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P28223 (5HT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 2A

Short name=5-HT-2
Short name=5-HT-2A
Alternative name(s):
Serotonin receptor 2A
Gene names
Name:HTR2A
Synonyms:HTR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
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 mescaline, psilocybin, 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 phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca2+ ions from intracellular stores. Affects neural activity, perception, cognition and mood. 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. Ref.10 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19

Subunit structure

Interacts with MPDZ and INADL. May interact with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2. Interacts with GRM2 and DRD2; this may affect signaling. Ref.11 Ref.12 Ref.15 Ref.17 Ref.19

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell projectiondendrite By similarity. Cell projectionaxon By similarity. Cytoplasmic vesicle By similarity. Membranecaveola By similarity. Note: Localizes to the postsynaptic thickening of axo-dendritic synapses By similarity. Ref.10 Ref.14 Ref.15 Ref.17 Ref.19

Tissue specificity

Detected in brain cortex (at protein level). Detected in blood platelets. Ref.15

Domain

The PDZ domain-binding motif is involved in the interaction with INADL, CASK, APBA1, DLG1 and DLG4.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell membrane
Cell projection
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Inferred from direct assay PubMed 16517693. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

artery smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

behavioral response to cocaine

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from direct assay PubMed 16517693Ref.16. Source: UniProtKB

detection of mechanical stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

detection of temperature stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 16517693. Source: UniProtKB

phospholipase C-activating serotonin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

regulation of behavior

Inferred from electronic annotation. Source: InterPro

regulation of dopamine secretion

Inferred from electronic annotation. Source: Ensembl

regulation of hormone secretion

Inferred from electronic annotation. Source: InterPro

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 15862800. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 15862800Ref.14. Source: UniProtKB

serotonin receptor signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

sleep

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement PubMed 9109547. Source: ProtInc

temperature homeostasis

Inferred from electronic annotation. Source: Ensembl

urinary bladder smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: UniProtKB-SubCell

caveola

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell body fiber

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement PubMed 9109547. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15862800Ref.14. Source: UniProtKB

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

Inferred from direct assay Ref.16. Source: UniProtKB

drug binding

Inferred from direct assay PubMed 15831837PubMed 15862800Ref.14. Source: UniProtKB

serotonin binding

Inferred from direct assay PubMed 15831837PubMed 15862800Ref.16. Source: UniProtKB

serotonin receptor activity

Inferred from direct assay PubMed 15862800. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28223-1)

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: P28223-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: MDILCEENTS...PVSMLTILYG → MQFLKSAKQK...ISCVDPEDKW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4714715-hydroxytryptamine receptor 2A
PRO_0000068946

Regions

Topological domain1 – 7575Extracellular By similarity
Transmembrane76 – 9924Helical; Name=1; By similarity
Topological domain100 – 11011Cytoplasmic By similarity
Transmembrane111 – 13222Helical; Name=2; By similarity
Topological domain133 – 14816Extracellular By similarity
Transmembrane149 – 17123Helical; Name=3; By similarity
Topological domain172 – 19120Cytoplasmic By similarity
Transmembrane192 – 21524Helical; Name=4; By similarity
Topological domain216 – 23318Extracellular By similarity
Transmembrane234 – 25421Helical; Name=5; By similarity
Topological domain255 – 32470Cytoplasmic By similarity
Transmembrane325 – 34622Helical; Name=6; By similarity
Topological domain347 – 36216Extracellular By similarity
Transmembrane363 – 38422Helical; Name=7; By similarity
Topological domain385 – 47187Cytoplasmic By similarity
Region155 – 1606Agonist binding By similarity
Region336 – 3405Agonist binding By similarity
Motif172 – 1743DRY motif; important for ligand-induced conformation changes By similarity
Motif376 – 3805NPxxY motif; important for ligand-induced conformation changes and signaling By similarity
Motif469 – 4713PDZ-binding

Amino acid modifications

Glycosylation81N-linked (GlcNAc...) Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation541N-linked (GlcNAc...) Potential
Disulfide bond148 ↔ 227 By similarity
Disulfide bond349 ↔ 353 By similarity

