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P41595

- 5HT2B_HUMAN

UniProt

P41595 - 5HT2B_HUMAN

Protein

5-hydroxytryptamine receptor 2B

Gene

HTR2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca2+ ions from intracellular stores. Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity. May play a role in the perception of pain. Plays a role in the regulation of behavior, including impulsive behavior. Required for normal proliferation of embryonic cardiac myocytes and normal heart development. Protects cardiomyocytes against apoptosis. Plays a role in the adaptation of pulmonary arteries to chronic hypoxia. Plays a role in vasoconstriction. Required for normal osteoblast function and proliferation, and for maintaining normal bone density. Required for normal proliferation of the interstitial cells of Cajal in the intestine.8 Publications

    GO - Molecular functioni

    1. drug binding Source: UniProtKB
    2. G-protein alpha-subunit binding Source: UniProtKB
    3. Ras GTPase activator activity Source: UniProtKB
    4. serotonin binding Source: UniProtKB
    5. serotonin receptor activity Source: UniProtKB

    GO - Biological processi

    1. activation of phospholipase C activity Source: UniProtKB
    2. behavior Source: UniProtKB-KW
    3. calcium-mediated signaling Source: UniProtKB
    4. cardiac muscle hypertrophy Source: UniProtKB
    5. cellular calcium ion homeostasis Source: UniProtKB
    6. cellular response to temperature stimulus Source: UniProtKB
    7. cGMP biosynthetic process Source: UniProtKB
    8. embryonic morphogenesis Source: UniProtKB
    9. ERK1 and ERK2 cascade Source: UniProtKB
    10. G-protein coupled receptor internalization Source: Ensembl
    11. G-protein coupled receptor signaling pathway Source: UniProtKB
    12. heart morphogenesis Source: UniProtKB
    13. intestine smooth muscle contraction Source: UniProtKB
    14. negative regulation of apoptotic process Source: UniProtKB
    15. negative regulation of autophagy Source: UniProtKB
    16. negative regulation of cell death Source: UniProtKB
    17. neural crest cell differentiation Source: UniProtKB
    18. neural crest cell migration Source: UniProtKB
    19. phosphatidylinositol 3-kinase signaling Source: UniProtKB
    20. phosphorylation Source: UniProtKB
    21. positive regulation of cell division Source: UniProtKB
    22. positive regulation of cell proliferation Source: UniProtKB
    23. positive regulation of cytokine production Source: UniProtKB
    24. positive regulation of cytokine secretion Source: UniProtKB
    25. positive regulation of endothelial cell proliferation Source: UniProtKB
    26. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    27. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    28. positive regulation of MAP kinase activity Source: UniProtKB
    29. positive regulation of nitric-oxide synthase activity Source: UniProtKB
    30. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
    31. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    32. protein kinase C signaling Source: UniProtKB
    33. regulation of behavior Source: UniProtKB
    34. release of sequestered calcium ion into cytosol Source: UniProtKB
    35. response to drug Source: UniProtKB
    36. serotonin receptor signaling pathway Source: UniProtKB
    37. vasoconstriction Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Behavior

    Enzyme and pathway databases

    ReactomeiREACT_17064. Serotonin receptors.
    REACT_18283. G alpha (q) signalling events.

    Protein family/group databases

    TCDBi9.A.14.3.7. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-hydroxytryptamine receptor 2B
    Short name:
    5-HT-2B
    Short name:
    5-HT2B
    Alternative name(s):
    Serotonin receptor 2B
    Gene namesi
    Name:HTR2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:5294. HTR2B.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. integral component of plasma membrane Source: InterPro
    4. neuron projection Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321L → A: No effect on agonist binding. 1 Publication
    Mutagenesisi135 – 1351D → A: Abolishes agonist binding. 1 Publication
    Mutagenesisi136 – 1361V → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi139 – 1391S → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi140 – 1401T → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi208 – 2081V → A: No effect on agonist binding. 1 Publication
    Mutagenesisi209 – 2091L → A: No effect on agonist binding. 1 Publication
    Mutagenesisi211 – 2111K → A: Impairs protein folding and stability. Strongly reduced cell surface expression. 1 Publication
    Mutagenesisi217 – 2171F → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi218 – 2181M → A: No effect on agonist binding. 1 Publication
    Mutagenesisi225 – 2251A → S: No effect on agonist binding. 1 Publication
    Mutagenesisi337 – 3371W → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi340 – 3401F → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi344 – 3441N → A: Slightly decreases agonist binding. 1 Publication
    Mutagenesisi347 – 3471L → A: No effect on agonist binding. 1 Publication
    Mutagenesisi348 – 3481V → A: No effect on agonist binding. 1 Publication
    Mutagenesisi362 – 3621L → A: No effect on agonist binding. 1 Publication
    Mutagenesisi363 – 3631E → A: No effect on agonist binding. 1 Publication
    Mutagenesisi366 – 3661V → A: No effect on agonist binding. 1 Publication
    Mutagenesisi370 – 3701Y → A: Slightly decreases agonist binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA29554.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4814815-hydroxytryptamine receptor 2BPRO_0000068953Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi128 ↔ 2071 PublicationPROSITE-ProRule annotation
    Disulfide bondi350 ↔ 3531 PublicationPROSITE-ProRule annotation
    Lipidationi397 – 3971S-palmitoyl cysteineSequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    PaxDbiP41595.
    PRIDEiP41595.

