 | CytoplasmicAdd BLAST | 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 166 – 187 | Helical; Name=4Add BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 188 – 205 | ExtracellularAdd BLAST | 18 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 206 – 228 | Helical; Name=5Add BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 229 – 315 | CytoplasmicAdd BLAST | 87 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 316 – 336 | Helical; Name=6Add BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 337 – 349 | ExtracellularAdd BLAST | 13 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 350 – 371 | Helical; Name=7Add BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 372 – 390 | CytoplasmicAdd BLAST | 19 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 126 | L → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 129 | D → A: Abolishes agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 130 | I → A: Abolishes agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 133 | C → A: Abolishes agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 134 | T → A: Slightly decreases agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 200 | V → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 201 | V → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 203 | T → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 209 | T → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 212 | S → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 216 | A → S: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 327 | W → A: Abolishes agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 330 | F → A: Abolishes agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 331 | F → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 334 | S → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 337 | M → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 351 | F → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 352 | D → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 355 | T → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 359 | Y → A: No effect on agonist binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 3351 |
Open Targets More...OpenTargetsi | ENSG00000135312 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29549 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1898 |
Drug and drug target database More...DrugBanki | DB00918 Almotriptan DB00321 Amitriptyline DB00543 Amoxapine DB00714 Apomorphine DB01238 Aripiprazole DB06216 Asenapine DB08807 Bopindolol DB01200 Bromocriptine DB00248 Cabergoline DB00363 Clozapine DB04884 Dapoxetine DB00320 Dihydroergotamine DB00216 Eletriptan DB01049 Ergoloid mesylate DB00696 Ergotamine DB00998 Frovatriptan DB01221 Ketamine DB00589 Lisuride DB00408 Loxapine DB05743 MAP-0004 DB00247 Methysergide DB00952 Naratriptan DB06096 NXN-188 DB00334 Olanzapine DB00904 Ondansetron DB01359 Penbutolol DB01186 Pergolide DB00960 Pindolol DB00413 Pramipexole DB00571 Propranolol DB01224 Quetiapine DB00953 Rizatriptan DB00268 Ropinirole DB00669 Sumatriptan DB13025 Tiapride DB09068 Vortioxetine DB01392 Yohimbine DB00246 Ziprasidone DB00315 Zolmitriptan |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HTR1B |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112821 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000068916 | 1 – 390 | 5-hydroxytryptamine receptor 1BAdd BLAST | 390 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 24 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 32 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 122 ↔ 199 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 388 | S-palmitoyl cysteineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
Palmitoylated.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P28222 |
PRoteomics IDEntifications database More...PRIDEi | P28222 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54452 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P28222 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P28222 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Detected in cerebral artery smooth muscle cells (at protein level). Detected in brain cortex, striatum, amygdala, medulla, hippocampus, caudate nucleus and putamen.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135312 |
CleanEx database of gene expression profiles More...CleanExi | HS_HTR1B |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P28222 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P28222 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA028808 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer. Heterodimer with HTR1D.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| MDFI | Q99750 | 6 | EBI-1056863,EBI-724076 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109583, 5 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P28222 |
Protein interaction database and analysis system More...IntActi | P28222, 5 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358963 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P28222 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 40 – 43 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 46 – 76 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 31 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 78 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 83 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 104 – 112 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 118 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 35 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 154 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 163 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 206 – 216 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 218 – 239 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 311 – 336 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 26 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 349 – 372 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 374 – 383 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P28222 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P28222 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 125 – 134 | Agonist binding | 10 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 327 – 331 | Agonist binding | 5 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 146 – 148 | DRY motif; important for ligand-induced conformation changes and signaling | 3 | |
