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P28335 (5HT2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HTR2C
Synonyms:HTR1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.10 Ref.13 Ref.14

Subunit structure

Interacts with MPDZ. Interacts with ARRB2. Ref.9 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2 Ref.10 Ref.13 Ref.14.

Tissue specificity

Detected in brain. Ref.3

Domain

The PDZ domain-binding motif is involved in the interaction with MPDZ. Ref.9

Post-translational modification

N-glycosylated. Ref.9

Polymorphism

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

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

RNA editing

Edited at positions 156, 158 and 160.
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. Ref.4

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
RNA editing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral fear response

Inferred from sequence or structural similarity. Source: UniProtKB

cGMP biosynthetic process

Inferred from direct assay Ref.10. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from direct assay Ref.14. Source: UniProtKB

feeding behavior

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: InterPro

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

phospholipase C-activating serotonin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of appetite

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of corticotropin-releasing hormone secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neurological system process

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype Ref.13. Source: UniProtKB

response to drug

Inferred from direct assay Ref.13. Source: UniProtKB

serotonin receptor signaling pathway

Inferred from mutant phenotype Ref.13. Source: UniProtKB

synaptic transmission

Traceable author statement PubMed 9241279. Source: ProtInc

   Cellular_componentintegral component of plasma membrane

Inferred from mutant phenotype Ref.13. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10Ref.13. Source: UniProtKB

   Molecular_function1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding

Inferred from direct assay Ref.14. Source: UniProtKB

Gq/11-coupled serotonin receptor activity

Inferred from direct assay Ref.13. Source: UniProtKB

drug binding

Inferred from direct assay Ref.10PubMed 15831837Ref.13. Source: UniProtKB

serotonin binding

Inferred from direct assay PubMed 15831837Ref.14. Source: UniProtKB

serotonin receptor activity

Inferred from direct assay PubMed 7582481. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28335-1)

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.
Isoform 2 (identifier: P28335-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 4584265-hydroxytryptamine receptor 2C
PRO_0000068958

Regions

Topological domain33 – 5220Extracellular By similarity
Transmembrane53 – 7826Helical; Name=1; By similarity
Topological domain79 – 8911Cytoplasmic By similarity
Transmembrane90 – 11021Helical; Name=2; By similarity
Topological domain111 – 12717Extracellular By similarity
Transmembrane128 – 15023Helical; Name=3; By similarity
Topological domain151 – 17020Cytoplasmic By similarity
Transmembrane171 – 19323Helical; Name=4; By similarity
Topological domain194 – 21320Extracellular By similarity
Transmembrane214 – 23522Helical; Name=5; By similarity
Topological domain236 – 31176Cytoplasmic By similarity
Transmembrane312 – 33322Helical; Name=6; By similarity
Topological domain334 – 34815Extracellular By similarity
Transmembrane349 – 37123Helical; Name=7; By similarity
Topological domain372 – 45887Cytoplasmic By similarity
Region134 – 1396Agonist binding By similarity
Region324 – 3285Agonist binding By similarity
Motif151 – 1533DRY motif; important for ligand-induced conformation changes By similarity
Motif364 – 3685NPxxY motif; important for ligand-induced conformation changes and signaling By similarity
Motif456 – 4583PDZ-binding

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Probable
Disulfide bond127 ↔ 207 By similarity
Disulfide bond337 ↔ 341 By similarity

Natural variations

Alternative sequence153 – 458306YVAIR…RISSV → CISSYPCDWTEGRRKGVREQ HDVRAQRPKFRSYWVLRSFL HTADDYGDYVLPDHLRSAPT SFDVTARPHRGTAWTKSGFP EVLQEEYGRGRELCKP in isoform 2.
VSP_045171
Natural variant231C → S. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Corresponds to variant rs6318 [ dbSNP | Ensembl ].
VAR_003450
Natural variant1561I → V in RNA edited version.
VAR_010166
Natural variant1581N → S in RNA edited version.
VAR_010167
Natural variant1601I → V in RNA edited version.
VAR_010168

Experimental info

Mutagenesis1591P → A: Decreases interaction with ARRB2. Ref.11
Mutagenesis4561S → A: Loss of interaction with MPDZ. Ref.9
Mutagenesis4561S → T: No effect on interaction with MPDZ. Ref.9
Mutagenesis4571S → A: No effect on interaction with MPDZ. Ref.9
Mutagenesis4581V → A: Loss of interaction with MPDZ. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 9E76B3FFD3E09C93

FASTA45851,821
        10         20         30         40         50         60 
MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD GVQNWPALSI 

        70         80         90        100        110        120 
VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW 

       130        140        150        160        170        180 
PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA 

       190        200        210        220        230        240 
ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV 

       250        260        270        280        290        300 
LRRQALMLLH GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM 

       310        320        330        340        350        360 
QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL NVFVWIGYVC 

       370        380        390        400        410        420 
SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR VAATALSGRE LNVNIYRHTN 

       430        440        450 
EPVIEKASDN EPGIEMQVEN LELPVNPSSV VSERISSV 

« Hide

Isoform 2 [UniParc].

Checksum: 8A8C81B80DA6B59E
Show »

FASTA24828,055

References

« Hide 'large scale' references
[1]"Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."
Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., Felder S.
Biochem. Biophys. Res. Commun. 181:1469-1478(1991) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Serotonin receptors."
Nichols D.E., Nichols C.D.
Chem. Rev. 108:1614-1641(2008) [PubMed] [Europe PMC] [Abstract]
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]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-23.
[21]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14564.1. [P28335-1]
CCDS59174.1. [P28335-2]
PIRJS0616.
RefSeqNP_000859.1. NM_000868.2. [P28335-1]
NP_001243689.1. NM_001256760.1. [P28335-1]
NP_001243690.1. NM_001256761.1. [P28335-2]
UniGeneHs.149037.

3D structure databases

ProteinModelPortalP28335.
SMRP28335. Positions 54-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109590. 7 interactions.
IntActP28335. 1 interaction.
MINTMINT-443944.
STRING9606.ENSP00000276198.

Chemistry

BindingDBP28335.
ChEMBLCHEMBL2111466.
DrugBankDB01239. 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.
GuidetoPHARMACOLOGY8.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP28335.

Polymorphism databases

DMDM112816.

Proteomic databases

PaxDbP28335.
PRIDEP28335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276198; ENSP00000276198; ENSG00000147246. [P28335-1]
ENST00000371950; ENSP00000361018; ENSG00000147246. [P28335-2]
ENST00000371951; ENSP00000361019; ENSG00000147246. [P28335-1]
GeneID3358.
KEGGhsa:3358.
UCSCuc004epu.1. human. [P28335-1]
uc004epv.1. human.

Organism-specific databases

CTD3358.
GeneCardsGC0XP113818.
HGNCHGNC:5295. HTR2C.
HPACAB006857.
HPA003133.
MIM312861. gene.
neXtProtNX_P28335.
PharmGKBPA194.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247243.
HOGENOMHOG000240378.
HOVERGENHBG107487.
InParanoidP28335.
KOK04157.
OMACCKRNTD.
OrthoDBEOG70ZZN5.
PhylomeDBP28335.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP28335.

Gene expression databases

ArrayExpressP28335.
BgeeP28335.
CleanExHS_HTR2C.
GenevestigatorP28335.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF32. PTHR24247:SF32. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00517. 5HT2CRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWiki5-HT2C_receptor.
GenomeRNAi3358.
NextBio13278.
PROP28335.
SOURCESearch...

Entry information

Entry name5HT2C_HUMAN
AccessionPrimary (citable) accession number: P28335
Secondary accession number(s): B1AMW4, Q5VUF8, Q9NP28
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries