Protein detail

5HT2B

5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (Serotonin receptor 2B)

Entry name 5HT2B	UniProt ID P41595	EVMP confidence score 0.25
Supporting publications (n) 2	Transmembrane count 7	Protein classification FDA approved drug targetsG-protein coupled receptorsPredicted membrane proteinsTransporters

EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information13

Protein Names

5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (Serotonin receptor 2B)

Protein Class (4)

FDA approved drug targetsG-protein coupled receptorsPredicted membrane proteinsTransporters

Protein Function (4)

G-protein coupled receptors:Serotonin receptors
Transporters
FDA approved drug targets:Small molecule drugs
G-protein coupled receptors:GPCRs excl olfactory receptors

Transmembrane

57..79; Helical; Name=1; 91..113; Helical; Name=2; 130..151; Helical; Name=3; 172..192; Helical; Name=4; 217..239; Helical; Name=5; 325..345; Helical; Name=6; 361..382; Helical; Name=7

Transmembrane Count

Ensembl

ENSG00000135914

Entrez Gene Symbol

HTR2B

Gene Synonym (2)

5-HT(2B)5-HT2B

Gene Description

5-hydroxytryptamine receptor 2B

Chromosome

Position

231108230-231125042

Supporting publications (n)

EVMP confidence score

0.25

Fluorescence & Localization5

Tissue Specificlymphoid tissueCell SpecificcDCSingle-Nuclei Brain Specificcentral nervous system macrophageBlood Cell SpecificbasophilBlood Lineage Specificgranulocytes

Function & Pathway7

Protein Function (4)

G-protein coupled receptors:Serotonin receptors
Transporters
FDA approved drug targets:Small molecule drugs
G-protein coupled receptors:GPCRs excl olfactory receptors

Cellular Component (6)

Molecular Function (8)

Biological Process (3)

KEGG (6)

Reactome (6)

Mediation Categories (5)

Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation

Relations & Evidence54

Ligand-Receptor Signaling (46)

46 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
7tm_a	receptor	HPMR	No	Yes	No	Yes	No
serotonin_7tm_a	receptor	HPMR	No	Yes	No	Yes	No
rhodopsin	receptor	Surfaceome	No	Yes	No	Yes	No
gpcr	receptor	Surfaceome	No	Yes	No	Yes	No
class_a_rhodopsin	receptor	GPCRdb	No	Yes	No	Yes	No
class_a_rhodopsin_aminergic	receptor	GPCRdb	No	Yes	No	Yes	No
class_a_rhodopsin_aminergic_5_hydroxytryptamine	receptor	GPCRdb	No	Yes	No	Yes	No
receptor	receptor	OmniPath	No	Yes	No	Yes	No
extracellular	extracellular	HPMR	No	No	No	Yes	No
extracellular	extracellular	OmniPath	No	No	No	Yes	No

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Regulatory Interaction Network (5)

5 records.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
5HT2B	P41595	GNAI1	P63096	Yes	Yes	No	SIGNOR	SIGNOR:31160049
5HT2B	P41595	GNAI3	P08754	Yes	Yes	No	SIGNOR	SIGNOR:31160049
5HT2B	P41595	GNAQ	P50148	Yes	Yes	No	HPRDWangSIGNOR	HPRD:11916537 SIGNOR:31160049
5HT2B	P41595	GNAZ	P19086	Yes	Yes	No	SIGNOR	SIGNOR:31160049
5HT2B	P41595	GNA14	O95837	Yes	Yes	No	WangSIGNOR	SIGNOR:31160049

Protein Complex Composition (2)

2 records.

Component Name	Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs	References
	HTR2B	P41595	2	PDB	PDB:5tud
	ARRB1 HTR2B	P41595 P49407	1:1	PDB	PDB:7srs

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
	Mass spectrometry	0

Sequence, Structure & Domains11

Sequences

Length

481

Mass

54,298

Sequence

MALSYRVSELQSTIPEHILQSTFVHVISSNWSGLQTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIMHLCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNITCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAYLVKNKPPQRLTWLTVSTVFQRDETPCSSPEKVAMLDGSRKDKALPNSGDETLMRRTSTIGKKSVQTISNEQRASKVLGIVFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCNYRATKSVKTLRKRSSKIYFRNPMAENSKFFKKHGIRNGINPAMYQSPMRLRSSTIQSSSIILLDTLLLTENEGDKTEEQVSYV

3D Structural Models

Turn

117..119; 395..397

Helix

40..49; 54..63; 65..81; 83..85; 88..106; 108..111; 113..116; 127..158; 160..163; 165..187; 189..193; 202..204; 211..225; 227..248; 281..284; 314..349; 355..381; 385..394

Beta Strand

198..201; 351..353

3D Structure

Electron microscopy (4); X-ray crystallography (8)

Domain & Motif Annotations

Motif

152..154; DRY motif; important for ligand-induced conformation changes; 212..215; [DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members; 376..380; NPxxY motif; important for ligand-induced conformation changes and signaling; 479..481; PDZ-binding

Domain (CC)

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

Protein Families

G-protein coupled receptor 1 family

Sequence Similarities

Belongs to the G-protein coupled receptor 1 family.

Clinical Relevance6

Disease Involvement

FDA approved drug targets

Related Diseases (9)

Anxiety disorder Attention deficit hyperactivity disorder Coronary atherosclerosis Depression Irritable bowel syndrome Migraine Pituitary gland disorder Psychotic disorder Pulmonary hypertension

Biomarker

Discontinued in Phase 3; Phase 4; Withdrawn from market; Approved; Investigative; Discontinued in Phase 1; Phase 2

Drug Targets

FDA approved drug targets

Antibody (2)

HPA012867 HPA063658

Supporting Publications2

PMID	Title	Abstract
9296387	Aggregation reroutes molecules from a recycling to a vesicle-mediated secretion pathway during reticulocyte maturation.	Endocytosis of the Tf/TfR complex is essentially the only pathway active in maturing reticulocytes, while exosomes, formed by invagination of the endosomal membrane, provide a mechanism to eliminate seemingly obsolescent proteins, including the TfR, when their function is completed. Prior to elimination via exosomes, the TfR actively recycles with a half-time of approx. Thus antibody-induced aggregation of specific proteins like the TfR and AChE, which are normally sorted into exosomes during reticulocyte maturation, enhances their shedding by the exosomal pathway.
9516159	Decay-accelerating factor (CD55) and membrane inhibitor of reactive lysis (CD59) are released within exosomes during In vitro maturation of reticulocytes.	The presence of AChE, decay-accelerating factor (DAF), membrane inhibitor of reactive lysis (MIRL), and lymphocyte function-associated antigen 3 (LFA-3) on the surface of exosomes obtained from normal and paroxysmal nocturnal hemoglobinuria (PNH) reticulocytes, suggests that (1) the GPI anchor is efficiently sorted during exosome formation, (2) exosome release could account for the observed discrepancy in GPI-protein expression between reticulocytes and erythrocytes from PNH patients, and (3) exosomes could have another physiologic function related to controlling membrane attack complex formation. To better understand the molecular events leading to protein sorting in exosomes, we analyzed the expression of glycosylphosphatidylinositol (GPI)-anchored proteins on the exosome surface through a technique involving bead coupling and flow cytometry immunodetection.