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 365 – 369 | NPxxY motif; important for ligand-induced conformation changes and signaling | 5 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Ligands are bound in a hydrophobic pocket formed by the transmembrane helices.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. , 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.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3656 Eukaryota ENOG410XRW9 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118795 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239242 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG106962 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P28222 |
KEGG Orthology (KO) More...KOi | K04153 |
Identification of Orthologs from Complete Genome Data More...OMAi | VNTDHVL |
Database of Orthologous Groups More...OrthoDBi | EOG091G06VI |
Database for complete collections of gene phylogenies More...PhylomeDBi | P28222 |
TreeFam database of animal gene trees More...TreeFami | TF316350 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002147 5HT1B_rcpt IPR002231 5HT_rcpt IPR000276 GPCR_Rhodpsn IPR017452 GPCR_Rhodpsn_7TM |
The PANTHER Classification System More...PANTHERi | PTHR24247:SF16 PTHR24247:SF16, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00001 7tm_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00513 5HT1BRECEPTR PR01101 5HTRECEPTOR PR00237 GPCRRHODOPSN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01381 7TM_GPCR_Srsx, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00237 G_PROTEIN_RECEP_F1_1, 1 hit PS50262 G_PROTEIN_RECEP_F1_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
P28222-1 [UniParc]FASTAAdd to basketAdded to basketShow »
10 20 30 40 50
MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV
60 70 80 90 100
LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI
110 120 130 140 150
LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA
160 170 180 190 200
ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV
210 220 230 240 250
VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR
260 270 280 290 300
LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE
310 320 330 340 350
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI
360 370 380 390
FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
Length:390
Mass (Da):43,568
Last modified:December 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iCD874DC7EB44CF12
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011715 | 124 | F → C1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011831 | 219 | F → L. Corresponds to variant dbSNP:rs130061Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011832 | 367 | I → V. Corresponds to variant dbSNP:rs130063Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_011833 | 374 | E → K. Corresponds to variant dbSNP:rs130064Ensembl. | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | 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 No translation available. BC069065 mRNA Translation: AAH69065.1 BC096206 mRNA Translation: AAH96206.1 BC096207 mRNA Translation: AAH96207.1 BC096208 mRNA Translation: AAH96208.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4986.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JN0268 |
NCBI Reference Sequences More...RefSeqi | NP_000854.1, NM_000863.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.123016 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369947; ENSP00000358963; ENSG00000135312 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3351 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3351 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P28222 | 5-hydroxytryptamine receptor 1B | 390 | |||
| 5-hydroxytryptamine (Serotonin) receptor 1B (Fragment) | 390 | ||||
| 5-hydroxytryptamine receptor 1B | 390 | ||||
| HTR1B isoform 1 | 390 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P28222 | 5-hydroxytryptamine receptor 1B | 390 | |||
| 5-hydroxytryptamine (Serotonin) receptor 1B (Fragment) | 390 | ||||
| 5-hydroxytryptamine receptor 1B | 390 | ||||
| 5-hydroxytryptamine receptor 1B (Fragment) | 399 | ||||
| 5-hydroxytryptamine receptor 1B | 399 | ||||
| +109 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P28222 | 5-hydroxytryptamine receptor 1B | 390 | |||
| 5-hydroxytryptamine (Serotonin) receptor 1B (Fragment) | 390 | ||||
| 5-hydroxytryptamine receptor 1B | 390 | ||||
| UPI0002BCEA09 | 399 | ||||
| 5-hydroxytryptamine receptor 1B (Fragment) | 399 | ||||
| +201 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | 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 No translation available. BC069065 mRNA Translation: AAH69065.1 BC096206 mRNA Translation: AAH96206.1 BC096207 mRNA Translation: AAH96207.1 BC096208 mRNA Translation: AAH96208.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS4986.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JN0268 |
NCBI Reference Sequences More...RefSeqi | NP_000854.1, NM_000863.2 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.123016 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2G1X | model | - | A | 1-390 | [»] | |
| 4IAQ | X-ray | 2.80 | A | 33-239 | [»] | |
| A | 304-390 | [»] | ||||
| 4IAR | X-ray | 2.70 | A | 33-239 | [»] | |
| A | 306-390 | [»] | ||||
| 5V54 | X-ray | 3.90 | A/B | 37-390 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P28222 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P28222 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 109583, 5 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P28222 |
Protein interaction database and analysis system More...IntActi | P28222, 5 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000358963 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P28222 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1898 |
Drug and drug target database More...DrugBanki | DB00918 Almotriptan DB00321 Amitriptyline DB00543 Amoxapine DB00714 Apomorphine DB01238 Aripiprazole DB06216 Asenapine DB08807 Bopindolol DB01200 Bromocriptine DB00248 Cabergoline DB00363 Clozapine DB04884 Dapoxetine DB00320 Dihydroergotamine DB00216 Eletriptan DB01049 Ergoloid mesylate DB00696 Ergotamine DB00998 Frovatriptan DB01221 Ketamine DB00589 Lisuride DB00408 Loxapine DB05743 MAP-0004 DB00247 Methysergide DB00952 Naratriptan DB06096 NXN-188 DB00334 Olanzapine DB00904 Ondansetron DB01359 Penbutolol DB01186 Pergolide DB00960 Pindolol DB00413 Pramipexole DB00571 Propranolol DB01224 Quetiapine DB00953 Rizatriptan DB00268 Ropinirole DB00669 Sumatriptan DB13025 Tiapride DB09068 Vortioxetine DB01392 Yohimbine DB00246 Ziprasidone DB00315 Zolmitriptan |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2 |
Protein family/group databases
Transport Classification Database More...TCDBi | 9.A.14.3.6 the g-protein-coupled receptor (gpcr) family |
Information system for G protein-coupled receptors (GPCRs) More...GPCRDBi | Search... |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P28222 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P28222 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | HTR1B |
Domain mapping of disease mutations (DMDM) More...DMDMi | 112821 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P28222 |
PRoteomics IDEntifications database More...PRIDEi | P28222 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54452 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 3351 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000369947; ENSP00000358963; ENSG00000135312 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3351 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3351 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3351 |
DisGeNET More...DisGeNETi | 3351 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135312.5 |
GeneCards: human genes, protein and diseases More...GeneCardsi | HTR1B |
Human Gene Nomenclature Database More...HGNCi | HGNC:5287 HTR1B |
Human Protein Atlas More...HPAi | HPA028808 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 182131 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P28222 |
Open Targets More...OpenTargetsi | ENSG00000135312 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA29549 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3656 Eukaryota ENOG410XRW9 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118795 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000239242 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG106962 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P28222 |
KEGG Orthology (KO) More...KOi | K04153 |
Identification of Orthologs from Complete Genome Data More...OMAi | VNTDHVL |
Database of Orthologous Groups More...OrthoDBi | EOG091G06VI |
Database for complete collections of gene phylogenies More...PhylomeDBi | P28222 |
TreeFam database of animal gene trees More...TreeFami | TF316350 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-390666 Serotonin receptors R-HSA-418594 G alpha (i) signalling events |
Miscellaneous databases
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | 5-HT1B_receptor |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3351 |
Protein Ontology More...PROi | PR:P28222 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135312 |
CleanEx database of gene expression profiles More...CleanExi | HS_HTR1B |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P28222 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P28222 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002147 5HT1B_rcpt IPR002231 5HT_rcpt IPR000276 GPCR_Rhodpsn IPR017452 GPCR_Rhodpsn_7TM |
The PANTHER Classification System More...PANTHERi | PTHR24247:SF16 PTHR24247:SF16, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00001 7tm_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00513 5HT1BRECEPTR PR01101 5HTRECEPTOR PR00237 GPCRRHODOPSN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01381 7TM_GPCR_Srsx, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00237 G_PROTEIN_RECEP_F1_1, 1 hit PS50262 G_PROTEIN_RECEP_F1_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | 5HT1B_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P28222Primary (citable) accession number: P28222 Secondary accession number(s): Q4VAY7 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 1992 |
| Last sequence update: | December 1, 1992 | |
| Last modified: | July 18, 2018 | |
| This is version 170 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- 7-transmembrane G-linked receptors
List of 7-transmembrane G-linked receptor entries - Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
