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5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (Serotonin receptor 2A)

 5HT2A_HUMAN             Reviewed;         471 AA.
P28223; B2RAC5; B4DZ79; F5GWE8; Q5T8C0;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
25-APR-2018, entry version 186.
RecName: Full=5-hydroxytryptamine receptor 2A;
Short=5-HT-2;
Short=5-HT-2A;
AltName: Full=Serotonin receptor 2A;
Name=HTR2A; Synonyms=HTR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain stem;
PubMed=1722404; DOI=10.1016/0006-291X(91)92105-S;
Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M.,
Felder S.;
"Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes.";
Biochem. Biophys. Res. Commun. 181:1469-1478(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1323014; DOI=10.1016/0169-328X(92)90005-V;
Chen K., Yang W., Grimsby J., Shih J.C.;
"The human 5-HT2 receptor is encoded by a multiple intron-exon gene.";
Brain Res. Mol. Brain Res. 14:20-26(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Platelet;
PubMed=8035173;
Cook E.H. Jr., Fletcher K.E., Wainwright M., Marks N., Yan S.Y.,
Leventhal B.L.;
"Primary structure of the human platelet serotonin 5-HT2A receptor:
identify with frontal cortex serotonin 5-HT2A receptor.";
J. Neurochem. 63:465-469(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-464 (ISOFORM 1).
TISSUE=Brain;
Tritch R.J., Robinson D.L., Sahagan B.G., Horlick R.A.;
"Cloning and nucleotide sequence of the human(5HT) type 2 receptor.";
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=1330647; DOI=10.1016/0922-4106(92)90123-D;
Stam N.J., van Huizen F., van Alebeek C., Brands J., Dijkema R.,
Tonnaer J.A., Olijve W.;
"Genomic organization, coding sequence and functional expression of
human 5-HT2 and 5-HT1A receptor genes.";
Eur. J. Pharmacol. 227:153-162(1992).
[11]
INTERACTION WITH MPDZ.
PubMed=11150294; DOI=10.1074/jbc.M008089200;
Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J.,
Luebbert H., Ullmer C.;
"Interaction of serotonin 5-hydroxytryptamine type 2C receptors with
PDZ10 of the multi-PDZ domain protein MUPP1.";
J. Biol. Chem. 276:12974-12982(2001).
[12]
INTERACTION WITH PATJ; MPP3; PRDX6; DLG4; DLG1; CASK; APBA1 AND MAGI2,
AND MUTAGENESIS OF GLY-463; ASN-465; CYS-470 AND VAL-471.
PubMed=14988405; DOI=10.1074/jbc.M312106200;
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
Dumuis A., Bockaert J., Marin P.;
"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
of PDZ proteins.";
J. Biol. Chem. 279:20257-20266(2004).
[13]
REVIEW.
PubMed=18476671; DOI=10.1021/cr078224o;
Nichols D.E., Nichols C.D.;
"Serotonin receptors.";
Chem. Rev. 108:1614-1641(2008).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040;
Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A.,
Martel J.C., Danty N., Rauly-Lestienne I.;
"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.";
Eur. J. Pharmacol. 594:32-38(2008).
[15]
INTERACTION WITH GRM2, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=18297054; DOI=10.1038/nature06612;
Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V.,
Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G.,
Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.;
"Identification of a serotonin/glutamate receptor complex implicated
in psychosis.";
Nature 452:93-97(2008).
[16]
FUNCTION.
PubMed=19057895; DOI=10.1007/s00210-008-0378-4;
Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.;
"Pharmacological characterization of mitogen-activated protein kinase
activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B
receptors.";
Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009).
[17]
INTERACTION WITH DRD2, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21645528; DOI=10.1016/j.neuropharm.2011.05.023;
Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.;
"Functional crosstalk and heteromerization of serotonin 5-HT2A and
dopamine D2 receptors.";
Neuropharmacology 61:770-777(2011).
[18]
REVIEW.
PubMed=20945968;
Pytliak M., Vargova V., Mechirova V., Felsoci M.;
"Serotonin receptors - from molecular biology to clinical
applications.";
Physiol. Res. 60:15-25(2011).
[19]
INTERACTION WITH GRM2, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22300836; DOI=10.1016/j.neuropharm.2012.01.010;
Delille H.K., Becker J.M., Burkhardt S., Bleher B., Terstappen G.C.,
Schmidt M., Meyer A.H., Unger L., Marek G.J., Mezler M.;
"Heterocomplex formation of 5-HT2A-mGlu2 and its relevance for
cellular signaling cascades.";
Neuropharmacology 62:2184-2191(2012).
