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P28335

- 5HT2C_HUMAN

UniProt

P28335 - 5HT2C_HUMAN

Protein

5-hydroxytryptamine receptor 2C

Gene

HTR2C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (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 various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and 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. 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. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis.4 Publications

    GO - Molecular functioni

    1. 1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding Source: UniProtKB
    2. drug binding Source: UniProtKB
    3. Gq/11-coupled serotonin receptor activity Source: UniProtKB
    4. serotonin binding Source: UniProtKB
    5. serotonin receptor activity Source: MGI

    GO - Biological processi

    1. behavioral fear response Source: UniProtKB
    2. cellular calcium ion homeostasis Source: UniProtKB
    3. cGMP biosynthetic process Source: UniProtKB
    4. feeding behavior Source: UniProtKB
    5. locomotory behavior Source: InterPro
    6. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
    7. phospholipase C-activating serotonin receptor signaling pathway Source: UniProtKB
    8. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
    9. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    10. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
    11. regulation of appetite Source: UniProtKB
    12. regulation of corticotropin-releasing hormone secretion Source: UniProtKB
    13. regulation of neurological system process Source: UniProtKB
    14. release of sequestered calcium ion into cytosol Source: UniProtKB
    15. response to drug Source: UniProtKB
    16. serotonin receptor signaling pathway Source: UniProtKB
    17. synaptic transmission Source: ProtInc

    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.
    SignaLinkiP28335.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5-hydroxytryptamine receptor 2C
    Short name:
    5-HT-2C
    Short name:
    5-HT2C
    Short name:
    5-HTR2C
    Alternative name(s):
    5-hydroxytryptamine receptor 1C
    Short name:
    5-HT-1C
    Short name:
    5-HT1C
    Serotonin receptor 2C
    Gene namesi
    Name:HTR2C
    Synonyms:HTR1C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:5295. HTR2C.

    Subcellular locationi

    Cell membrane 4 Publications; Multi-pass membrane protein 4 Publications

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591P → A: Decreases interaction with ARRB2. 1 Publication
    Mutagenesisi456 – 4561S → A: Loss of interaction with MPDZ. 1 Publication
    Mutagenesisi456 – 4561S → T: No effect on interaction with MPDZ. 1 Publication
    Mutagenesisi457 – 4571S → A: No effect on interaction with MPDZ. 1 Publication
    Mutagenesisi458 – 4581V → A: Loss of interaction with MPDZ. 1 Publication

    Organism-specific databases

    PharmGKBiPA194.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 4584265-hydroxytryptamine receptor 2CPRO_0000068958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)1 Publication
    Disulfide bondi127 ↔ 207PROSITE-ProRule annotation
    Disulfide bondi337 ↔ 341PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP28335.
    PRIDEiP28335.

    PTM databases

    PhosphoSiteiP28335.

    Expressioni

    Tissue specificityi

    Detected in brain.1 Publication

    Gene expression databases

    ArrayExpressiP28335.
    BgeeiP28335.
    CleanExiHS_HTR2C.
    GenevestigatoriP28335.

    Organism-specific databases

    HPAiCAB006857.
    HPA003133.

    Interactioni

    Subunit structurei

    Interacts with MPDZ. Interacts with ARRB2.2 Publications

    Protein-protein interaction databases

    BioGridi109590. 7 interactions.
    IntActiP28335. 1 interaction.
    MINTiMINT-443944.
    STRINGi9606.ENSP00000276198.

