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Protein

5-hydroxytryptamine receptor 2B

Gene

HTR2B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

GO - Molecular functioni

  • drug binding Source: UniProtKB
  • G-protein alpha-subunit binding Source: UniProtKB
  • GTPase activator activity Source: UniProtKB
  • serotonin binding Source: UniProtKB
  • serotonin receptor activity Source: UniProtKB

GO - Biological processi

  • activation of phospholipase C activity Source: UniProtKB
  • behavior Source: UniProtKB-KW
  • calcium-mediated signaling Source: UniProtKB
  • cardiac muscle hypertrophy Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular response to temperature stimulus Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • embryonic morphogenesis Source: UniProtKB
  • ERK1 and ERK2 cascade Source: UniProtKB
  • G-protein coupled receptor internalization Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • heart morphogenesis Source: UniProtKB
  • intestine smooth muscle contraction Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of cell death Source: UniProtKB
  • neural crest cell differentiation Source: UniProtKB
  • neural crest cell migration Source: UniProtKB
  • phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • phosphorylation Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cytokine production Source: UniProtKB
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of GTPase activity Source: GOC
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of nitric-oxide synthase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • regulation of behavior Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • response to drug Source: UniProtKB
  • serotonin receptor signaling pathway Source: UniProtKB
  • vasoconstriction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

Enzyme and pathway databases

ReactomeiREACT_17064. Serotonin receptors.
REACT_18283. G alpha (q) signalling events.

Protein family/group databases

TCDBi9.A.14.3.7. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 2B
Short name:
5-HT-2B
Short name:
5-HT2B
Alternative name(s):
Serotonin receptor 2B
Gene namesi
Name:HTR2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:5294. HTR2B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656ExtracellularAdd
BLAST
Transmembranei57 – 7923Helical; Name=1Add
BLAST
Topological domaini80 – 9011CytoplasmicAdd
BLAST
Transmembranei91 – 11323Helical; Name=2Add
BLAST
Topological domaini114 – 12916ExtracellularAdd
BLAST
Transmembranei130 – 15122Helical; Name=3Add
BLAST
Topological domaini152 – 17120CytoplasmicAdd
BLAST
Transmembranei172 – 19221Helical; Name=4Add
BLAST
Topological domaini193 – 21624ExtracellularAdd
BLAST
Transmembranei217 – 23923Helical; Name=5Add
BLAST
Topological domaini240 – 32485CytoplasmicAdd
BLAST
Transmembranei325 – 34521Helical; Name=6Add
BLAST
Topological domaini346 – 36015ExtracellularAdd
BLAST
Transmembranei361 – 38222Helical; Name=7Add
BLAST
Topological domaini383 – 48199CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • integral component of plasma membrane Source: InterPro
  • neuron projection Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321L → A: No effect on agonist binding. 1 Publication
Mutagenesisi135 – 1351D → A: Abolishes agonist binding. 1 Publication
Mutagenesisi136 – 1361V → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi139 – 1391S → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi140 – 1401T → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi208 – 2081V → A: No effect on agonist binding. 1 Publication
Mutagenesisi209 – 2091L → A: No effect on agonist binding. 1 Publication
Mutagenesisi211 – 2111K → A: Impairs protein folding and stability. Strongly reduced cell surface expression. 1 Publication
Mutagenesisi217 – 2171F → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi218 – 2181M → A: No effect on agonist binding. 1 Publication
Mutagenesisi225 – 2251A → S: No effect on agonist binding. 1 Publication
Mutagenesisi337 – 3371W → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi340 – 3401F → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi344 – 3441N → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi347 – 3471L → A: No effect on agonist binding. 1 Publication
Mutagenesisi348 – 3481V → A: No effect on agonist binding. 1 Publication
Mutagenesisi362 – 3621L → A: No effect on agonist binding. 1 Publication
Mutagenesisi363 – 3631E → A: No effect on agonist binding. 1 Publication
Mutagenesisi366 – 3661V → A: No effect on agonist binding. 1 Publication
Mutagenesisi370 – 3701Y → A: Slightly decreases agonist binding. 1 Publication

Organism-specific databases

PharmGKBiPA29554.