[20]
PHOSPHORYLATION AT SER-280, AND MUTAGENESIS OF SER-280.
PubMed=24637012; DOI=10.1074/mcp.M113.036558;
Karaki S., Becamel C., Murat S., Mannoury la Cour C., Millan M.J.,
Prezeau L., Bockaert J., Marin P., Vandermoere F.;
"Quantitative phosphoproteomics unravels biased phosphorylation of
serotonin 2A receptor at Ser280 by hallucinogenic versus
nonhallucinogenic agonists.";
Mol. Cell. Proteomics 13:1273-1285(2014).
[21]
FUNCTION (MICROBIAL INFECTION).
PubMed=24089568; DOI=10.1128/JVI.02252-13;
Assetta B., Maginnis M.S., Gracia Ahufinger I., Haley S.A., Gee G.V.,
Nelson C.D., O'Hara B.A., Allen Ramdial S.A., Atwood W.J.;
"5-HT2 receptors facilitate JC polyomavirus entry.";
J. Virol. 87:13490-13498(2013).
[22]
FUNCTION, AND MUTAGENESIS OF LEU-229.
PubMed=28129538; DOI=10.1016/j.cell.2016.12.033;
Wacker D., Wang S., McCorvy J.D., Betz R.M., Venkatakrishnan A.J.,
Levit A., Lansu K., Schools Z.L., Che T., Nichols D.E., Shoichet B.K.,
Dror R.O., Roth B.L.;
"Crystal structure of an LSD-bound human serotonin receptor.";
Cell 168:377-389(2017).
[23]
VARIANTS ASN-25 AND TYR-452.
PubMed=8655141; DOI=10.1007/BF02281871;
Erdmann J., Shimron-Abarbanell D., Rietschel M., Albus M., Maier W.,
Koerner J., Bondy B., Chen K., Shih J.C., Knapp M., Propping P.,
Noethen M.M.;
"Systematic screening for mutations in the human serotonin-2A (5-HT2A)
receptor gene: identification of two naturally occurring receptor
variants and association analysis in schizophrenia.";
Hum. Genet. 97:614-619(1996).
[24]
VARIANTS ASN-25 AND TYR-452.
PubMed=10581480;
DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H;
Marshall S.E., Bird T.G., Hart K., Welsh K.I.;
"Unified approach to the analysis of genetic variation in serotonergic
pathways.";
Am. J. Med. Genet. 88:621-627(1999).
[25]
VARIANTS VAL-197; VAL-447 AND TYR-452.
PubMed=10391209; DOI=10.1038/10290;
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.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[26]
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).
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895).
Also functions as a receptor for various drugs and psychoactive
substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-
iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide
(LSD) (PubMed:28129538). Ligand binding causes a conformation
change that triggers signaling via guanine nucleotide-binding
proteins (G proteins) and modulates the activity of down-stream
effectors (PubMed:28129538). Beta-arrestin family members inhibit
signaling via G proteins and mediate activation of alternative
signaling pathways (PubMed:28129538). Signaling activates
phospholipase C and a phosphatidylinositol-calcium second
messenger system that modulates the activity of
phosphatidylinositol 3-kinase and promotes the release of Ca(2+)
ions from intracellular stores (PubMed:18703043, PubMed:28129538).
Affects neural activity, perception, cognition and mood
(PubMed:18297054). Plays a role in the regulation of behavior,
including responses to anxiogenic situations and psychoactive
substances. Plays a role in intestinal smooth muscle contraction,
and may play a role in arterial vasoconstriction.
{ECO:0000269|PubMed:1330647, ECO:0000269|PubMed:18297054,
ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895,
ECO:0000269|PubMed:21645528, ECO:0000269|PubMed:22300836,
ECO:0000269|PubMed:28129538}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for human JC
polyomavirus/JCPyV. {ECO:0000269|PubMed:24089568}.
-!- SUBUNIT: Interacts (via C-terminus) with MPDZ and PATJ
(PubMed:11150294, PubMed:14988405). May interact (via C-terminus)
with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2
(PubMed:14988405). Interacts with GRM2 and DRD2; this may affect
signaling (PubMed:18297054, PubMed:21645528, PubMed:22300836).
{ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:14988405,
ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:21645528,
ECO:0000269|PubMed:22300836}.
-!- INTERACTION:
P21554:CNR1; NbExp=2; IntAct=EBI-15573967, EBI-2909859;
Q14416:GRM2; NbExp=4; IntAct=EBI-15573967, EBI-10232876;
P18654:Rps6ka3 (xeno); NbExp=2; IntAct=EBI-15573967, EBI-397744;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28129538};
Multi-pass membrane protein {ECO:0000305}. Cell projection,
dendrite {ECO:0000250}. Cell projection, axon
{ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P14842}. Membrane, caveola
{ECO:0000250|UniProtKB:P14842}. Note=Localizes to the postsynaptic
thickening of axo-dendritic synapses. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28223-1; Sequence=Displayed;
Name=2;
IsoId=P28223-2; Sequence=VSP_046663;
Note=Ref.5 (BAG63991) sequence is in conflict in position:
49:D->N. {ECO:0000305};
-!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level).
Detected in blood platelets. {ECO:0000269|PubMed:18297054}.
-!- DOMAIN: The PDZ domain-binding motif is involved in the
interaction with PATJ, CASK, APBA1, DLG1 and DLG4.
{ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:14988405}.
-!- MISCELLANEOUS: Binds lysergic acid diethylamine (LSD) in the
orthosteric pocket (Probable). Bound LSD dissociates extremely
slowly, with a residence time of about 221 minutes at 37 degrees
Celsius. {ECO:0000269|PubMed:28129538}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HTR2A";
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EMBL; X57830; CAA40963.1; -; mRNA.
EMBL; S42168; AAB22791.2; -; Genomic_DNA.
EMBL; S42165; AAB22791.2; JOINED; Genomic_DNA.
EMBL; S42167; AAB22791.2; JOINED; Genomic_DNA.
EMBL; S71229; AAB31320.1; -; mRNA.
EMBL; AF498982; AAM21129.1; -; mRNA.
EMBL; AK302787; BAG63991.1; -; mRNA.
EMBL; AK314132; BAG36822.1; -; mRNA.
EMBL; AL160397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08770.1; -; Genomic_DNA.
EMBL; BC069356; AAH69356.1; -; mRNA.
EMBL; BC069576; AAH69576.1; -; mRNA.
EMBL; BC074848; AAH74848.1; -; mRNA.
EMBL; BC074849; AAH74849.1; -; mRNA.
EMBL; BC096839; AAH96839.1; -; mRNA.
EMBL; M86841; AAA58354.1; -; mRNA.
EMBL; S50130; AAB24166.2; -; Genomic_DNA.
EMBL; S49737; AAB24166.2; JOINED; Genomic_DNA.
EMBL; S50113; AAB24166.2; JOINED; Genomic_DNA.
CCDS; CCDS53867.1; -. [P28223-2]
CCDS; CCDS9405.1; -. [P28223-1]
PIR; A43956; A43956.
RefSeq; NP_000612.1; NM_000621.4. [P28223-1]
RefSeq; NP_001159419.1; NM_001165947.2. [P28223-2]
UniGene; Hs.72630; -.
ProteinModelPortal; P28223; -.
SMR; P28223; -.
BioGrid; 109588; 4.
DIP; DIP-41844N; -.
IntAct; P28223; 16.
MINT; P28223; -.
STRING; 9606.ENSP00000367959; -.
BindingDB; P28223; -.
ChEMBL; CHEMBL224; -.
DrugBank; DB01614; Acepromazine.
DrugBank; DB06288; Amisulpride.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00543; Amoxapine.
DrugBank; DB08927; Amperozide.
DrugBank; DB04599; Aniracetam.
DrugBank; DB05026; APD125.
DrugBank; DB05227; APD791.
DrugBank; DB00714; Apomorphine.
DrugBank; DB01238; Aripiprazole.
DrugBank; DB06216; Asenapine.
DrugBank; DB05687; BL-1020.
DrugBank; DB09128; Brexpiprazole.
DrugBank; DB01200; Bromocriptine.
DrugBank; DB09016; Butriptyline.
DrugBank; DB00248; Cabergoline.
DrugBank; DB06016; Cariprazine.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB01239; Chlorprothixene.
DrugBank; DB08810; Cinitapride.
DrugBank; DB00604; Cisapride.
DrugBank; DB01242; Clomipramine.
DrugBank; DB00363; Clozapine.
DrugBank; DB00924; Cyclobenzaprine.
DrugBank; DB00434; Cyproheptadine.
DrugBank; DB06512; Deramciclane.
DrugBank; DB01151; Desipramine.
DrugBank; DB01488; Dimethyltryptamine.
DrugBank; DB00843; Donepezil.
DrugBank; DB01142; Doxepin.
DrugBank; DB05492; Epicept NP-1.
DrugBank; DB00751; Epinastine.
DrugBank; DB01049; Ergoloid mesylate.
DrugBank; DB00696; Ergotamine.
DrugBank; DB06678; Esmirtazapine.
DrugBank; DB04908; Flibanserin.
DrugBank; DB00875; Flupentixol.
DrugBank; DB04842; Fluspirilene.
DrugBank; DB00502; Haloperidol.
DrugBank; DB05079; HY10275.
DrugBank; DB04946; Iloperidone.
DrugBank; DB00458; Imipramine.
DrugBank; DB01221; Ketamine.
DrugBank; DB00589; Lisuride.
DrugBank; DB00408; Loxapine.
DrugBank; DB06077; Lumateperone.
DrugBank; DB08815; Lurasidone.
DrugBank; DB05743; MAP-0004.
DrugBank; DB00934; Maprotiline.
DrugBank; DB00933; Mesoridazine.
DrugBank; DB01403; Methotrimeprazine.
DrugBank; DB00247; Methysergide.
DrugBank; DB06148; Mianserin.
DrugBank; DB00805; Minaprine.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01442; MMDA.
DrugBank; DB01618; Molindone.
DrugBank; DB01149; Nefazodone.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB01267; Paliperidone.
DrugBank; DB00715; Paroxetine.
DrugBank; DB01186; Pergolide.
DrugBank; DB05316; Pimavanserin.
DrugBank; DB01621; Pipotiazine.
DrugBank; DB00413; Pramipexole.
DrugBank; DB00420; Promazine.
DrugBank; DB01069; Promethazine.
DrugBank; DB00777; Propiomazine.
DrugBank; DB01224; Quetiapine.
DrugBank; DB00409; Remoxipride.
DrugBank; DB00734; Risperidone.
DrugBank; DB00268; Ropinirole.
DrugBank; DB06144; Sertindole.
DrugBank; DB01079; Tegaserod.
DrugBank; DB01622; Thioproperazine.
DrugBank; DB00679; Thioridazine.
DrugBank; DB01623; Thiothixene.
DrugBank; DB13025; Tiapride.
DrugBank; DB00656; Trazodone.
DrugBank; DB00726; Trimipramine.
DrugBank; DB01392; Yohimbine.
DrugBank; DB00246; Ziprasidone.
DrugBank; DB01624; Zuclopenthixol.
GuidetoPHARMACOLOGY; 6; -.
iPTMnet; P28223; -.
PhosphoSitePlus; P28223; -.
BioMuta; HTR2A; -.
DMDM; 543727; -.
PaxDb; P28223; -.
PeptideAtlas; P28223; -.
PRIDE; P28223; -.
Ensembl; ENST00000378688; ENSP00000367959; ENSG00000102468. [P28223-1]
Ensembl; ENST00000542664; ENSP00000437737; ENSG00000102468. [P28223-1]
Ensembl; ENST00000543956; ENSP00000441861; ENSG00000102468. [P28223-2]
GeneID; 3356; -.
KEGG; hsa:3356; -.
UCSC; uc001vbr.5; human. [P28223-1]
CTD; 3356; -.
DisGeNET; 3356; -.
EuPathDB; HostDB:ENSG00000102468.10; -.
GeneCards; HTR2A; -.
HGNC; HGNC:5293; HTR2A.
HPA; HPA014011; -.
MalaCards; HTR2A; -.
MIM; 182135; gene.
neXtProt; NX_P28223; -.
OpenTargets; ENSG00000102468; -.
PharmGKB; PA193; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00890000139331; -.
HOGENOM; HOG000240378; -.
HOVERGEN; HBG107487; -.
InParanoid; P28223; -.
KO; K04157; -.
OMA; AGRRTMQ; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P28223; -.
TreeFam; TF316350; -.
Reactome; R-HSA-390666; Serotonin receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
SignaLink; P28223; -.
GeneWiki; 5-HT2A_receptor; -.
GenomeRNAi; 3356; -.
PRO; PR:P28223; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102468; -.
CleanEx; HS_HTR2A; -.