Natural variations

Alternative sequence1 – 138138MDILC…TILYG → MQFLKSAKQKPNYYHIMLVE DQEEGTLHQFNYCERCSESQ NNKCISCVDPEDKW in isoform 2.
VSP_046663
Natural variant251T → N. Ref.20 Ref.21
Corresponds to variant rs1805055 [ dbSNP | Ensembl ].
VAR_003448
Natural variant1971I → V. Ref.22
Corresponds to variant rs6304 [ dbSNP | Ensembl ].
VAR_013901
Natural variant4471A → V. Ref.22
Corresponds to variant rs6308 [ dbSNP | Ensembl ].
VAR_013902
Natural variant4521H → Y. Ref.20 Ref.21 Ref.22
Corresponds to variant rs6314 [ dbSNP | Ensembl ].
VAR_003449

Experimental info

Mutagenesis4631G → V: Loss of interaction with INADL. Ref.12
Mutagenesis4651N → S: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-470. Ref.12
Mutagenesis4701C → S: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-465. Ref.12
Mutagenesis4711V → A: Loss of interaction with INADL, CASK, APBA1, DLG1 and DLG4. Ref.12
Isoform 2:
Sequence conflict491D → N in BAG63991. Ref.5

Sequences

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

Last modified June 1, 1994. Version 2.
Checksum: EF8AAC0BC5379DA2

FASTA47152,603
        10         20         30         40         50         60 
MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC 

        70         80         90        100        110        120 
LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD 

       130        140        150        160        170        180 
MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP 

       190        200        210        220        230        240 
IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF 

       250        260        270        280        290        300 
VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH 

       310        320        330        340        350        360 
REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA 

       370        380        390        400        410        420 
LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK 

       430        440        450        460        470 
SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEEASKDN SDGVNEKVSC V 

« Hide

Isoform 2 [UniParc].

Checksum: DA98167A87C1AAB7
Show »

FASTA38743,940

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 stem.
[2]"The human 5-HT2 receptor is encoded by a multiple intron-exon gene."
Chen K., Yang W., Grimsby J., Shih J.C.
Brain Res. Mol. Brain Res. 14:20-26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Primary structure of the human platelet serotonin 5-HT2A receptor: identify with frontal cortex serotonin 5-HT2A receptor."
Cook E.H. Jr., Fletcher K.E., Wainwright M., Marks N., Yan S.Y., Leventhal B.L.
J. Neurochem. 63:465-469(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Platelet.
[4]"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.
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Testis and Thalamus.
[6]"The DNA sequence and analysis of human chromosome 13."
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. expand/collapse author list , 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.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
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).
Tissue: Lung.
[9]"Cloning and nucleotide sequence of the human(5HT) type 2 receptor."
Tritch R.J., Robinson D.L., Sahagan B.G., Horlick R.A.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-464 (ISOFORM 1).
Tissue: Brain.
[10]"Genomic organization, coding sequence and functional expression of human 5-HT2 and 5-HT1A receptor genes."
Stam N.J., van Huizen F., van Alebeek C., Brands J., Dijkema R., Tonnaer J.A., Olijve W.
Eur. J. Pharmacol. 227:153-162(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218, FUNCTION, SUBCELLULAR LOCATION.
[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]"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins."
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.
J. Biol. Chem. 279:20257-20266(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INADL; MPP3; PRDX6; DLG4; DLG1; CASK; APBA1 AND MAGI2, MUTAGENESIS OF GLY-463; ASN-465; CYS-470 AND VAL-471.
[13]"Serotonin receptors."
Nichols D.E., Nichols C.D.
Chem. Rev. 108:1614-1641(2008) [PubMed] [Europe PMC] [Abstract]
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, SUBCELLULAR LOCATION.
[15]"Identification of a serotonin/glutamate receptor complex implicated in psychosis."
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.
Nature 452:93-97(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRM2, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[16]"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.
[17]"Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine D2 receptors."
Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.
Neuropharmacology 61:770-777(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DRD2, FUNCTION, SUBCELLULAR LOCATION.
[18]"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.
[19]"Heterocomplex formation of 5-HT2A-mGlu2 and its relevance for cellular signaling cascades."
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.
Neuropharmacology 62:2184-2191(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRM2, FUNCTION, SUBCELLULAR LOCATION.
[20]"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."
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.
Hum. Genet. 97:614-619(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-25 AND TYR-452.
[21]"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: VARIANTS ASN-25 AND TYR-452.
[22]"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: VARIANTS VAL-197; VAL-447 AND TYR-452.
[23]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.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57830 mRNA. Translation: CAA40963.1.
S42168, S42165, S42167 Genomic DNA. Translation: AAB22791.2.
S71229 mRNA. Translation: AAB31320.1.
AF498982 mRNA. Translation: AAM21129.1.
AK302787 mRNA. Translation: BAG63991.1.
AK314132 mRNA. Translation: BAG36822.1.
AL160397, AL136958 Genomic DNA. Translation: CAI16877.1.
AL136958, AL160397 Genomic DNA. Translation: CAI12227.1.
CH471075 Genomic DNA. Translation: EAX08770.1.
BC069356 mRNA. Translation: AAH69356.1.
BC069576 mRNA. Translation: AAH69576.1.
BC074848 mRNA. Translation: AAH74848.1.
BC074849 mRNA. Translation: AAH74849.1.
BC096839 mRNA. Translation: AAH96839.1.
M86841 mRNA. Translation: AAA58354.1.
S50130, S49737, S50113 Genomic DNA. Translation: AAB24166.2.
PIRA43956.
RefSeqNP_000612.1. NM_000621.4.
NP_001159419.1. NM_001165947.2.
UniGeneHs.72630.