Chemistry

DrugBankiDB00543. Amoxapine.
DB00714. Apomorphine.
DB06216. Asenapine.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB01242. Clomipramine.
DB00320. Dihydroergotamine.
DB01142. Doxepin.
DB00216. Eletriptan.
DB01049. Ergoloid mesylate.
DB01221. Ketamine.
DB00589. Lisuride.
DB00247. Methysergide.
DB06148. Mianserin.
DB00805. Minaprine.
DB00370. Mirtazapine.
DB00334. Olanzapine.
DB01186. Pergolide.
DB00413. Pramipexole.
DB00268. Ropinirole.
DB00508. Triflupromazine.
DB01392. Yohimbine.

Polymorphism and mutation databases

BioMutaiHTR2B.
DMDMi1168220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4814815-hydroxytryptamine receptor 2BPRO_0000068953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi128 ↔ 207PROSITE-ProRule annotation1 Publication
Disulfide bondi350 ↔ 353PROSITE-ProRule annotation1 Publication
Lipidationi397 – 3971S-palmitoyl cysteineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP41595.
PRIDEiP41595.

PTM databases

PhosphoSiteiP41595.

Expressioni

Tissue specificityi

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.5 Publications

Gene expression databases

BgeeiP41595.
CleanExiHS_HTR2B.
GenevisibleiP41595. HS.

Organism-specific databases

HPAiCAB011448.
HPA012867.

Interactioni

Subunit structurei

Interacts with MPDZ.2 Publications

Protein-protein interaction databases

BioGridi109589. 3 interactions.
MINTiMINT-444010.
STRINGi9606.ENSP00000258400.

Structurei

Secondary structure

1
481
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 6310Combined sources
Helixi65 – 8117Combined sources
Helixi83 – 853Combined sources
Helixi88 – 10619Combined sources
Helixi108 – 1114Combined sources
Helixi113 – 1164Combined sources
Helixi127 – 15832Combined sources
Helixi165 – 18723Combined sources
Helixi189 – 1935Combined sources
Helixi211 – 22515Combined sources
Helixi227 – 24822Combined sources
Helixi314 – 34936Combined sources
Beta strandi351 – 3533Combined sources
Helixi355 – 38127Combined sources
Helixi385 – 39410Combined sources
Turni395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IB4X-ray2.70A36-248[»]
A314-405[»]
4NC3X-ray2.80A36-248[»]
A314-405[»]
ProteinModelPortaliP41595.
SMRiP41595. Positions 48-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1406Agonist binding
Regioni337 – 3415Agonist binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi152 – 1543DRY motif; important for ligand-induced conformation changes
Motifi212 – 2154[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members
Motifi376 – 3805NPxxY motif; important for ligand-induced conformation changes and signaling
Motifi479 – 4813PDZ-binding

Domaini

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

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG247243.
GeneTreeiENSGT00780000121897.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiP41595.
KOiK04157.
OMAiQYNSRAT.
OrthoDBiEOG70ZZN5.
PhylomeDBiP41595.
TreeFamiTF316350.

Family and domain databases

InterProiIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ
60 70 80 90 100
GNKLHWAALL ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD
110 120 130 140 150
LLVGLFVMPI ALLTIMFEAM WPLPLVLCPA WLFLDVLFST ASIMHLCAIS
160 170 180 190 200
VDRYIAIKKP IQANQYNSRA TAFIKITVVW LISIGIAIPV PIKGIETDVD
210 220 230 240 250
NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT IHALQKKAYL
260 270 280 290 300
VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET
310 320 330 340 350
LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC
360 370 380 390 400
DSCNQTTLQM LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR
410 420 430 440 450
ATKSVKTLRK RSSKIYFRNP MAENSKFFKK HGIRNGINPA MYQSPMRLRS
460 470 480
STIQSSSIIL LDTLLLTENE GDKTEEQVSY V
Length:481
Mass (Da):54,298
Last modified:November 1, 1995 - v1
Checksum:iCDA4447ECDBA3B46
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti452 – 4521T → P in CAA85319 (PubMed:7926008).Curated
Sequence conflicti477 – 4771Q → R in AAH63123 (PubMed:15489334).Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451Q → E.1 Publication
Corresponds to variant rs78484969 [ dbSNP | Ensembl ].
VAR_064574
Natural varianti173 – 1731F → L.1 Publication
Corresponds to variant rs77570025 [ dbSNP | Ensembl ].
VAR_064575
Natural varianti388 – 3881R → W.1 Publication
Corresponds to variant rs77982984 [ dbSNP | Ensembl ].
VAR_064576
Natural varianti421 – 4211M → V.
Corresponds to variant rs6736017 [ dbSNP | Ensembl ].
VAR_055907