    Structurei

    3D structure databases

    ProteinModelPortaliP28335.
    SMRiP28335. Positions 54-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 5220ExtracellularBy similarityAdd
    BLAST
    Topological domaini79 – 8911CytoplasmicBy similarityAdd
    BLAST
    Topological domaini111 – 12717ExtracellularBy similarityAdd
    BLAST
    Topological domaini151 – 17020CytoplasmicBy similarityAdd
    BLAST
    Topological domaini194 – 21320ExtracellularBy similarityAdd
    BLAST
    Topological domaini236 – 31176CytoplasmicBy similarityAdd
    BLAST
    Topological domaini334 – 34815ExtracellularBy similarityAdd
    BLAST
    Topological domaini372 – 45887CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 7826Helical; Name=1By similarityAdd
    BLAST
    Transmembranei90 – 11021Helical; Name=2By similarityAdd
    BLAST
    Transmembranei128 – 15023Helical; Name=3By similarityAdd
    BLAST
    Transmembranei171 – 19323Helical; Name=4By similarityAdd
    BLAST
    Transmembranei214 – 23522Helical; Name=5By similarityAdd
    BLAST
    Transmembranei312 – 33322Helical; Name=6By similarityAdd
    BLAST
    Transmembranei349 – 37123Helical; Name=7By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 1396Agonist bindingBy similarity
    Regioni324 – 3285Agonist bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi151 – 1533DRY motif; important for ligand-induced conformation changesBy similarity
    Motifi364 – 3685NPxxY motif; important for ligand-induced conformation changes and signalingBy similarity
    Motifi456 – 4583PDZ-binding

    Domaini

    The PDZ domain-binding motif is involved in the interaction with MPDZ.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG247243.
    HOGENOMiHOG000240378.
    HOVERGENiHBG107487.
    InParanoidiP28335.
    KOiK04157.
    OMAiCCKRNTD.
    OrthoDBiEOG70ZZN5.
    PhylomeDBiP28335.
    TreeFamiTF316350.

    Family and domain databases

    Gene3Di1.20.1070.10. 2 hits.
    InterProiIPR000377. 5HT2C_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24247:SF32. PTHR24247:SF32. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00517. 5HT2CRECEPTR.
    PR01101. 5HTRECEPTOR.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28335-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD    50
    GVQNWPALSI VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM 100
    LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL 150
    DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV 200
    FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH 250
    GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM 300
    QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL 350
    NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR 400
    VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV 450
    VSERISSV 458
    Length:458
    Mass (Da):51,821
    Last modified:December 1, 1992 - v1
    Checksum:i9E76B3FFD3E09C93
    GO
    Isoform 2 (identifier: P28335-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-458: YVAIRNPIEH...SVVSERISSV → CISSYPCDWT...YGRGRELCKP

    Show »
    Length:248
    Mass (Da):28,055
    Checksum:i8A8C81B80DA6B59E
    GO

    RNA editingi

    Partially edited. RNA editing generates receptor isoforms that differ in their ability to interact with the phospholipase C signaling cascade in a transfected cell line, suggesting that this RNA processing event may contribute to the modulation of serotonergic neurotransmission in the central nervous system.

    Polymorphismi

    Position 23 is polymorphic; the frequencies in unrelated Caucasians are 0.87 for Cys and 0.13 for Ser.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231C → S.5 Publications
    Corresponds to variant rs6318 [ dbSNP | Ensembl ].
    VAR_003450
    Natural varianti156 – 1561I → V in RNA edited version.
    VAR_010166
    Natural varianti158 – 1581N → S in RNA edited version.
    VAR_010167
    Natural varianti160 – 1601I → V in RNA edited version.
    VAR_010168

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei153 – 458306YVAIR…RISSV → CISSYPCDWTEGRRKGVREQ HDVRAQRPKFRSYWVLRSFL HTADDYGDYVLPDHLRSAPT SFDVTARPHRGTAWTKSGFP EVLQEEYGRGRELCKP in isoform 2. 1 PublicationVSP_045171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81778 mRNA. Translation: AAA60317.1.
    X80763 Genomic DNA. Translation: CAB59978.1.
    U49516 mRNA. Translation: AAB40898.1.
    AF208053 mRNA. Translation: AAF35842.1.
    AF498983 mRNA. Translation: AAM21130.1.
    AK295753 mRNA. Translation: BAG58583.1.
    AC007022 Genomic DNA. No translation available.
    AC007025 Genomic DNA. No translation available.
    AL591402 Genomic DNA. No translation available.
    AL355812, AC004822, AL590097 Genomic DNA. Translation: CAI41334.1.
    AC004822 Genomic DNA. Translation: AAC71658.1.
    AL355812, AL590097, AC004822 Genomic DNA. Translation: CAI41335.1.
    AL590097, AC004822, AL355812 Genomic DNA. Translation: CAH70193.1.
    BC095543 mRNA. Translation: AAH95543.1.
    CCDSiCCDS14564.1. [P28335-1]
    CCDS59174.1. [P28335-2]
    PIRiJS0616.
    RefSeqiNP_000859.1. NM_000868.2. [P28335-1]
    NP_001243689.1. NM_001256760.1. [P28335-1]
    NP_001243690.1. NM_001256761.1. [P28335-2]
    UniGeneiHs.149037.