ExpressionAtlas; P28223; baseline and differential.
Genevisible; P28223; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0070852; C:cell body fiber; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0071886; F:1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; IDA:UniProtKB.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
GO; GO:0008219; P:cell death; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0044380; P:protein localization to cytoskeleton; IEA:Ensembl.
GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0030431; P:sleep; IEA:Ensembl.
GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
InterPro; IPR000455; 5HT2A_rcpt.
InterPro; IPR002231; 5HT_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24247:SF30; PTHR24247:SF30; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00516; 5HT2ARECEPTR.
PRINTS; PR01101; 5HTRECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Behavior; Cell membrane; Cell projection;
Complete proteome; Cytoplasmic vesicle; Disulfide bond;
G-protein coupled receptor; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 471 5-hydroxytryptamine receptor 2A.
/FTId=PRO_0000068946.
TOPO_DOM 1 75 Extracellular. {ECO:0000250}.
TRANSMEM 76 99 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 100 110 Cytoplasmic. {ECO:0000250}.
TRANSMEM 111 132 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 133 148 Extracellular. {ECO:0000250}.
TRANSMEM 149 171 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 172 191 Cytoplasmic. {ECO:0000250}.
TRANSMEM 192 215 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 216 233 Extracellular. {ECO:0000250}.
TRANSMEM 234 254 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 255 324 Cytoplasmic. {ECO:0000250}.
TRANSMEM 325 346 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 347 362 Extracellular. {ECO:0000250}.
TRANSMEM 363 384 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 385 471 Cytoplasmic. {ECO:0000250}.
REGION 155 160 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
REGION 336 340 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 172 174 DRY motif; important for ligand-induced
conformation changes.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 376 380 NPxxY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 469 471 PDZ-binding.
{ECO:0000269|PubMed:11150294,
ECO:0000269|PubMed:14988405}.
SITE 229 229 Hydrophobic barrier that decreases the
speed of ligand binding and dissociation.
{ECO:0000269|PubMed:28129538}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000269|PubMed:24637012}.
CARBOHYD 8 8 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 148 227 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 349 353 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VAR_SEQ 1 138 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSD
AFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTA
VVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLL
GFLVMPVSMLTILYG -> MQFLKSAKQKPNYYHIMLVEDQ
EEGTLHQFNYCERCSESQNNKCISCVDPEDKW (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046663.
VARIANT 25 25 T -> N (in dbSNP:rs1805055).
{ECO:0000269|PubMed:10581480,
ECO:0000269|PubMed:8655141}.
/FTId=VAR_003448.
VARIANT 197 197 I -> V (in dbSNP:rs6304).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013901.
VARIANT 447 447 A -> V (in dbSNP:rs6308).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013902.
VARIANT 452 452 H -> Y (in dbSNP:rs6314).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10581480,
ECO:0000269|PubMed:8655141}.
/FTId=VAR_003449.
MUTAGEN 229 229 L->A: Strongly increases dissociation of
bound lysergic acid diethylamine, without
affecting binding affinity. Reduces
signaling via arrestins, but has no
effect on signaling via the
phosphatidylinositol-calcium second
messenger system.
{ECO:0000269|PubMed:28129538}.
MUTAGEN 280 280 S->A: Increased ability of hallucinogens
to desensitize the receptor.
{ECO:0000269|PubMed:24637012}.
MUTAGEN 280 280 S->D: Reduced receptor desensitization by
nonhallucinogenic agonists.
{ECO:0000269|PubMed:24637012}.
MUTAGEN 463 463 G->V: Loss of interaction with PATJ.
{ECO:0000269|PubMed:14988405}.
MUTAGEN 465 465 N->S: No effect on interaction with PATJ.
Acquires the binding properties of HTR2C;
when associated with S-470.
{ECO:0000269|PubMed:14988405}.
MUTAGEN 470 470 C->S: No effect on interaction with PATJ.
Acquires the binding properties of HTR2C;
when associated with S-465.
{ECO:0000269|PubMed:14988405}.
MUTAGEN 471 471 V->A: Loss of interaction with PATJ,
CASK, APBA1, DLG1 and DLG4.
{ECO:0000269|PubMed:14988405}.
SEQUENCE 471 AA; 52603 MW; EF8AAC0BC5379DA2 CRC64;
MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC
LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD
MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP
IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF
VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH
REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA
LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK
SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEEASKDN SDGVNEKVSC V


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