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2483.1.
PIRiS43687.
S49442.
RefSeqiNP_000858.3. NM_000867.4.
UniGeneiHs.421649.

Genome annotation databases

EnsembliENST00000258400; ENSP00000258400; ENSG00000135914.
GeneIDi3357.
KEGGihsa:3357.
UCSCiuc002vro.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2483.1.
PIRiS43687.
S49442.
RefSeqiNP_000858.3. NM_000867.4.
UniGeneiHs.421649.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IB4X-ray2.70A36-248[»]
A314-405[»]
4NC3X-ray2.80A36-248[»]
A314-405[»]
ProteinModelPortaliP41595.
SMRiP41595. Positions 48-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109589. 3 interactions.
MINTiMINT-444010.
STRINGi9606.ENSP00000258400.

Chemistry

BindingDBiP41595.
ChEMBLiCHEMBL2096904.
DrugBankiDB00543. Amoxapine.
DB00714. Apomorphine.
DB06216. Asenapine.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB01242. Clomipramine.
DB00320. Dihydroergotamine.
DB01142. Doxepin.
DB00216. Eletriptan.
DB01049. Ergoloid mesylate.
DB01221. Ketamine.
DB00589. Lisuride.
DB00247. Methysergide.
DB06148. Mianserin.
DB00805. Minaprine.
DB00370. Mirtazapine.
DB00334. Olanzapine.
DB01186. Pergolide.
DB00413. Pramipexole.
DB00268. Ropinirole.
DB00508. Triflupromazine.
DB01392. Yohimbine.
GuidetoPHARMACOLOGYi7.

Protein family/group databases

TCDBi9.A.14.3.7. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

PhosphoSiteiP41595.

Polymorphism and mutation databases

BioMutaiHTR2B.
DMDMi1168220.

Proteomic databases

PaxDbiP41595.
PRIDEiP41595.

Protocols and materials databases

DNASUi3357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258400; ENSP00000258400; ENSG00000135914.
GeneIDi3357.
KEGGihsa:3357.
UCSCiuc002vro.3. human.

Organism-specific databases

CTDi3357.
GeneCardsiGC02M231936.
HGNCiHGNC:5294. HTR2B.
HPAiCAB011448.
HPA012867.
MIMi601122. gene.
neXtProtiNX_P41595.
PharmGKBiPA29554.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247243.
GeneTreeiENSGT00780000121897.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiP41595.
KOiK04157.
OMAiQYNSRAT.
OrthoDBiEOG70ZZN5.
PhylomeDBiP41595.
TreeFamiTF316350.

Enzyme and pathway databases

ReactomeiREACT_17064. Serotonin receptors.
REACT_18283. G alpha (q) signalling events.

Miscellaneous databases

GeneWikii5-HT2B_receptor.
GenomeRNAii3357.
NextBioi13274.
PROiP41595.
SOURCEiSearch...

Gene expression databases

BgeeiP41595.
CleanExiHS_HTR2B.
GenevisibleiP41595. HS.

Family and domain databases

InterProiIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry namei5HT2B_HUMAN
AccessioniPrimary (citable) accession number: P41595
Secondary accession number(s): B2R9D5
, Q53TI1, Q62221, Q6P523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.