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

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. This receptor is involved in tracheal smooth muscle contraction, bronchoconstriction, and control of aldosterone production.
Subunit structure	Interacts with MPDZ and INADL. May interact with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2. Ref.11 Ref.12
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Note: Localizes to the postsynaptic thickening of axo-dendritic synapses By similarity.
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
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ERK1 and ERK2 cascade Inferred from mutant phenotype PubMed 19057895. Source: UniProtKB aging Inferred from electronic annotation. Source: Compara cell death Inferred from electronic annotation. Source: Compara memory Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transport Inferred from electronic annotation. Source: Compara negative regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara phosphatidylinositol 3-kinase cascade Inferred from mutant phenotype PubMed 16517693. Source: UniProtKB phosphatidylinositol biosynthetic process Inferred from mutant phenotype PubMed 19057895. Source: UniProtKB phospholipase C-activating serotonin receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of vasoconstriction Inferred from electronic annotation. Source: Compara regulation of dopamine secretion Inferred from electronic annotation. Source: Compara release of sequestered calcium ion into cytosol Inferred from direct assay PubMed 15862800. Source: UniProtKB response to drug Inferred from direct assay PubMed 15862800PubMed 18703043. Source: UniProtKB response to stress Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara sleep Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement PubMed 9109547. Source: ProtInc temperature homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara dendritic shaft Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement PubMed 9109547. Source: ProtInc
Molecular_function	1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding Inferred from direct assay PubMed 19057895. Source: UniProtKB drug binding Inferred from direct assay PubMed 15831837PubMed 15862800PubMed 18703043. Source: UniProtKB phosphatidylinositol phospholipase C activity Inferred from mutant phenotype PubMed 16517693. Source: UniProtKB serotonin binding Inferred from direct assay PubMed 15831837PubMed 15862800PubMed 19057895. 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:
     1-54: MDILCEENTS...WTVDSENRTN → MQFLKSAKQK...ISCVNPEDKW
     55-138: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 471	471	5-hydroxytryptamine receptor 2A		PRO_0000068946
Regions
	Topological domain	1 – 75	75	Extracellular By similarity
	Transmembrane	76 – 99	24	Helical; Name=1; By similarity
	Topological domain	100 – 110	11	Cytoplasmic By similarity
	Transmembrane	111 – 132	22	Helical; Name=2; By similarity
	Topological domain	133 – 147	15	Extracellular By similarity
	Transmembrane	148 – 171	24	Helical; Name=3; By similarity
	Topological domain	172 – 191	20	Cytoplasmic By similarity
	Transmembrane	192 – 215	24	Helical; Name=4; By similarity
	Topological domain	216 – 233	18	Extracellular By similarity
	Transmembrane	234 – 254	21	Helical; Name=5; By similarity
	Topological domain	255 – 324	70	Cytoplasmic By similarity
	Transmembrane	325 – 346	22	Helical; Name=6; By similarity
	Topological domain	347 – 362	16	Extracellular By similarity
	Transmembrane	363 – 384	22	Helical; Name=7; By similarity
	Topological domain	385 – 471	87	Cytoplasmic By similarity
	Motif	469 – 471	3	PDZ-binding
Amino acid modifications
	Glycosylation	8	1	N-linked (GlcNAc...) Potential
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	51	1	N-linked (GlcNAc...) Potential
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Disulfide bond	148 ↔ 227		By similarity
Natural variations
	Alternative sequence	1 – 54	54	MDILC…ENRTN → MQFLKSAKQKPNYYHIMLVE DQEEGTLHQFNYCERCSESQ NNKCISCVNPEDKW in isoform 2.		VSP_044593
	Alternative sequence	55 – 138	84	Missing in isoform 2.		VSP_044594
	Natural variant	25	1	T → N. Ref.13 Ref.14 Corresponds to variant rs1805055 [ dbSNP | Ensembl ].		VAR_003448
	Natural variant	197	1	I → V. Ref.15 Corresponds to variant rs6304 [ dbSNP | Ensembl ].		VAR_013901
	Natural variant	447	1	A → V. Ref.15 Corresponds to variant rs6308 [ dbSNP | Ensembl ].		VAR_013902
	Natural variant	452	1	H → Y. Ref.13 Ref.14 Ref.15 Corresponds to variant rs6314 [ dbSNP | Ensembl ].		VAR_003449
Experimental info
	Mutagenesis	463	1	G → V: Loss of interaction with INADL. Ref.12
	Mutagenesis	465	1	N → S: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-470. Ref.12
	Mutagenesis	470	1	C → S: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-465. Ref.12
	Mutagenesis	471	1	V → A: Loss of interaction with INADL, CASK, APBA1, DLG1 and DLG4. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: EF8AAC0BC5379DA2	FASTA	471	52,603
	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
	Isoform 2 [UniParc]. Checksum: 84B45FFECE422D9E	FASTA	387	43,939
	10 20 30 40 50 60 MQFLKSAKQK PNYYHIMLVE DQEEGTLHQF NYCERCSESQ NNKCISCVNP EDKWYRWPLP 70 80 90 100 110 120 SKLCAVWIYL DVLFSTASIM HLCAISLDRY VAIQNPIHHS RFNSRTKAFL KIIAVWTISV 130 140 150 160 170 180 GISMPIPVFG LQDDSKVFKE GSCLLADDNF VLIGSFVSFF IPLTIMVITY FLTIKSLQKE 190 200 210 220 230 240 ATLCVSDLGT RAKLASFSFL PQSSLSSEKL FQRSIHREPG SYTGRRTMQS ISNEQKACKV 250 260 270 280 290 300 LGIVFFLFVV MWCPFFITNI MAVICKESCN EDVIGALLNV FVWIGYLSSA VNPLVYTLFN 310 320 330 340 350 360 KTYRSAFSRY IQCQYKENKK PLQLILVNTI PALAYKSSQL QMGQKKNSKQ DAKTTDNDCS 370 380 MVALGKQHSE EASKDNSDGV NEKVSCV

References

	« Hide 'large scale' referencesShow '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).
[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. , 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. , 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. , 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.
[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]	"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.
[14]	"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.
[15]	"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.
[16]	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.
IPI	IPI00002185. IPI00942926.
PIR	A43956.
RefSeq	NP_000612.1. NM_000621.4.
UniGene	Hs.72630.
3D structure databases
ProteinModelPortal	P28223.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41844N.
MINT	MINT-443877.
STRING	9606.ENSP00000367959.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P28223.
Polymorphism databases
DMDM	543727.
Proteomic databases
PaxDb	P28223.
PRIDE	P28223.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378688; ENSP00000367959; ENSG00000102468. ENST00000542664; ENSP00000437737; ENSG00000102468.
GeneID	3356.
KEGG	hsa:3356.
UCSC	uc010acr.3. human.
Organism-specific databases
CTD	3356.
GeneCards	GC13M047407.
HGNC	HGNC:5293. HTR2A.
HPA	HPA014011.
MIM	182135. gene.
neXtProt	NX_P28223.
PharmGKB	PA193.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG247243.
HOGENOM	HOG000240378.
HOVERGEN	HBG107487.
InParanoid	P28223.
KO	K04157.
OMA	FITNVMA.
OrthoDB	EOG4TMR24.
PhylomeDB	P28223.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P28223.
Bgee	P28223.
CleanEx	HS_HTR2A.
Genevestigator	P28223.
GermOnline	ENSG00000102468. Homo sapiens.
Family and domain databases
InterPro	IPR000455. 5HT2A_rcpt. IPR002231. 5HT_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00516. 5HT2ARECEPTR. PR01101. 5HTRECEPTOR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P28223.
ChEMBL	CHEMBL224.
DrugBank	DB01238. 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.
GenomeRNAi	3356.
NextBio	13270.
SOURCE	Search...

Entry information

Entry name

5HT2A_HUMAN

Accession

Primary (citable) accession number: P28223
Secondary accession number(s): B2RAC5 , B4DZ79, F5GWE8, Q5T8C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.