Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P41595 (5HT2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 2B

Short name=5-HT-2B
Short name=5-HT2B
Alternative name(s):
Serotonin receptor 2B
Gene names
Name:HTR2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length481 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 ergot alkaloid derivatives and psychoactive substances. 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. Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity. May play a role in the perception of pain. Plays a role in the regulation of behavior, including impulsive behavior. Required for normal proliferation of embryonic cardiac myocytes and normal heart development. Protects cardiomyocytes against apoptosis. Plays a role in the adaptation of pulmonary arteries to chronic hypoxia. Plays a role in vasoconstriction. Required for normal osteoblast function and proliferation, and for maintaining normal bone density. Required for normal proliferation of the interstitial cells of Cajal in the intestine. Ref.1 Ref.2 Ref.3 Ref.10 Ref.12 Ref.14 Ref.17 Ref.18

Subunit structure

Interacts with MPDZ. Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsesynaptosome By similarity Ref.1 Ref.2 Ref.3 Ref.12 Ref.17 Ref.18.

Tissue specificity

Ubiquitous. Detected in liver, kidney, heart, pulmonary artery, and intestine. Detected at lower levels in blood, placenta and brain, especially in cerebellum, occipital cortex and frontal cortex. Ref.1 Ref.2 Ref.3 Ref.10 Ref.15

Domain

Ligands are bound in a hydrophobic pocket formed by the transmembrane helices.

Polymorphism

A variation at a single nucleotide base, which results in an erroneous stop codon and affects Gln-20, triggers non-sense mediated RNA decay, such that no HTR2B-receptor protein is expressed. It is associated with impulsive behavior and co-segregates with disorders characterized by impulsivity. However, the presence of this variant is not in itself sufficient to cause impulsive behavior: male sex, testosterone level, alcohol and stress exposure are other factors playing important roles.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
Synaptosome
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 19308295. Source: UniProtKB

G-protein coupled receptor internalization

Inferred from electronic annotation. Source: Ensembl

G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 15625277. Source: UniProtKB

activation of phospholipase C activity

Inferred from direct assay PubMed 16517693PubMed 19057895. Source: UniProtKB

behavior

Inferred from electronic annotation. Source: UniProtKB-KW

cGMP biosynthetic process

Inferred from direct assay Ref.12. Source: UniProtKB

calcium-mediated signaling

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cardiac muscle hypertrophy

Inferred from sequence or structural similarity. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from direct assay PubMed 16517693PubMed 19057895. Source: UniProtKB

cellular response to temperature stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

heart morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

intestine smooth muscle contraction

Inferred from mutant phenotype PubMed 7599919PubMed 9186750. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of autophagy

Inferred from mutant phenotype PubMed 20099302. Source: UniProtKB

negative regulation of cell death

Inferred from mutant phenotype PubMed 20099302. Source: UniProtKB

neural crest cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

neural crest cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 16517693. Source: UniProtKB

phosphorylation

Inferred from mutant phenotype PubMed 19308295. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 19057895. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 15625277. Source: UniProtKB

positive regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 15625277. Source: UniProtKB

positive regulation of cytokine production

Inferred from direct assay PubMed 19023134. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 19308295. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 15625277. Source: UniProtKB

positive regulation of phosphatidylinositol biosynthetic process

Inferred from direct assay PubMed 19057895. Source: UniProtKB

protein kinase C signaling

Inferred from mutant phenotype PubMed 20099302. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of behavior

Inferred from mutant phenotype Ref.15. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 15862800. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 15625277PubMed 15862800Ref.14. Source: UniProtKB

serotonin receptor signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

vasoconstriction

Inferred from mutant phenotype PubMed 15625277. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 15925089. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.12PubMed 15625277PubMed 15862800Ref.14PubMed 19023134Ref.2. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionG-protein alpha-subunit binding

Inferred from mutant phenotype PubMed 15625277. Source: UniProtKB

Ras GTPase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from direct assay Ref.12PubMed 15625277PubMed 15831837PubMed 15862800PubMed 17609583Ref.14PubMed 19307114Ref.2. Source: UniProtKB

serotonin binding

Inferred from direct assay PubMed 15625277PubMed 15831837PubMed 15862800PubMed 17609583PubMed 19057895Ref.2. Source: UniProtKB

serotonin receptor activity

Inferred from direct assay PubMed 15862800Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4814815-hydroxytryptamine receptor 2B
PRO_0000068953