    PTM databases

    PhosphoSiteiP41595.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in liver, kidney, heart, pulmonary artery, and intestine. Detected at lower levels in blood, placenta and brain, especially in cerebellum, occipital cortex and frontal cortex.5 Publications

    Gene expression databases

    ArrayExpressiP41595.
    BgeeiP41595.
    CleanExiHS_HTR2B.
    GenevestigatoriP41595.

    Organism-specific databases

    HPAiCAB011448.
    HPA012867.

    Interactioni

    Subunit structurei

    Interacts with MPDZ.2 Publications

    Protein-protein interaction databases

    BioGridi109589. 3 interactions.
    MINTiMINT-444010.
    STRINGi9606.ENSP00000258400.

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi54 – 6310
    Helixi65 – 8117
    Helixi83 – 853
    Helixi88 – 10619
    Helixi108 – 1114
    Helixi113 – 1164
    Helixi127 – 15832
    Helixi165 – 18723
    Helixi189 – 1935
    Helixi211 – 22515
    Helixi227 – 24822
    Helixi314 – 34936
    Beta strandi351 – 3533
    Helixi355 – 38127
    Helixi385 – 39410
    Turni395 – 3973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IB4X-ray2.70A36-248[»]
    A314-405[»]
    4NC3X-ray2.80A36-248[»]
    A314-405[»]
    ProteinModelPortaliP41595.
    SMRiP41595. Positions 48-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5656ExtracellularAdd
    BLAST
    Topological domaini80 – 9011CytoplasmicAdd
    BLAST
    Topological domaini114 – 12916ExtracellularAdd
    BLAST
    Topological domaini152 – 17120CytoplasmicAdd
    BLAST
    Topological domaini193 – 21624ExtracellularAdd
    BLAST
    Topological domaini240 – 32485CytoplasmicAdd
    BLAST
    Topological domaini346 – 36015ExtracellularAdd
    BLAST
    Topological domaini383 – 48199CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei57 – 7923Helical; Name=1Add
    BLAST
    Transmembranei91 – 11323Helical; Name=2Add
    BLAST
    Transmembranei130 – 15122Helical; Name=3Add
    BLAST
    Transmembranei172 – 19221Helical; Name=4Add
    BLAST
    Transmembranei217 – 23923Helical; Name=5Add
    BLAST
    Transmembranei325 – 34521Helical; Name=6Add
    BLAST
    Transmembranei361 – 38222Helical; Name=7Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni135 – 1406Agonist binding
    Regioni337 – 3415Agonist binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi152 – 1543DRY motif; important for ligand-induced conformation changes
    Motifi212 – 2154[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members
    Motifi376 – 3805NPxxY motif; important for ligand-induced conformation changes and signaling
    Motifi479 – 4813PDZ-binding

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG247243.
    HOGENOMiHOG000240378.
    HOVERGENiHBG107487.
    InParanoidiP41595.
    KOiK04157.
    OMAiCDSCNQT.
    OrthoDBiEOG70ZZN5.
    PhylomeDBiP41595.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 2 hits.
    InterProiIPR000482. 5HT2B_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24247:SF31. PTHR24247:SF31. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00651. 5HT2BRECEPTR.
    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.

    P41595-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ    50
    GNKLHWAALL ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD 100
    LLVGLFVMPI ALLTIMFEAM WPLPLVLCPA WLFLDVLFST ASIMHLCAIS 150
    VDRYIAIKKP IQANQYNSRA TAFIKITVVW LISIGIAIPV PIKGIETDVD 200
    NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT IHALQKKAYL 250
    VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET 300
    LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC 350
    DSCNQTTLQM LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR 400
    ATKSVKTLRK RSSKIYFRNP MAENSKFFKK HGIRNGINPA MYQSPMRLRS 450
    STIQSSSIIL LDTLLLTENE GDKTEEQVSY V 481
    Length:481
    Mass (Da):54,298
    Last modified:November 1, 1995 - v1
    Checksum:iCDA4447ECDBA3B46
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti452 – 4521T → P in CAA85319. (PubMed:7926008)Curated
    Sequence conflicti477 – 4771Q → R in AAH63123. (PubMed:15489334)Curated

    Polymorphismi

    A variation at a single nucleotide base, which results in an erroneous stop codon and affects Gln-20, triggers non-sense mediated RNA decay, such that no HTR2B-receptor protein is expressed. It is associated with impulsive behavior and co-segregates with disorders characterized by impulsivity. However, the presence of this variant is not in itself sufficient to cause impulsive behavior: male sex, testosterone level, alcohol and stress exposure are other factors playing important roles.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451Q → E.1 Publication
    Corresponds to variant rs78484969 [ dbSNP | Ensembl ].
    VAR_064574
    Natural varianti173 – 1731F → L.1 Publication
    Corresponds to variant rs77570025 [ dbSNP | Ensembl ].
    VAR_064575
    Natural varianti388 – 3881R → W.1 Publication
    Corresponds to variant rs77982984 [ dbSNP | Ensembl ].
    VAR_064576
    Natural varianti421 – 4211M → V.
    Corresponds to variant rs6736017 [ dbSNP | Ensembl ].
    VAR_055907

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77307 mRNA. Translation: CAA54513.1.
    Z36748 mRNA. Translation: CAA85319.1.
    AF156160, AF156158, AF156159 Genomic DNA. Translation: AAD39259.1.
    AY136751 mRNA. Translation: AAN01277.1.
    AC009407 Genomic DNA. Translation: AAX93128.1.
    AK313741 mRNA. Translation: BAG36482.1.
    CH471063 Genomic DNA. Translation: EAW70949.1.
    BC063123 mRNA. Translation: AAH63123.1.
    CCDSiCCDS2483.1.
    PIRiS43687.
    S49442.
    RefSeqiNP_000858.3. NM_000867.4.
    UniGeneiHs.421649.

    Genome annotation databases

    EnsembliENST00000258400; ENSP00000258400; ENSG00000135914.
    GeneIDi3357.
    KEGGihsa:3357.
    UCSCiuc002vro.3. human.

    Polymorphism databases

    DMDMi1168220.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    On the spur of a whim - Issue 127 of March 2011

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77307 mRNA. Translation: CAA54513.1 .
    Z36748 mRNA. Translation: CAA85319.1 .
    AF156160 , AF156158 , AF156159 Genomic DNA. Translation: AAD39259.1 .
    AY136751 mRNA. Translation: AAN01277.1 .
    AC009407 Genomic DNA. Translation: AAX93128.1 .
    AK313741 mRNA. Translation: BAG36482.1 .
    CH471063 Genomic DNA. Translation: EAW70949.1 .
    BC063123 mRNA. Translation: AAH63123.1 .
    CCDSi CCDS2483.1.
    PIRi S43687.
    S49442.
    RefSeqi NP_000858.3. NM_000867.4.
    UniGenei Hs.421649.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IB4 X-ray 2.70 A 36-248 [» ]
    A 314-405 [» ]
    4NC3 X-ray 2.80 A 36-248 [» ]
    A 314-405 [» ]
    ProteinModelPortali P41595.
    SMRi P41595. Positions 48-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109589. 3 interactions.
    MINTi MINT-444010.
    STRINGi 9606.ENSP00000258400.

    Chemistry

    BindingDBi P41595.
    ChEMBLi CHEMBL2111466.
    DrugBanki DB01239. Chlorprothixene.
    DB00216. Eletriptan.
    DB00574. Fenfluramine.
    DB01403. Methotrimeprazine.
    DB00805. Minaprine.
    DB01224. Quetiapine.
    DB00669. Sumatriptan.
    DB01079. Tegaserod.
    DB00508. Triflupromazine.
    GuidetoPHARMACOLOGYi 7.

    Protein family/group databases

    TCDBi 9.A.14.3.7. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei P41595.

    Polymorphism databases

    DMDMi 1168220.

    Proteomic databases

    PaxDbi P41595.
    PRIDEi P41595.

    Protocols and materials databases

    DNASUi 3357.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258400 ; ENSP00000258400 ; ENSG00000135914 .
    GeneIDi 3357.
    KEGGi hsa:3357.
    UCSCi uc002vro.3. human.

    Organism-specific databases

    CTDi 3357.
    GeneCardsi GC02M231936.
    HGNCi HGNC:5294. HTR2B.
    HPAi CAB011448.
    HPA012867.
    MIMi 601122. gene.
    neXtProti NX_P41595.
    PharmGKBi PA29554.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247243.
    HOGENOMi HOG000240378.
    HOVERGENi HBG107487.
    InParanoidi P41595.
    KOi K04157.
    OMAi CDSCNQT.
    OrthoDBi EOG70ZZN5.
    PhylomeDBi P41595.
    TreeFami TF316350.

    Enzyme and pathway databases

    Reactomei REACT_17064. Serotonin receptors.
    REACT_18283. G alpha (q) signalling events.

    Miscellaneous databases

    GeneWikii 5-HT2B_receptor.
    GenomeRNAii 3357.
    NextBioi 13274.
    PROi P41595.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41595.
    Bgeei P41595.
    CleanExi HS_HTR2B.
    Genevestigatori P41595.

    Family and domain databases

    Gene3Di 1.20.1070.10. 2 hits.
    InterProi IPR000482. 5HT2B_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24247:SF31. PTHR24247:SF31. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00651. 5HT2BRECEPTR.
    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. "Cloning and functional characterization of the human 5-HT2B serotonin receptor."
      Schmuck K., Ullmer C., Engels P., Luebbert H.
      FEBS Lett. 342:85-90(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "The human serotonin 5-HT2B receptor: pharmacological link between 5-HT2 and 5-HT1D receptors."
      Choi D.S., Birraux G., Launay J.-M., Maroteaux L.
      FEBS Lett. 352:393-399(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Molecular cloning, functional expression, and mRNA tissue distribution of the human 5-hydroxytryptamine2B receptor."
      Kursar J.D., Nelson D.L., Wainscott D.B., Baez M.
      Mol. Pharmacol. 46:227-234(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Uterus.
    4. "Mutation screening of human 5-HT(2B) receptor gene in early-onset obsessive-compulsive disorder."
      Kim S.J., Veenstra-VanderWeele J., Hanna G.L., Gonen D., Leventhal B.L., Cook E.H. Jr.
      Mol. Cell. Probes 14:47-52(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Skin.
    10. "5-HT2B receptor-mediated calcium release from ryanodine-sensitive intracellular stores in human pulmonary artery endothelial cells."
      Ullmer C., Boddeke H.G., Schmuck K., Lubbert H.
      Br. J. Pharmacol. 117:1081-1088(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1."
      Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., Luebbert H., Ullmer C.
      J. Biol. Chem. 276:12974-12982(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPDZ.
    12. "Agonist actions of dihydroergotamine at 5-HT2B and 5-HT2C receptors and their possible relevance to antimigraine efficacy."
      Schaerlinger B., Hickel P., Etienne N., Guesnier L., Maroteaux L.
      Br. J. Pharmacol. 140:277-284(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. Cited for: REVIEW.
    14. "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5-HT2B and 5-HT2C-VSV receptors mediated Gq/11 activation and calcium mobilisation in CHO cells."
      Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A., Martel J.C., Danty N., Rauly-Lestienne I.
      Eur. J. Pharmacol. 594:32-38(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: INVOLVEMENT IN IMPULSIVE BEHAVIOR, TISSUE SPECIFICITY, POLYMORPHISM, VARIANTS GLU-45; LEU-173 AND TRP-388.
    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, MUTAGENESIS OF LEU-132; ASP-135; VAL-136; SER-139; THR-140; VAL-208; LEU-209; LYS-211; PHE-217; MET-218; ALA-225; TRP-337; PHE-340; ASN-344; LEU-347; VAL-348; LEU-362; GLU-363; VAL-366 AND TYR-370.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-405 IN COMPLEX WITH THE AGONIST ERGOTAMINE, FUNCTION, ROLE IN ARRESTIN-MEDIATED SIGNALING AND CALCIUM RELEASE, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DISULFIDE BONDS.

    Entry informationi

    Entry namei5HT2B_HUMAN
    AccessioniPrimary (citable) accession number: P41595
    Secondary accession number(s): B2R9D5
    , Q53TI1, Q62221, Q6P523
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 141 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

    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 2
      Human chromosome 2: 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

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