    Genome annotation databases

    EnsembliENST00000276198; ENSP00000276198; ENSG00000147246. [P28335-1]
    ENST00000371950; ENSP00000361018; ENSG00000147246. [P28335-2]
    ENST00000371951; ENSP00000361019; ENSG00000147246. [P28335-1]
    GeneIDi3358.
    KEGGihsa:3358.
    UCSCiuc004epu.1. human. [P28335-1]
    uc004epv.1. human.

    Polymorphism databases

    DMDMi112816.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M81778 mRNA. Translation: AAA60317.1 .
    X80763 Genomic DNA. Translation: CAB59978.1 .
    U49516 mRNA. Translation: AAB40898.1 .
    AF208053 mRNA. Translation: AAF35842.1 .
    AF498983 mRNA. Translation: AAM21130.1 .
    AK295753 mRNA. Translation: BAG58583.1 .
    AC007022 Genomic DNA. No translation available.
    AC007025 Genomic DNA. No translation available.
    AL591402 Genomic DNA. No translation available.
    AL355812 , AC004822 , AL590097 Genomic DNA. Translation: CAI41334.1 .
    AC004822 Genomic DNA. Translation: AAC71658.1 .
    AL355812 , AL590097 , AC004822 Genomic DNA. Translation: CAI41335.1 .
    AL590097 , AC004822 , AL355812 Genomic DNA. Translation: CAH70193.1 .
    BC095543 mRNA. Translation: AAH95543.1 .
    CCDSi CCDS14564.1. [P28335-1 ]
    CCDS59174.1. [P28335-2 ]
    PIRi JS0616.
    RefSeqi NP_000859.1. NM_000868.2. [P28335-1 ]
    NP_001243689.1. NM_001256760.1. [P28335-1 ]
    NP_001243690.1. NM_001256761.1. [P28335-2 ]
    UniGenei Hs.149037.

    3D structure databases

    ProteinModelPortali P28335.
    SMRi P28335. Positions 54-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109590. 7 interactions.
    IntActi P28335. 1 interaction.
    MINTi MINT-443944.
    STRINGi 9606.ENSP00000276198.

    Chemistry

    BindingDBi P28335.
    ChEMBLi CHEMBL2111466.
    DrugBanki DB01239. Chlorprothixene.
    DB00363. Clozapine.
    DB01191. Dexfenfluramine.
    DB00574. Fenfluramine.
    DB00247. Methysergide.
    DB06148. Mianserin.
    DB00805. Minaprine.
    DB00370. Mirtazapine.
    DB00334. Olanzapine.
    DB00420. Promazine.
    DB00777. Propiomazine.
    DB01224. Quetiapine.
    DB06144. Sertindole.
    DB00372. Thiethylperazine.
    DB00193. Tramadol.
    DB00246. Ziprasidone.
    GuidetoPHARMACOLOGYi 8.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P28335.

    Polymorphism databases

    DMDMi 112816.

    Proteomic databases

    PaxDbi P28335.
    PRIDEi P28335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276198 ; ENSP00000276198 ; ENSG00000147246 . [P28335-1 ]
    ENST00000371950 ; ENSP00000361018 ; ENSG00000147246 . [P28335-2 ]
    ENST00000371951 ; ENSP00000361019 ; ENSG00000147246 . [P28335-1 ]
    GeneIDi 3358.
    KEGGi hsa:3358.
    UCSCi uc004epu.1. human. [P28335-1 ]
    uc004epv.1. human.

    Organism-specific databases

    CTDi 3358.
    GeneCardsi GC0XP113818.
    HGNCi HGNC:5295. HTR2C.
    HPAi CAB006857.
    HPA003133.
    MIMi 312861. gene.
    neXtProti NX_P28335.
    PharmGKBi PA194.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247243.
    HOGENOMi HOG000240378.
    HOVERGENi HBG107487.
    InParanoidi P28335.
    KOi K04157.
    OMAi CCKRNTD.
    OrthoDBi EOG70ZZN5.
    PhylomeDBi P28335.
    TreeFami TF316350.

    Enzyme and pathway databases

    Reactomei REACT_17064. Serotonin receptors.
    REACT_18283. G alpha (q) signalling events.
    SignaLinki P28335.

    Miscellaneous databases

    GeneWikii 5-HT2C_receptor.
    GenomeRNAii 3358.
    NextBioi 13278.
    PROi P28335.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28335.
    Bgeei P28335.
    CleanExi HS_HTR2C.
    Genevestigatori P28335.

    Family and domain databases

    Gene3Di 1.20.1070.10. 2 hits.
    InterProi IPR000377. 5HT2C_rcpt.
    IPR002231. 5HT_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24247:SF32. PTHR24247:SF32. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00517. 5HT2CRECEPTR.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Genomic organisation and functional expression of the gene encoding the human serotonin 5-HT2C receptor."
      Stam N.J., Vanderheyden P., Van Alebeek C., Klomp J., De Boer T., Van Delft A.M.L., Olijve W.
      Eur. J. Pharmacol. 269:339-348(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Hippocampus and Placenta.
    3. "The human serotonin 5-HT2C receptor: complete cDNA, genomic structure, and alternatively spliced variant."
      Xie E., Zhao L., Levine A.J., Shenk T., Chang L.-S.
      Genomics 35:551-561(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    4. "Identification and characterization of RNA editing events within the 5-HT2C receptor."
      Niswender C.M., Sanders-Bush E., Emeson R.B.
      Ann. N. Y. Acad. Sci. 861:38-48(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA EDITING OF POSITIONS 156; 158 AND 160.
      Tissue: Brain.
    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 (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORM 2).
      Tissue: Hippocampus.
    7. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "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, DOMAIN, MUTAGENESIS OF SER-456; SER-457 AND VAL-458, GLYCOSYLATION.
    10. "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.
    11. "A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors."
      Marion S., Oakley R.H., Kim K.-M., Caron M.G., Barak L.S.
      J. Biol. Chem. 281:2932-2938(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2, MUTAGENESIS OF PRO-159.
    12. Cited for: REVIEW.
    13. "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, SUBCELLULAR LOCATION.
    14. "Pharmacological characterization of mitogen-activated protein kinase activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B receptors."
      Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.
      Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "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.
    16. "The N-terminal region of the human 5-HT(2)C receptor has as a cleavable signal peptide."
      Jahnsen J.A., Uhlen S.
      Eur. J. Pharmacol. 684:44-50(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, VARIANT SER-23.
    17. "Identification, expression, and pharmacology of a Cys23-Ser23 substitution in the human 5-HT2c receptor gene (HTR2C)."
      Lappalainen J., Zhang L., Dean M., Oz M., Ozaki N., Yu D., Virkkunen M., Weight F., Linnoila M., Goldman D.
      Genomics 27:274-279(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-23.
    18. "Association analysis between a Cys23Ser substitution polymorphism of the human 5-HT2c receptor gene and neuronal hyperexcitability."
      Samochowiec J., Smolka M., Winterer G., Rommelspacher H., Schmidt L.G., Sander T.
      Am. J. Med. Genet. 88:126-130(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-23.
    19. "Unified approach to the analysis of genetic variation in serotonergic pathways."
      Marshall S.E., Bird T.G., Hart K., Welsh K.I.
      Am. J. Med. Genet. 88:621-627(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-23.
    20. Cited for: VARIANT SER-23.

    Entry informationi

    Entry namei5HT2C_HUMAN
    AccessioniPrimary (citable) accession number: P28335
    Secondary accession number(s): B1AMW4, Q5VUF8, Q9NP28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 154 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

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3