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P28222

- 5HT1B_HUMAN

UniProt

P28222 - 5HT1B_HUMAN

Protein

5-hydroxytryptamine receptor 1B

Gene

HTR1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei355 – 3551Important for species-specific agonist sensitivity

    GO - Molecular functioni

    1. drug binding Source: Ensembl
    2. serotonin binding Source: Ensembl
    3. serotonin receptor activity Source: UniProtKB

    GO - Biological processi

    1. adenylate cyclase-inhibiting serotonin receptor signaling pathway Source: UniProtKB
    2. bone remodeling Source: Ensembl
    3. cellular response to alkaloid Source: UniProtKB
    4. cellular response to drug Source: UniProtKB
    5. cellular response to temperature stimulus Source: Ensembl
    6. drinking behavior Source: Ensembl
    7. G-protein coupled receptor internalization Source: Ensembl
    8. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
    9. negative regulation of cAMP biosynthetic process Source: UniProtKB
    10. negative regulation of serotonin secretion Source: UniProtKB
    11. negative regulation of synaptic transmission, GABAergic Source: Ensembl
    12. negative regulation of synaptic transmission, glutamatergic Source: Ensembl
    13. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    14. regulation of behavior Source: InterPro
    15. regulation of dopamine secretion Source: Ensembl
    16. response to cocaine Source: Ensembl
    17. response to ethanol Source: Ensembl
    18. response to mineralocorticoid Source: Ensembl
    19. synaptic transmission Source: ProtInc
    20. vasoconstriction Source: InterPro

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Behavior

    Enzyme and pathway databases

    ReactomeiREACT_17064. Serotonin receptors.
    REACT_19231. G alpha (i) signalling events.

    Protein family/group databases

    TCDBi9.A.14.3.6. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:HTR1B
    Synonyms:HTR1DB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5287. HTR1B.

    Subcellular locationi

    Cell membrane 10 Publications; Multi-pass membrane protein 10 Publications

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi126 – 1261L → A: No effect on agonist binding. 1 Publication
    Mutagenesisi129 – 1291D → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi130 – 1301I → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi133 – 1331C → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi134 – 1341T → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi200 – 2001V → A: No effect on agonist binding. 1 Publication
    Mutagenesisi201 – 2011V → A: No effect on agonist binding. 1 Publication
    Mutagenesisi203 – 2031T → A: No effect on agonist binding. 1 Publication
    Mutagenesisi209 – 2091T → A: No effect on agonist binding. 1 Publication
    Mutagenesisi212 – 2121S → A: No effect on agonist binding. 1 Publication
    Mutagenesisi216 – 2161A → S: No effect on agonist binding. 1 Publication
    Mutagenesisi327 – 3271W → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi330 – 3301F → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi331 – 3311F → A: No effect on agonist binding. 1 Publication
    Mutagenesisi334 – 3341S → A: No effect on agonist binding. 1 Publication
    Mutagenesisi337 – 3371M → A: No effect on agonist binding. 1 Publication
    Mutagenesisi351 – 3511F → A: No effect on agonist binding. 1 Publication
    Mutagenesisi352 – 3521D → A: No effect on agonist binding. 1 Publication
    Mutagenesisi355 – 3551T → A: No effect on agonist binding. 1 Publication
    Mutagenesisi359 – 3591Y → A: No effect on agonist binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA29549.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3903905-hydroxytryptamine receptor 1BPRO_0000068916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi122 ↔ 1991 PublicationPROSITE-ProRule annotation
    Lipidationi388 – 3881S-palmitoyl cysteineSequence Analysis

    Post-translational modificationi

    Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation.1 Publication
    Palmitoylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP28222.
    PRIDEiP28222.

    PTM databases

    PhosphoSiteiP28222.

    Expressioni

    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

    Gene expression databases

    BgeeiP28222.
    CleanExiHS_HTR1B.
    GenevestigatoriP28222.

    Organism-specific databases

    HPAiHPA049046.

    Interactioni

    Subunit structurei

    Homodimer. Heterodimer with HTR1D.1 Publication

    Protein-protein interaction databases

    BioGridi109583. 3 interactions.
    IntActiP28222. 1 interaction.
    STRINGi9606.ENSP00000358963.

    Structurei

    Secondary structure

    1
    390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 434
    Helixi46 – 7631
    Helixi78 – 803
    Helixi83 – 10119
    Helixi104 – 1129
    Helixi118 – 15235
    Helixi154 – 1585
    Helixi163 – 18119
    Helixi206 – 21611
    Helixi218 – 23922
    Helixi311 – 33626
    Helixi349 – 37224
    Helixi374 – 38310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G1Xmodel-A1-390[»]
    4IAQX-ray2.80A33-239[»]
    A304-390[»]
    4IARX-ray2.70A33-239[»]
    A306-390[»]
    ProteinModelPortaliP28222.
    SMRiP28222. Positions 38-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4949ExtracellularAdd
    BLAST
    Topological domaini76 – 849Cytoplasmic
    Topological domaini111 – 12313ExtracellularAdd
    BLAST
    Topological domaini146 – 16520CytoplasmicAdd
    BLAST
    Topological domaini188 – 20518ExtracellularAdd
    BLAST
    Topological domaini229 – 31587CytoplasmicAdd
    BLAST
    Topological domaini337 – 34913ExtracellularAdd
    BLAST
    Topological domaini372 – 39019CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei50 – 7526Helical; Name=1Add
    BLAST
    Transmembranei85 – 11026Helical; Name=2Add
    BLAST
    Transmembranei124 – 14522Helical; Name=3Add
    BLAST
    Transmembranei166 – 18722Helical; Name=4Add
    BLAST
    Transmembranei206 – 22823Helical; Name=5Add
    BLAST
    Transmembranei316 – 33621Helical; Name=6Add
    BLAST
    Transmembranei350 – 37122Helical; Name=7Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni125 – 13410Agonist binding
    Regioni327 – 3315Agonist binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi146 – 1483DRY motif; important for ligand-induced conformation changes and signaling
    Motifi365 – 3695NPxxY motif; important for ligand-induced conformation changes and signaling

    Domaini

    Ligands are bound in a hydrophobic pocket formed by the transmembrane helices.1 Publication

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG249628.
    HOGENOMiHOG000239242.
    HOVERGENiHBG106962.
    InParanoidiP28222.
    KOiK04153.
    OMAiIALPWKV.
    OrthoDBiEOG7NCV3Q.
    PhylomeDBiP28222.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 2 hits.
    InterProiIPR002147. 5HT1B_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24247:SF16. PTHR24247:SF16. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00513. 5HT1BRECEPTR.
    PR01101. 5HTRECEPTOR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28222-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV    50
    LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI 100
    LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA 150
    ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV 200
    VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR 250
    LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE 300
    KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI 350
    FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS 390
    Length:390
    Mass (Da):43,568
    Last modified:December 1, 1992 - v1
    Checksum:iCD874DC7EB44CF12
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241F → C.1 Publication
    Corresponds to variant rs130060 [ dbSNP | Ensembl ].
    VAR_011715
    Natural varianti219 – 2191F → L.
    Corresponds to variant rs130061 [ dbSNP | Ensembl ].
    VAR_011831
    Natural varianti367 – 3671I → V.
    Corresponds to variant rs130063 [ dbSNP | Ensembl ].
    VAR_011832
    Natural varianti374 – 3741E → K.
    Corresponds to variant rs130064 [ dbSNP | Ensembl ].
    VAR_011833

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links 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. Translation: CAB51537.1.
    BC069065 mRNA. Translation: AAH69065.1.
    BC096206 mRNA. Translation: AAH96206.1.
    BC096207 mRNA. Translation: AAH96207.1.
    BC096208 mRNA. Translation: AAH96208.1.
    CCDSiCCDS4986.1.
    PIRiJN0268.
    RefSeqiNP_000854.1. NM_000863.1.
    UniGeneiHs.123016.

    Genome annotation databases

    EnsembliENST00000369947; ENSP00000358963; ENSG00000135312.
    GeneIDi3351.
    KEGGihsa:3351.
    UCSCiuc003pil.1. human.

    Polymorphism databases

    DMDMi112821.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links 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. Translation: CAB51537.1 .
    BC069065 mRNA. Translation: AAH69065.1 .
    BC096206 mRNA. Translation: AAH96206.1 .
    BC096207 mRNA. Translation: AAH96207.1 .
    BC096208 mRNA. Translation: AAH96208.1 .
    CCDSi CCDS4986.1.
    PIRi JN0268.
    RefSeqi NP_000854.1. NM_000863.1.
    UniGenei Hs.123016.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P28222.
    SMRi P28222. Positions 38-387.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109583. 3 interactions.
    IntActi P28222. 1 interaction.
    STRINGi 9606.ENSP00000358963.

    Chemistry

    BindingDBi P28222.
    ChEMBLi CHEMBL2095230.
    DrugBanki DB00918. 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.
    GuidetoPHARMACOLOGYi 2.

    Protein family/group databases

    TCDBi 9.A.14.3.6. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei P28222.

    Polymorphism databases

    DMDMi 112821.

    Proteomic databases

    PaxDbi P28222.
    PRIDEi P28222.

    Protocols and materials databases

    DNASUi 3351.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369947 ; ENSP00000358963 ; ENSG00000135312 .
    GeneIDi 3351.
    KEGGi hsa:3351.
    UCSCi uc003pil.1. human.

    Organism-specific databases

    CTDi 3351.
    GeneCardsi GC06M078171.
    HGNCi HGNC:5287. HTR1B.
    HPAi HPA049046.
    MIMi 182131. gene.
    neXtProti NX_P28222.
    PharmGKBi PA29549.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249628.
    HOGENOMi HOG000239242.
    HOVERGENi HBG106962.
    InParanoidi P28222.
    KOi K04153.
    OMAi IALPWKV.
    OrthoDBi EOG7NCV3Q.
    PhylomeDBi P28222.
    TreeFami TF316350.

    Enzyme and pathway databases

    Reactomei REACT_17064. Serotonin receptors.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii 5-HT1B_receptor.
    GenomeRNAii 3351.
    NextBioi 13252.
    PROi P28222.
    SOURCEi Search...

    Gene expression databases

    Bgeei P28222.
    CleanExi HS_HTR1B.
    Genevestigatori P28222.

    Family and domain databases

    Gene3Di 1.20.1070.10. 2 hits.
    InterProi IPR002147. 5HT1B_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24247:SF16. PTHR24247:SF16. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00513. 5HT1BRECEPTR.
    PR01101. 5HTRECEPTOR.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    18. 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.

    Entry informationi

    Entry namei5HT1B_HUMAN
    AccessioniPrimary (citable) accession number: P28222
    Secondary accession number(s): Q4VAY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3