3D structure databases

ProteinModelPortalP28223.
SMRP28223. Positions 38-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109588. 4 interactions.
DIPDIP-41844N.
MINTMINT-443877.
STRING9606.ENSP00000367959.

Chemistry

BindingDBP28223.
ChEMBLCHEMBL2095200.
DrugBankDB01238. Aripiprazole.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB00604. Cisapride.
DB01242. Clomipramine.
DB00363. Clozapine.
DB00924. Cyclobenzaprine.
DB00434. Cyproheptadine.
DB00320. Dihydroergotamine.
DB00843. Donepezil.
DB00751. Epinastine.
DB00696. Ergotamine.
DB00176. Fluvoxamine.
DB00933. Mesoridazine.
DB00247. Methysergide.
DB06148. Mianserin.
DB00805. Minaprine.
DB00370. Mirtazapine.
DB01149. Nefazodone.
DB00334. Olanzapine.
DB01267. Paliperidone.
DB00715. Paroxetine.
DB00433. Prochlorperazine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB06144. Sertindole.
DB00372. Thiethylperazine.
DB00679. Thioridazine.
DB00752. Tranylcypromine.
DB00656. Trazodone.
DB00285. Venlafaxine.
DB00246. Ziprasidone.
GuidetoPHARMACOLOGY6.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP28223.

Polymorphism databases

DMDM543727.

Proteomic databases

PaxDbP28223.
PRIDEP28223.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378688; ENSP00000367959; ENSG00000102468. [P28223-1]
ENST00000542664; ENSP00000437737; ENSG00000102468. [P28223-1]
ENST00000543956; ENSP00000441861; ENSG00000102468. [P28223-2]
GeneID3356.
KEGGhsa:3356.
UCSCuc010acr.4. human. [P28223-1]

Organism-specific databases

CTD3356.
GeneCardsGC13M047407.
HGNCHGNC:5293. HTR2A.
HPAHPA014011.
MIM182135. gene.
neXtProtNX_P28223.
PharmGKBPA193.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247243.
HOGENOMHOG000240378.
HOVERGENHBG107487.
InParanoidP28223.
KOK04157.
OMAFITNVMA.
OrthoDBEOG70ZZN5.
PhylomeDBP28223.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP28223.

Gene expression databases

ArrayExpressP28223.
BgeeP28223.
CleanExHS_HTR2A.
GenevestigatorP28223.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000455. 5HT2A_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF30. PTHR24247:SF30. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00516. 5HT2ARECEPTR.
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-HT2A_receptor.
GenomeRNAi3356.
NextBio13270.
PROP28223.
SOURCESearch...

Entry information

Entry name5HT2A_HUMAN
AccessionPrimary (citable) accession number: P28223
Secondary accession number(s): B2RAC5 expand/collapse secondary AC list , B4DZ79, F5GWE8, Q5T8C0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 145 of the entry and version 2 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 13

Human chromosome 13: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries