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P28335

- 5HT2C_HUMAN

UniProt

P28335 - 5HT2C_HUMAN

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Protein

5-hydroxytryptamine receptor 2C

Gene

HTR2C

Organism
Homo sapiens (Human)
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 drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). 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. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis.4 Publications

GO - Molecular functioni

  1. 1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding Source: UniProtKB
  2. drug binding Source: UniProtKB
  3. Gq/11-coupled serotonin receptor activity Source: UniProtKB
  4. serotonin binding Source: UniProtKB
  5. serotonin receptor activity Source: MGI

GO - Biological processi

  1. behavioral fear response Source: UniProtKB
  2. cellular calcium ion homeostasis Source: UniProtKB
  3. cGMP biosynthetic process Source: UniProtKB
  4. feeding behavior Source: UniProtKB
  5. locomotory behavior Source: InterPro
  6. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  7. phospholipase C-activating serotonin receptor signaling pathway Source: UniProtKB
  8. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
  9. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  10. positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  11. regulation of appetite Source: UniProtKB
  12. regulation of corticotropin-releasing hormone secretion Source: UniProtKB
  13. regulation of neurological system process Source: UniProtKB
  14. release of sequestered calcium ion into cytosol Source: UniProtKB
  15. response to drug Source: UniProtKB
  16. serotonin receptor signaling pathway Source: UniProtKB
  17. synaptic transmission Source: ProtInc
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.
SignaLinkiP28335.

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 2C
Short name:
5-HT-2C
Short name:
5-HT2C
Short name:
5-HTR2C
Alternative name(s):
5-hydroxytryptamine receptor 1C
Short name:
5-HT-1C
Short name:
5-HT1C
Serotonin receptor 2C
Gene namesi
Name:HTR2C
Synonyms:HTR1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:5295. HTR2C.

Subcellular locationi

Cell membrane 4 Publications; Multi-pass membrane protein 4 Publications

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
  2. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591P → A: Decreases interaction with ARRB2. 1 Publication
Mutagenesisi456 – 4561S → A: Loss of interaction with MPDZ. 1 Publication
Mutagenesisi456 – 4561S → T: No effect on interaction with MPDZ. 1 Publication
Mutagenesisi457 – 4571S → A: No effect on interaction with MPDZ. 1 Publication
Mutagenesisi458 – 4581V → A: Loss of interaction with MPDZ. 1 Publication

Organism-specific databases

PharmGKBiPA194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 4584265-hydroxytryptamine receptor 2CPRO_0000068958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)1 Publication
Disulfide bondi127 ↔ 207PROSITE-ProRule annotation
Disulfide bondi337 ↔ 341PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP28335.
PRIDEiP28335.

PTM databases

PhosphoSiteiP28335.

Expressioni

Tissue specificityi

Detected in brain.1 Publication

Gene expression databases

BgeeiP28335.
CleanExiHS_HTR2C.
ExpressionAtlasiP28335. baseline and differential.
GenevestigatoriP28335.

Organism-specific databases

HPAiCAB006857.
HPA003133.

Interactioni

Subunit structurei

Interacts with MPDZ. Interacts with ARRB2.2 Publications

Protein-protein interaction databases

BioGridi109590. 7 interactions.
IntActiP28335. 1 interaction.
MINTiMINT-443944.
STRINGi9606.ENSP00000276198.

Structurei

3D structure databases

ProteinModelPortaliP28335.
SMRiP28335. Positions 54-388.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 5220ExtracellularBy similarityAdd
BLAST
Topological domaini79 – 8911CytoplasmicBy similarityAdd
BLAST
Topological domaini111 – 12717ExtracellularBy similarityAdd
BLAST
Topological domaini151 – 17020CytoplasmicBy similarityAdd
BLAST
Topological domaini194 – 21320ExtracellularBy similarityAdd
BLAST
Topological domaini236 – 31176CytoplasmicBy similarityAdd
BLAST
Topological domaini334 – 34815ExtracellularBy similarityAdd
BLAST
Topological domaini372 – 45887CytoplasmicBy similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei53 – 7826Helical; Name=1By similarityAdd
BLAST
Transmembranei90 – 11021Helical; Name=2By similarityAdd
BLAST
Transmembranei128 – 15023Helical; Name=3By similarityAdd
BLAST
Transmembranei171 – 19323Helical; Name=4By similarityAdd
BLAST
Transmembranei214 – 23522Helical; Name=5By similarityAdd
BLAST
Transmembranei312 – 33322Helical; Name=6By similarityAdd
BLAST
Transmembranei349 – 37123Helical; Name=7By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1396Agonist bindingBy similarity
Regioni324 – 3285Agonist bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi151 – 1533DRY motif; important for ligand-induced conformation changesBy similarity
Motifi364 – 3685NPxxY motif; important for ligand-induced conformation changes and signalingBy similarity
Motifi456 – 4583PDZ-binding

Domaini

The PDZ domain-binding motif is involved in the interaction with MPDZ.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG247243.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiP28335.
KOiK04157.
OMAiCCKRNTD.
OrthoDBiEOG70ZZN5.
PhylomeDBiP28335.
TreeFamiTF316350.

Family and domain databases

Gene3Di1.20.1070.10. 2 hits.
InterProiIPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF32. PTHR24247:SF32. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00517. 5HT2CRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28335-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD
60 70 80 90 100
GVQNWPALSI VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM
110 120 130 140 150
LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL
160 170 180 190 200
DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV
210 220 230 240 250
FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH
260 270 280 290 300
GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM
310 320 330 340 350
QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL
360 370 380 390 400
NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR
410 420 430 440 450
VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV

VSERISSV
Length:458
Mass (Da):51,821
Last modified:December 1, 1992 - v1
Checksum:i9E76B3FFD3E09C93
GO
Isoform 2 (identifier: P28335-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-458: YVAIRNPIEH...SVVSERISSV → CISSYPCDWT...YGRGRELCKP

Show »
Length:248
Mass (Da):28,055
Checksum:i8A8C81B80DA6B59E
GO

RNA editingi

Partially edited. RNA editing generates receptor isoforms that differ in their ability to interact with the phospholipase C signaling cascade in a transfected cell line, suggesting that this RNA processing event may contribute to the modulation of serotonergic neurotransmission in the central nervous system.

Polymorphismi

Position 23 is polymorphic; the frequencies in unrelated Caucasians are 0.87 for Cys and 0.13 for Ser.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231C → S.5 Publications
Corresponds to variant rs6318 [ dbSNP | Ensembl ].
VAR_003450
Natural varianti156 – 1561I → V in RNA edited version.
VAR_010166
Natural varianti158 – 1581N → S in RNA edited version.
VAR_010167
Natural varianti160 – 1601I → V in RNA edited version.
VAR_010168

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 458306YVAIR…RISSV → CISSYPCDWTEGRRKGVREQ HDVRAQRPKFRSYWVLRSFL HTADDYGDYVLPDHLRSAPT SFDVTARPHRGTAWTKSGFP EVLQEEYGRGRELCKP in isoform 2. 1 PublicationVSP_045171Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81778 mRNA. Translation: AAA60317.1.
X80763 Genomic DNA. Translation: CAB59978.1.
U49516 mRNA. Translation: AAB40898.1.
AF208053 mRNA. Translation: AAF35842.1.
AF498983 mRNA. Translation: AAM21130.1.
AK295753 mRNA. Translation: BAG58583.1.
AC007022 Genomic DNA. No translation available.
AC007025 Genomic DNA. No translation available.
AL591402 Genomic DNA. No translation available.
AL355812, AC004822, AL590097 Genomic DNA. Translation: CAI41334.1.
AC004822 Genomic DNA. Translation: AAC71658.1.
AL355812, AL590097, AC004822 Genomic DNA. Translation: CAI41335.1.
AL590097, AC004822, AL355812 Genomic DNA. Translation: CAH70193.1.
BC095543 mRNA. Translation: AAH95543.1.
CCDSiCCDS14564.1. [P28335-1]
CCDS59174.1. [P28335-2]
PIRiJS0616.
RefSeqiNP_000859.1. NM_000868.2. [P28335-1]
NP_001243689.1. NM_001256760.1. [P28335-1]
NP_001243690.1. NM_001256761.1. [P28335-2]
UniGeneiHs.149037.

Genome annotation databases

EnsembliENST00000276198; ENSP00000276198; ENSG00000147246.
ENST00000371950; ENSP00000361018; ENSG00000147246.
ENST00000371951; ENSP00000361019; ENSG00000147246.
GeneIDi3358.
KEGGihsa:3358.
UCSCiuc004epu.1. human. [P28335-1]
uc004epv.1. human.

Polymorphism databases

DMDMi112816.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81778 mRNA. Translation: AAA60317.1 .
X80763 Genomic DNA. Translation: CAB59978.1 .
U49516 mRNA. Translation: AAB40898.1 .
AF208053 mRNA. Translation: AAF35842.1 .
AF498983 mRNA. Translation: AAM21130.1 .
AK295753 mRNA. Translation: BAG58583.1 .
AC007022 Genomic DNA. No translation available.
AC007025 Genomic DNA. No translation available.
AL591402 Genomic DNA. No translation available.
AL355812 , AC004822 , AL590097 Genomic DNA. Translation: CAI41334.1 .
AC004822 Genomic DNA. Translation: AAC71658.1 .
AL355812 , AL590097 , AC004822 Genomic DNA. Translation: CAI41335.1 .
AL590097 , AC004822 , AL355812 Genomic DNA. Translation: CAH70193.1 .
BC095543 mRNA. Translation: AAH95543.1 .
CCDSi CCDS14564.1. [P28335-1 ]
CCDS59174.1. [P28335-2 ]
PIRi JS0616.
RefSeqi NP_000859.1. NM_000868.2. [P28335-1 ]
NP_001243689.1. NM_001256760.1. [P28335-1 ]
NP_001243690.1. NM_001256761.1. [P28335-2 ]
UniGenei Hs.149037.

3D structure databases

ProteinModelPortali P28335.
SMRi P28335. Positions 54-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109590. 7 interactions.
IntActi P28335. 1 interaction.
MINTi MINT-443944.
STRINGi 9606.ENSP00000276198.

Chemistry

BindingDBi P28335.
ChEMBLi CHEMBL2096904.
DrugBanki DB06594. Agomelatine.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB00714. Apomorphine.
DB01238. Aripiprazole.
DB06216. Asenapine.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB01242. Clomipramine.
DB00363. Clozapine.
DB00434. Cyproheptadine.
DB01151. Desipramine.
DB01191. Dexfenfluramine.
DB01142. Doxepin.
DB01049. Ergoloid mesylate.
DB00696. Ergotamine.
DB00458. Imipramine.
DB01221. Ketamine.
DB00589. Lisuride.
DB04871. Lorcaserin.
DB00408. Loxapine.
DB00934. Maprotiline.
DB01403. Methotrimeprazine.
DB00247. Methysergide.
DB06148. Mianserin.
DB00805. Minaprine.
DB00370. Mirtazapine.
DB01149. Nefazodone.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB01267. Paliperidone.
DB01186. Pergolide.
DB00413. Pramipexole.
DB00420. Promazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB00268. Ropinirole.
DB06144. Sertindole.
DB00193. Tramadol.
DB00656. Trazodone.
DB00726. Trimipramine.
DB01392. Yohimbine.
DB00246. Ziprasidone.
GuidetoPHARMACOLOGYi 8.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P28335.

Polymorphism databases

DMDMi 112816.

Proteomic databases

PaxDbi P28335.
PRIDEi P28335.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276198 ; ENSP00000276198 ; ENSG00000147246 .
ENST00000371950 ; ENSP00000361018 ; ENSG00000147246 .
ENST00000371951 ; ENSP00000361019 ; ENSG00000147246 .
GeneIDi 3358.
KEGGi hsa:3358.
UCSCi uc004epu.1. human. [P28335-1 ]
uc004epv.1. human.

Organism-specific databases

CTDi 3358.
GeneCardsi GC0XP113818.
HGNCi HGNC:5295. HTR2C.
HPAi CAB006857.
HPA003133.
MIMi 312861. gene.
neXtProti NX_P28335.
PharmGKBi PA194.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247243.
HOGENOMi HOG000240378.
HOVERGENi HBG107487.
InParanoidi P28335.
KOi K04157.
OMAi CCKRNTD.
OrthoDBi EOG70ZZN5.
PhylomeDBi P28335.
TreeFami TF316350.

Enzyme and pathway databases

Reactomei REACT_17064. Serotonin receptors.
REACT_18283. G alpha (q) signalling events.
SignaLinki P28335.

Miscellaneous databases

GeneWikii 5-HT2C_receptor.
GenomeRNAii 3358.
NextBioi 13278.
PROi P28335.
SOURCEi Search...

Gene expression databases

Bgeei P28335.
CleanExi HS_HTR2C.
ExpressionAtlasi P28335. baseline and differential.
Genevestigatori P28335.

Family and domain databases

Gene3Di 1.20.1070.10. 2 hits.
InterProi IPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24247:SF32. PTHR24247:SF32. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00517. 5HT2CRECEPTR.
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Genomic organisation and functional expression of the gene encoding the human serotonin 5-HT2C receptor."
    Stam N.J., Vanderheyden P., Van Alebeek C., Klomp J., De Boer T., Van Delft A.M.L., Olijve W.
    Eur. J. Pharmacol. 269:339-348(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Hippocampus and Placenta.
  3. "The human serotonin 5-HT2C receptor: complete cDNA, genomic structure, and alternatively spliced variant."
    Xie E., Zhao L., Levine A.J., Shenk T., Chang L.-S.
    Genomics 35:551-561(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "Identification and characterization of RNA editing events within the 5-HT2C receptor."
    Niswender C.M., Sanders-Bush E., Emeson R.B.
    Ann. N. Y. Acad. Sci. 861:38-48(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA EDITING OF POSITIONS 156; 158 AND 160.
    Tissue: Brain.
  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 (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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] (ISOFORM 2).
    Tissue: Hippocampus.
  7. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    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).
  9. "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, DOMAIN, MUTAGENESIS OF SER-456; SER-457 AND VAL-458, GLYCOSYLATION.
  10. "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.
  11. "A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors."
    Marion S., Oakley R.H., Kim K.-M., Caron M.G., Barak L.S.
    J. Biol. Chem. 281:2932-2938(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2, MUTAGENESIS OF PRO-159.
  12. Cited for: REVIEW.
  13. "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, SUBCELLULAR LOCATION.
  14. "Pharmacological characterization of mitogen-activated protein kinase activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B receptors."
    Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.
    Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "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.
  16. "The N-terminal region of the human 5-HT(2)C receptor has as a cleavable signal peptide."
    Jahnsen J.A., Uhlen S.
    Eur. J. Pharmacol. 684:44-50(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, VARIANT SER-23.
  17. "Identification, expression, and pharmacology of a Cys23-Ser23 substitution in the human 5-HT2c receptor gene (HTR2C)."
    Lappalainen J., Zhang L., Dean M., Oz M., Ozaki N., Yu D., Virkkunen M., Weight F., Linnoila M., Goldman D.
    Genomics 27:274-279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-23.
  18. "Association analysis between a Cys23Ser substitution polymorphism of the human 5-HT2c receptor gene and neuronal hyperexcitability."
    Samochowiec J., Smolka M., Winterer G., Rommelspacher H., Schmidt L.G., Sander T.
    Am. J. Med. Genet. 88:126-130(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-23.
  19. "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: VARIANT SER-23.
  20. Cited for: VARIANT SER-23.

Entry informationi

Entry namei5HT2C_HUMAN
AccessioniPrimary (citable) accession number: P28335
Secondary accession number(s): B1AMW4, Q5VUF8, Q9NP28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 155 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

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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