Regions

Topological domain1 – 5656Extracellular Ref.18
Transmembrane57 – 7923Helical; Name=1
Topological domain80 – 9011Cytoplasmic Ref.18
Transmembrane91 – 11323Helical; Name=2
Topological domain114 – 12916Extracellular Ref.18
Transmembrane130 – 15122Helical; Name=3
Topological domain152 – 17120Cytoplasmic Ref.18
Transmembrane172 – 19221Helical; Name=4
Topological domain193 – 21624Extracellular Ref.18
Transmembrane217 – 23923Helical; Name=5
Topological domain240 – 32485Cytoplasmic Ref.18
Transmembrane325 – 34521Helical; Name=6
Topological domain346 – 36015Extracellular Ref.18
Transmembrane361 – 38222Helical; Name=7
Topological domain383 – 48199Cytoplasmic Ref.18
Region135 – 1406Agonist binding
Region337 – 3415Agonist binding
Motif152 – 1543DRY motif; important for ligand-induced conformation changes
Motif212 – 2154[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members
Motif376 – 3805NPxxY motif; important for ligand-induced conformation changes and signaling
Motif479 – 4813PDZ-binding

Amino acid modifications

Lipidation3971S-palmitoyl cysteine Potential
Glycosylation301N-linked (GlcNAc...) Potential
Disulfide bond128 ↔ 207 Ref.18
Disulfide bond350 ↔ 353 Ref.18

Natural variations

Natural variant451Q → E. Ref.15
Corresponds to variant rs78484969 [ dbSNP | Ensembl ].
VAR_064574
Natural variant1731F → L. Ref.15
Corresponds to variant rs77570025 [ dbSNP | Ensembl ].
VAR_064575
Natural variant3881R → W. Ref.15
Corresponds to variant rs77982984 [ dbSNP | Ensembl ].
VAR_064576
Natural variant4211M → V.
Corresponds to variant rs6736017 [ dbSNP | Ensembl ].
VAR_055907

Experimental info

Mutagenesis1321L → A: No effect on agonist binding. Ref.17
Mutagenesis1351D → A: Abolishes agonist binding. Ref.17
Mutagenesis1361V → A: Slightly decreases agonist binding. Ref.17
Mutagenesis1391S → A: Slightly decreases agonist binding. Ref.17
Mutagenesis1401T → A: Slightly decreases agonist binding. Ref.17
Mutagenesis2081V → A: No effect on agonist binding. Ref.17
Mutagenesis2091L → A: No effect on agonist binding. Ref.17
Mutagenesis2111K → A: Impairs protein folding and stability. Strongly reduced cell surface expression. Ref.17
Mutagenesis2171F → A: Slightly decreases agonist binding. Ref.17
Mutagenesis2181M → A: No effect on agonist binding. Ref.17
Mutagenesis2251A → S: No effect on agonist binding. Ref.17
Mutagenesis3371W → A: Slightly decreases agonist binding. Ref.17
Mutagenesis3401F → A: Slightly decreases agonist binding. Ref.17
Mutagenesis3441N → A: Slightly decreases agonist binding. Ref.17
Mutagenesis3471L → A: No effect on agonist binding. Ref.17
Mutagenesis3481V → A: No effect on agonist binding. Ref.17
Mutagenesis3621L → A: No effect on agonist binding. Ref.17
Mutagenesis3631E → A: No effect on agonist binding. Ref.17
Mutagenesis3661V → A: No effect on agonist binding. Ref.17
Mutagenesis3701Y → A: Slightly decreases agonist binding. Ref.17
Sequence conflict4521T → P in CAA85319. Ref.2
Sequence conflict4771Q → R in AAH63123. Ref.9

Secondary structure

................................ 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41595 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CDA4447ECDBA3B46

FASTA48154,298
        10         20         30         40         50         60 
MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ GNKLHWAALL 

        70         80         90        100        110        120 
ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD LLVGLFVMPI ALLTIMFEAM 

       130        140        150        160        170        180 
WPLPLVLCPA WLFLDVLFST ASIMHLCAIS VDRYIAIKKP IQANQYNSRA TAFIKITVVW 

       190        200        210        220        230        240 
LISIGIAIPV PIKGIETDVD NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT 

       250        260        270        280        290        300 
IHALQKKAYL VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET 

       310        320        330        340        350        360 
LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC DSCNQTTLQM 

       370        380        390        400        410        420 
LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR ATKSVKTLRK RSSKIYFRNP 

       430        440        450        460        470        480 
MAENSKFFKK HGIRNGINPA MYQSPMRLRS STIQSSSIIL LDTLLLTENE GDKTEEQVSY 


