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Q02152

- 5HT2B_MOUSE

UniProt

Q02152 - 5HT2B_MOUSE

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Protein

5-hydroxytryptamine receptor 2B

Gene

Htr2b

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.10 Publications

GO - Molecular functioni

  1. drug binding Source: UniProtKB
  2. G-protein alpha-subunit binding Source: UniProtKB
  3. Ras GTPase activator activity Source: UniProtKB
  4. serotonin binding Source: UniProtKB
  5. serotonin receptor activity Source: UniProtKB

GO - Biological processi

  1. activation of phospholipase C activity Source: Ensembl
  2. behavior Source: UniProtKB-KW
  3. calcium-mediated signaling Source: UniProtKB
  4. cardiac muscle hypertrophy Source: UniProtKB
  5. cellular response to temperature stimulus Source: UniProtKB
  6. cGMP biosynthetic process Source: UniProtKB
  7. embryonic morphogenesis Source: UniProtKB
  8. ERK1 and ERK2 cascade Source: UniProtKB
  9. G-protein coupled receptor internalization Source: UniProtKB
  10. G-protein coupled receptor signaling pathway Source: UniProtKB
  11. heart development Source: MGI
  12. heart morphogenesis Source: UniProtKB
  13. intestine smooth muscle contraction Source: UniProtKB
  14. negative regulation of apoptotic process Source: UniProtKB
  15. negative regulation of autophagy Source: UniProtKB
  16. negative regulation of cell death Source: UniProtKB
  17. neural crest cell differentiation Source: UniProtKB
  18. neural crest cell migration Source: UniProtKB
  19. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  20. phospholipase C-activating serotonin receptor signaling pathway Source: MGI
  21. phosphorylation Source: UniProtKB
  22. positive regulation of cell division Source: UniProtKB
  23. positive regulation of cell proliferation Source: UniProtKB
  24. positive regulation of cytokine production Source: UniProtKB
  25. positive regulation of cytokine secretion Source: UniProtKB
  26. positive regulation of endothelial cell proliferation Source: UniProtKB
  27. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  28. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  29. positive regulation of MAP kinase activity Source: Ensembl
  30. positive regulation of nitric-oxide synthase activity Source: UniProtKB
  31. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  32. positive regulation of Ras GTPase activity Source: GOC
  33. protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  34. protein kinase C signaling Source: UniProtKB
  35. regulation of behavior Source: UniProtKB
  36. release of sequestered calcium ion into cytosol Source: UniProtKB
  37. response to drug Source: UniProtKB
  38. serotonin receptor signaling pathway Source: UniProtKB
  39. vasoconstriction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_232980. Serotonin receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 2B
Short name:
5-HT-2B
Short name:
5-HT2B
Alternative name(s):
5-HT-2F
NP75 protein
Serotonin receptor 2B
Gene namesi
Name:Htr2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:109323. Htr2b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555ExtracellularBy similarityAdd
BLAST
Transmembranei56 – 7823Helical; Name=1By similarityAdd
BLAST
Topological domaini79 – 8911CytoplasmicBy similarityAdd
BLAST
Transmembranei90 – 11223Helical; Name=2By similarityAdd
BLAST
Topological domaini113 – 12816ExtracellularBy similarityAdd
BLAST
Transmembranei129 – 15022Helical; Name=3By similarityAdd
BLAST
Topological domaini151 – 17020CytoplasmicBy similarityAdd
BLAST
Transmembranei171 – 19121Helical; Name=4By similarityAdd
BLAST
Topological domaini192 – 21524ExtracellularBy similarityAdd
BLAST
Transmembranei216 – 23823Helical; Name=5By similarityAdd
BLAST
Topological domaini239 – 32385CytoplasmicBy similarityAdd
BLAST
Transmembranei324 – 34421Helical; Name=6By similarityAdd
BLAST
Topological domaini345 – 35915ExtracellularBy similarityAdd
BLAST
Transmembranei360 – 38122Helical; Name=7By similarityAdd
BLAST
Topological domaini382 – 47998CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB
  3. integral component of plasma membrane Source: InterPro
  4. neuron projection Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
  6. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Partial embryonic and perinatal lethality, due to heart ventricle hypoplasia and impaired proliferative capacity of heart myocytes. Mutant mice that survive into adulthood have a decreased heart weight relative to body weight. They display dilated cardiomyopathy with a loss of ventricular mass, due to a reduction in the number and size of cardiomyocytes. The myocardium from mutant mice displays abnormal organization of the contractile elements, with an irregular array of sarcomeric myofibrils and abnormally wide Z bands. In addition, heart muscle mitochondria display structural and functional defects. Mutant mice do not respond to chronic exposure to low oxygen levels by remodeling of their lung arteries, contrary to wild-type mice, and as a consequence, do not develop increased right ventricular systolic pressure in response to chronic hypoxia. Adult mutant female mice display reduced bone density that worsens with age. Osteopenia is due to reduced proliferation and delayed differentiation of osteoblasts and reduced calcium incorporation by osteoblasts. In addition, mutant mice display a reduced number of proliferating interstitial cells of Cajal in the myenteric plexus in jejunum muscle, and a reduced number of interstitial cells of Cajal in the deep muscular plexus. Besides, mutant mice show increased locomotor activity in a novel environment, compared to wild-type. Contrary to wild-type, they do not respond to the drug 3,4-methylenedioxymethamphetamine with increased locomotion and increased 5-hydroxytryptamine and dopamine levels in the brain.7 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4794795-hydroxytryptamine receptor 2BPRO_0000068954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi127 ↔ 206PROSITE-ProRule annotation
Disulfide bondi349 ↔ 352PROSITE-ProRule annotation
Lipidationi396 – 3961S-palmitoyl cysteineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiQ02152.

PTM databases

PhosphoSiteiQ02152.

Expressioni

Tissue specificityi

Ubiquitous. Detected in intestine, heart, skeletal muscle, testis, urinary bladder, stomach, liver, lung, brain and kidney. Detected in osteoblasts. Detected in the raphe nucleus in the brain, in dorsal root ganglion neurons, the brain stem, cerebellum and spinal cord. Detected in interstitial cells of Cajal in the small intestine.6 Publications

Gene expression databases

BgeeiQ02152.
CleanExiMM_HTR2B.
ExpressionAtlasiQ02152. differential.
GenevestigatoriQ02152.

Interactioni

Subunit structurei

Interacts with MPDZ.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ02152.
SMRiQ02152. Positions 47-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1396Agonist bindingBy similarity
Regioni336 – 3405Agonist bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi151 – 1533DRY motif; important for ligand-induced conformation changes
Motifi211 – 2144[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family membersBy similarity
Motifi375 – 3795NPxxY motif; important for ligand-induced conformation changes and signaling
Motifi477 – 4793PDZ-binding

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG247243.
GeneTreeiENSGT00770000120457.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiQ02152.
KOiK04157.
OMAiCDSCNQT.
OrthoDBiEOG70ZZN5.
TreeFamiTF316350.

Family and domain databases

Gene3Di1.20.1070.10. 2 hits.
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.

Q02152-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSYKMSEQ STTSEHILQK TCDHLILTNR SGLETDSVAE EMKQTVEGQG
60 70 80 90 100
HTVHWAALLI LAVIIPTIGG NILVILAVAL EKRLQYATNY FLMSLAIADL
110 120 130 140 150
LVGLFVMPIA LLTIMFEAIW PLPLALCPAW LFLDVLFSTA SIMHLCAISL
160 170 180 190 200
DRYIAIKKPI QANQCNSRAT AFIKITVVWL ISIGIAIPVP IKGIETDVIN
210 220 230 240 250
PHNVTCELTK DRFGSFMVFG SLAAFFAPLT IMVVTYFLTI HTLQKKAYLV
260 270 280 290 300
KNKPPQRLTR WTVPTVFLRE DSSFSSPEKV AMLDGSHRDK ILPNSSDETL
310 320 330 340 350
MRRMSSVGKR SAQTISNEQR ASKALGVVFF LFLLMWCPFF ITNLTLALCD
360 370 380 390 400
SCNQTTLKTL LEIFVWIGYV SSGVNPLIYT LFNKTFREAF GRYITCNYRA
410 420 430 440 450
TKSVKALRKF SSTLCFGNSM VENSKFFTKH GIRNGINPAM YQSPMRLRSS
460 470
TIQSSSIILL DTLLTENDGD KAEEQVSYI
Length:479
Mass (Da):53,597
Last modified:October 16, 2013 - v3
Checksum:iF02B30D80C8C9B6D
GO

Sequence cautioni

The sequence CAA78824.1 differs from that shown. Reason: Erroneous termination at position 480. Translated as stop.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671S → T in CAA78824. (PubMed:1426253)Curated
Sequence conflicti227 – 2271A → V in CAA78824. (PubMed:1426253)Curated
Sequence conflicti227 – 2271A → V in CAA10051. 1 PublicationCurated
Sequence conflicti449 – 4491S → C in CAA78824. (PubMed:1426253)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15119 mRNA. Translation: CAA78824.1. Sequence problems.
AJ012488 Genomic DNA. Translation: CAA10051.1.
AF498254 mRNA. Translation: AAM22971.1.
AF498255 mRNA. Translation: AAM22972.1.
AK033713 mRNA. Translation: BAC28441.1.
BC023690 mRNA. Translation: AAH23690.1.
CCDSiCCDS35644.1.
PIRiS27269.
RefSeqiNP_032337.2. NM_008311.2.
XP_006529210.1. XM_006529147.1.
UniGeneiMm.439747.

Genome annotation databases

EnsembliENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
GeneIDi15559.
KEGGimmu:15559.
UCSCiuc007buz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15119 mRNA. Translation: CAA78824.1 . Sequence problems.
AJ012488 Genomic DNA. Translation: CAA10051.1 .
AF498254 mRNA. Translation: AAM22971.1 .
AF498255 mRNA. Translation: AAM22972.1 .
AK033713 mRNA. Translation: BAC28441.1 .
BC023690 mRNA. Translation: AAH23690.1 .
CCDSi CCDS35644.1.
PIRi S27269.
RefSeqi NP_032337.2. NM_008311.2.
XP_006529210.1. XM_006529147.1.
UniGenei Mm.439747.

3D structure databases

ProteinModelPortali Q02152.
SMRi Q02152. Positions 47-399.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2096671.
GuidetoPHARMACOLOGYi 7.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei Q02152.

Proteomic databases

PRIDEi Q02152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027431 ; ENSMUSP00000027431 ; ENSMUSG00000026228 .
GeneIDi 15559.
KEGGi mmu:15559.
UCSCi uc007buz.1. mouse.

Organism-specific databases

CTDi 3357.
MGIi MGI:109323. Htr2b.

Phylogenomic databases

eggNOGi NOG247243.
GeneTreei ENSGT00770000120457.
HOGENOMi HOG000240378.
HOVERGENi HBG107487.
InParanoidi Q02152.
KOi K04157.
OMAi CDSCNQT.
OrthoDBi EOG70ZZN5.
TreeFami TF316350.

Enzyme and pathway databases

Reactomei REACT_207651. G alpha (q) signalling events.
REACT_232980. Serotonin receptors.

Miscellaneous databases

NextBioi 288504.
PROi Q02152.
SOURCEi Search...

Gene expression databases

Bgeei Q02152.
CleanExi MM_HTR2B.
ExpressionAtlasi Q02152. differential.
Genevestigatori Q02152.

Family and domain databases

Gene3Di 1.20.1070.10. 2 hits.
InterProi IPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24247:SF31. PTHR24247:SF31. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "New mouse 5-HT2-like receptor. Expression in brain, heart and intestine."
    Loric S., Launay J.-M., Colas J.-F., Maroteaux L.
    FEBS Lett. 312:203-207(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Genomic sequence of the 5-HT2B receptor locus."
    Choi D.S., Maroteaux L.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ILS and ISS.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cecum.
  5. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  7. "Ablation of serotonin 5-HT(2B) receptors in mice leads to abnormal cardiac structure and function."
    Nebigil C.G., Hickel P., Messaddeq N., Vonesch J.L., Douchet M.P., Monassier L., Gyorgy K., Matz R., Andriantsitohaina R., Manivet P., Launay J.M., Maroteaux L.
    Circulation 103:2973-2979(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "Function of the serotonin 5-hydroxytryptamine 2B receptor in pulmonary hypertension."
    Launay J.M., Herve P., Peoc'h K., Tournois C., Callebert J., Nebigil C.G., Etienne N., Drouet L., Humbert M., Simonneau G., Maroteaux L.
    Nat. Med. 8:1129-1135(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Serotonin is a novel survival factor of cardiomyocytes: mitochondria as a target of 5-HT2B receptor signaling."
    Nebigil C.G., Etienne N., Messaddeq N., Maroteaux L.
    FASEB J. 17:1373-1375(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  10. "Serotonin transport and serotonin transporter-mediated antidepressant recognition are controlled by 5-HT2B receptor signaling in serotonergic neuronal cells."
    Launay J.M., Schneider B., Loric S., Da Prada M., Kellermann O.
    FASEB J. 20:1843-1854(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The serotonin 5-HT2B receptor controls bone mass via osteoblast recruitment and proliferation."
    Collet C., Schiltz C., Geoffroy V., Maroteaux L., Launay J.M., de Vernejoul M.C.
    FASEB J. 22:418-427(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  12. "Serotonin 5-HT2B receptors are required for 3,4-methylenedioxymethamphetamine-induced hyperlocomotion and 5-HT release in vivo and in vitro."
    Doly S., Valjent E., Setola V., Callebert J., Herve D., Launay J.M., Maroteaux L.
    J. Neurosci. 28:2933-2940(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. Cited for: INVOLVEMENT IN IMPULSIVE BEHAVIOR.
  14. "Lack of serotonin 5-HT2B receptor alters proliferation and network volume of interstitial cells of Cajal in vivo."
    Tharayil V.S., Wouters M.M., Stanich J.E., Roeder J.L., Lei S., Beyder A., Gomez-Pinilla P.J., Gershon M.D., Maroteaux L., Gibbons S.J., Farrugia G.
    Neurogastroenterol. Motil. 22:462-469(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
  15. "Serotonin receptor 5-HT2B mediates serotonin-induced mechanical hyperalgesia."
    Lin S.Y., Chang W.J., Lin C.S., Huang C.Y., Wang H.F., Sun W.H.
    J. Neurosci. 31:1410-1418(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, POSSIBLE FUNCTION IN PAIN PERCEPTION.
  16. "5HT(2A) and 5HT(2B) receptors contribute to serotonin-induced vascular dysfunction in diabetes."
    Nelson P.M., Harrod J.S., Lamping K.G.
    Exp. Diabetes Res. 2012:398406-398406(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry namei5HT2B_MOUSE
AccessioniPrimary (citable) accession number: Q02152
Secondary accession number(s): Q8JZK5, Q9QWS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 16, 2013
Last modified: November 26, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3