V 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional characterization of the human 5-HT2B serotonin receptor."
Schmuck K., Ullmer C., Engels P., Luebbert H.
FEBS Lett. 342:85-90(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"The human serotonin 5-HT2B receptor: pharmacological link between 5-HT2 and 5-HT1D receptors."
Choi D.S., Birraux G., Launay J.-M., Maroteaux L.
FEBS Lett. 352:393-399(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Molecular cloning, functional expression, and mRNA tissue distribution of the human 5-hydroxytryptamine2B receptor."
Kursar J.D., Nelson D.L., Wainscott D.B., Baez M.
Mol. Pharmacol. 46:227-234(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Uterus.
[4]"Mutation screening of human 5-HT(2B) receptor gene in early-onset obsessive-compulsive disorder."
Kim S.J., Veenstra-VanderWeele J., Hanna G.L., Gonen D., Leventhal B.L., Cook E.H. Jr.
Mol. Cell. Probes 14:47-52(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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 (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[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].
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"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].
Tissue: Skin.
[10]"5-HT2B receptor-mediated calcium release from ryanodine-sensitive intracellular stores in human pulmonary artery endothelial cells."
Ullmer C., Boddeke H.G., Schmuck K., Lubbert H.
Br. J. Pharmacol. 117:1081-1088(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[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]"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.
[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.
[15]"A population-specific HTR2B stop codon predisposes to severe impulsivity."
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., Virkkunen M., Goldman D.
Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IMPULSIVE BEHAVIOR, TISSUE SPECIFICITY, POLYMORPHISM, VARIANTS GLU-45; LEU-173 AND TRP-388.
[16]"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.
[17]"Structural basis for molecular recognition at serotonin receptors."
Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., Liu W., Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., Melcher K., Zhang C., Bai F., Yang H., Yang L. expand/collapse author list , Jiang H., Roth B.L., Cherezov V., Stevens R.C., Xu H.E.
Science 340:610-614(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-132; ASP-135; VAL-136; SER-139; THR-140; VAL-208; LEU-209; LYS-211; PHE-217; MET-218; ALA-225; TRP-337; PHE-340; ASN-344; LEU-347; VAL-348; LEU-362; GLU-363; VAL-366 AND TYR-370.
[18]"Structural features for functional selectivity at serotonin receptors."
Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E., McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., Cherezov V., Roth B.L., Stevens R.C.
Science 340:615-619(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-405 IN COMPLEX WITH THE AGONIST ERGOTAMINE, FUNCTION, ROLE IN ARRESTIN-MEDIATED SIGNALING AND CALCIUM RELEASE, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Protein Spotlight

On the spur of a whim - Issue 127 of March 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77307 mRNA. Translation: CAA54513.1.
Z36748 mRNA. Translation: CAA85319.1.
AF156160, AF156158, AF156159 Genomic DNA. Translation: AAD39259.1.
AY136751 mRNA. Translation: AAN01277.1.
AC009407 Genomic DNA. Translation: AAX93128.1.
AK313741 mRNA. Translation: BAG36482.1.
CH471063 Genomic DNA. Translation: EAW70949.1.
BC063123 mRNA. Translation: AAH63123.1.
PIRS43687.
S49442.
RefSeqNP_000858.3. NM_000867.4.
UniGeneHs.421649.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IB4X-ray2.70A36-405[»]
4NC3X-ray2.80A36-248[»]
A314-405[»]
ProteinModelPortalP41595.
SMRP41595. Positions 48-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109589. 3 interactions.
MINTMINT-444010.
STRING9606.ENSP00000258400.

Chemistry

BindingDBP41595.
ChEMBLCHEMBL1833.
DrugBankDB01239. Chlorprothixene.
DB00216. Eletriptan.
DB00574. Fenfluramine.
DB01403. Methotrimeprazine.
DB00805. Minaprine.
DB01224. Quetiapine.
DB00669. Sumatriptan.
DB01079. Tegaserod.
DB00508. Triflupromazine.
GuidetoPHARMACOLOGY7.

Protein family/group databases

TCDB9.A.14.3.7. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP41595.

Polymorphism databases

DMDM1168220.

Proteomic databases

PaxDbP41595.
PRIDEP41595.

Protocols and materials databases

DNASU3357.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258400; ENSP00000258400; ENSG00000135914.
GeneID3357.
KEGGhsa:3357.
UCSCuc002vro.3. human.

Organism-specific databases

CTD3357.
GeneCardsGC02M231936.
HGNCHGNC:5294. HTR2B.
HPACAB011448.
HPA012867.
MIM601122. gene.
neXtProtNX_P41595.
PharmGKBPA29554.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247243.
HOGENOMHOG000240378.
HOVERGENHBG107487.
InParanoidP41595.
KOK04157.
OMAQYNSRAT.
OrthoDBEOG70ZZN5.
PhylomeDBP41595.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP41595.
BgeeP41595.
CleanExHS_HTR2B.
GenevestigatorP41595.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00651. 5HT2BRECEPTR.
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-HT2B_receptor.
GenomeRNAi3357.
NextBio13274.
PROP41595.
SOURCESearch...

Entry information

Entry name5HT2B_HUMAN
AccessionPrimary (citable) accession number: P41595
Secondary accession number(s): B2R9D5 expand/collapse secondary AC list , Q53TI1, Q62221, Q6P523
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 136 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 2

Human chromosome 2: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries