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P28222

- 5HT1B_HUMAN

UniProt

P28222 - 5HT1B_HUMAN

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Protein

5-hydroxytryptamine receptor 1B

Gene

HTR1B

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 ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as 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, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei355 – 3551Important for species-specific agonist sensitivity

GO - Molecular functioni

  1. drug binding Source: Ensembl
  2. serotonin binding Source: Ensembl
  3. serotonin receptor activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-inhibiting serotonin receptor signaling pathway Source: UniProtKB
  2. bone remodeling Source: Ensembl
  3. cellular response to alkaloid Source: UniProtKB
  4. cellular response to drug Source: UniProtKB
  5. cellular response to temperature stimulus Source: Ensembl
  6. drinking behavior Source: Ensembl
  7. G-protein coupled receptor internalization Source: Ensembl
  8. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  9. negative regulation of cAMP biosynthetic process Source: UniProtKB
  10. negative regulation of serotonin secretion Source: UniProtKB
  11. negative regulation of synaptic transmission, GABAergic Source: Ensembl
  12. negative regulation of synaptic transmission, glutamatergic Source: Ensembl
  13. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
  14. regulation of behavior Source: InterPro
  15. regulation of dopamine secretion Source: Ensembl
  16. response to cocaine Source: Ensembl
  17. response to ethanol Source: Ensembl
  18. response to mineralocorticoid Source: Ensembl
  19. synaptic transmission Source: ProtInc
  20. vasoconstriction Source: InterPro
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_19231. G alpha (i) signalling events.

Protein family/group databases

TCDBi9.A.14.3.6. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 1B
Short name:
5-HT-1B
Short name:
5-HT1B
Alternative name(s):
S12
Serotonin 1D beta receptor
Short name:
5-HT-1D-beta
Serotonin receptor 1B
Gene namesi
Name:HTR1B
Synonyms:HTR1DB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:5287. HTR1B.

Subcellular locationi

Cell membrane 10 Publications; Multi-pass membrane protein 10 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4949ExtracellularAdd
BLAST
Transmembranei50 – 7526Helical; Name=1Add
BLAST
Topological domaini76 – 849Cytoplasmic
Transmembranei85 – 11026Helical; Name=2Add
BLAST
Topological domaini111 – 12313ExtracellularAdd
BLAST
Transmembranei124 – 14522Helical; Name=3Add
BLAST
Topological domaini146 – 16520CytoplasmicAdd
BLAST
Transmembranei166 – 18722Helical; Name=4Add
BLAST
Topological domaini188 – 20518ExtracellularAdd
BLAST
Transmembranei206 – 22823Helical; Name=5Add
BLAST
Topological domaini229 – 31587CytoplasmicAdd
BLAST
Transmembranei316 – 33621Helical; Name=6Add
BLAST
Topological domaini337 – 34913ExtracellularAdd
BLAST
Transmembranei350 – 37122Helical; Name=7Add
BLAST
Topological domaini372 – 39019CytoplasmicAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. integral component of plasma membrane Source: UniProtKB
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261L → A: No effect on agonist binding. 1 Publication
Mutagenesisi129 – 1291D → A: Abolishes agonist binding. 1 Publication
Mutagenesisi130 – 1301I → A: Abolishes agonist binding. 1 Publication
Mutagenesisi133 – 1331C → A: Abolishes agonist binding. 1 Publication
Mutagenesisi134 – 1341T → A: Slightly decreases agonist binding. 1 Publication
Mutagenesisi200 – 2001V → A: No effect on agonist binding. 1 Publication
Mutagenesisi201 – 2011V → A: No effect on agonist binding. 1 Publication
Mutagenesisi203 – 2031T → A: No effect on agonist binding. 1 Publication
Mutagenesisi209 – 2091T → A: No effect on agonist binding. 1 Publication
Mutagenesisi212 – 2121S → A: No effect on agonist binding. 1 Publication
Mutagenesisi216 – 2161A → S: No effect on agonist binding. 1 Publication
Mutagenesisi327 – 3271W → A: Abolishes agonist binding. 1 Publication
Mutagenesisi330 – 3301F → A: Abolishes agonist binding. 1 Publication
Mutagenesisi331 – 3311F → A: No effect on agonist binding. 1 Publication
Mutagenesisi334 – 3341S → A: No effect on agonist binding. 1 Publication
Mutagenesisi337 – 3371M → A: No effect on agonist binding. 1 Publication
Mutagenesisi351 – 3511F → A: No effect on agonist binding. 1 Publication
Mutagenesisi352 – 3521D → A: No effect on agonist binding. 1 Publication
Mutagenesisi355 – 3551T → A: No effect on agonist binding. 1 Publication
Mutagenesisi359 – 3591Y → A: No effect on agonist binding. 1 Publication

Organism-specific databases

PharmGKBiPA29549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3903905-hydroxytryptamine receptor 1BPRO_0000068916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi122 ↔ 1991 PublicationPROSITE-ProRule annotation
Lipidationi388 – 3881S-palmitoyl cysteineSequence Analysis

Post-translational modificationi

Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation.1 Publication
Palmitoylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP28222.
PRIDEiP28222.

PTM databases

PhosphoSiteiP28222.

Expressioni

Tissue specificityi

Detected in cerebral artery smooth muscle cells (at protein level). Detected in brain cortex, striatum, amygdala, medulla, hippocampus, caudate nucleus and putamen.3 Publications

Gene expression databases

BgeeiP28222.
CleanExiHS_HTR1B.
ExpressionAtlasiP28222. baseline and differential.
GenevestigatoriP28222.

Organism-specific databases

HPAiHPA049046.

Interactioni

Subunit structurei

Homodimer. Heterodimer with HTR1D.1 Publication

Protein-protein interaction databases

BioGridi109583. 5 interactions.
IntActiP28222. 1 interaction.
STRINGi9606.ENSP00000358963.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 434Combined sources
Helixi46 – 7631Combined sources
Helixi78 – 803Combined sources
Helixi83 – 10119Combined sources
Helixi104 – 1129Combined sources
Helixi118 – 15235Combined sources
Helixi154 – 1585Combined sources
Helixi163 – 18119Combined sources
Helixi206 – 21611Combined sources
Helixi218 – 23922Combined sources
Helixi311 – 33626Combined sources
Helixi349 – 37224Combined sources
Helixi374 – 38310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G1Xmodel-A1-390[»]
4IAQX-ray2.80A33-239[»]
A304-390[»]
4IARX-ray2.70A33-239[»]
A306-390[»]
ProteinModelPortaliP28222.
SMRiP28222. Positions 38-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 13410Agonist binding
Regioni327 – 3315Agonist binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi146 – 1483DRY motif; important for ligand-induced conformation changes and signaling
Motifi365 – 3695NPxxY motif; important for ligand-induced conformation changes and signaling

Domaini

Ligands are bound in a hydrophobic pocket formed by the transmembrane helices.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249628.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP28222.
KOiK04153.
OMAiIALPWKV.
OrthoDBiEOG7NCV3Q.
PhylomeDBiP28222.
TreeFamiTF316350.

Family and domain databases

Gene3Di1.20.1070.10. 2 hits.
InterProiIPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF16. PTHR24247:SF16. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00513. 5HT1BRECEPTR.
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.

P28222-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV
60 70 80 90 100
LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI
110 120 130 140 150
LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA
160 170 180 190 200
ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV
210 220 230 240 250
VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR
260 270 280 290 300
LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE
310 320 330 340 350
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI
360 370 380 390
FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
Length:390
Mass (Da):43,568
Last modified:December 1, 1992 - v1
Checksum:iCD874DC7EB44CF12
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241F → C.1 Publication
Corresponds to variant rs130060 [ dbSNP | Ensembl ].
VAR_011715
Natural varianti219 – 2191F → L.
Corresponds to variant rs130061 [ dbSNP | Ensembl ].
VAR_011831
Natural varianti367 – 3671I → V.
Corresponds to variant rs130063 [ dbSNP | Ensembl ].
VAR_011832
Natural varianti374 – 3741E → K.
Corresponds to variant rs130064 [ dbSNP | Ensembl ].
VAR_011833

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89478 Genomic DNA. No translation available.
D10995 Genomic DNA. Translation: BAA01763.1.
M83180 Genomic DNA. Translation: AAA36029.1.
L09732 Genomic DNA. Translation: AAA36030.1.
M81590 mRNA. Translation: AAA60316.1.
M75128 Genomic DNA. Translation: AAA58675.1.
AB041370 Genomic DNA. Translation: BAA94455.1.
AY225227 Genomic DNA. Translation: AAO67712.1.
AL049595 Genomic DNA. Translation: CAB51537.1.
BC069065 mRNA. Translation: AAH69065.1.
BC096206 mRNA. Translation: AAH96206.1.
BC096207 mRNA. Translation: AAH96207.1.
BC096208 mRNA. Translation: AAH96208.1.
CCDSiCCDS4986.1.
PIRiJN0268.
RefSeqiNP_000854.1. NM_000863.1.
UniGeneiHs.123016.

Genome annotation databases

EnsembliENST00000369947; ENSP00000358963; ENSG00000135312.
GeneIDi3351.
KEGGihsa:3351.
UCSCiuc003pil.1. human.

Polymorphism databases

DMDMi112821.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89478 Genomic DNA. No translation available.
D10995 Genomic DNA. Translation: BAA01763.1 .
M83180 Genomic DNA. Translation: AAA36029.1 .
L09732 Genomic DNA. Translation: AAA36030.1 .
M81590 mRNA. Translation: AAA60316.1 .
M75128 Genomic DNA. Translation: AAA58675.1 .
AB041370 Genomic DNA. Translation: BAA94455.1 .
AY225227 Genomic DNA. Translation: AAO67712.1 .
AL049595 Genomic DNA. Translation: CAB51537.1 .
BC069065 mRNA. Translation: AAH69065.1 .
BC096206 mRNA. Translation: AAH96206.1 .
BC096207 mRNA. Translation: AAH96207.1 .
BC096208 mRNA. Translation: AAH96208.1 .
CCDSi CCDS4986.1.
PIRi JN0268.
RefSeqi NP_000854.1. NM_000863.1.
UniGenei Hs.123016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G1X model - A 1-390 [» ]
4IAQ X-ray 2.80 A 33-239 [» ]
A 304-390 [» ]
4IAR X-ray 2.70 A 33-239 [» ]
A 306-390 [» ]
ProteinModelPortali P28222.
SMRi P28222. Positions 38-387.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109583. 5 interactions.
IntActi P28222. 1 interaction.
STRINGi 9606.ENSP00000358963.

Chemistry

BindingDBi P28222.
ChEMBLi CHEMBL2095230.
DrugBanki DB00918. Almotriptan.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB00714. Apomorphine.
DB01238. Aripiprazole.
DB06216. Asenapine.
DB08807. Bopindolol.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB00363. Clozapine.
DB00320. Dihydroergotamine.
DB00216. Eletriptan.
DB01049. Ergoloid mesylate.
DB00696. Ergotamine.
DB00998. Frovatriptan.
DB01221. Ketamine.
DB00589. Lisuride.
DB00408. Loxapine.
DB00247. Methysergide.
DB00952. Naratriptan.
DB00334. Olanzapine.
DB00904. Ondansetron.
DB01359. Penbutolol.
DB01186. Pergolide.
DB00960. Pindolol.
DB00413. Pramipexole.
DB00571. Propranolol.
DB01224. Quetiapine.
DB00953. Rizatriptan.
DB00268. Ropinirole.
DB00669. Sumatriptan.
DB01392. Yohimbine.
DB00246. Ziprasidone.
DB00315. Zolmitriptan.
GuidetoPHARMACOLOGYi 2.

Protein family/group databases

TCDBi 9.A.14.3.6. the g-protein-coupled receptor (gpcr) family.
GPCRDBi Search...

PTM databases

PhosphoSitei P28222.

Polymorphism databases

DMDMi 112821.

Proteomic databases

PaxDbi P28222.
PRIDEi P28222.

Protocols and materials databases

DNASUi 3351.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369947 ; ENSP00000358963 ; ENSG00000135312 .
GeneIDi 3351.
KEGGi hsa:3351.
UCSCi uc003pil.1. human.

Organism-specific databases

CTDi 3351.
GeneCardsi GC06M078171.
HGNCi HGNC:5287. HTR1B.
HPAi HPA049046.
MIMi 182131. gene.
neXtProti NX_P28222.
PharmGKBi PA29549.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249628.
HOGENOMi HOG000239242.
HOVERGENi HBG106962.
InParanoidi P28222.
KOi K04153.
OMAi IALPWKV.
OrthoDBi EOG7NCV3Q.
PhylomeDBi P28222.
TreeFami TF316350.

Enzyme and pathway databases

Reactomei REACT_17064. Serotonin receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikii 5-HT1B_receptor.
GenomeRNAii 3351.
NextBioi 13252.
PROi P28222.
SOURCEi Search...

Gene expression databases

Bgeei P28222.
CleanExi HS_HTR1B.
ExpressionAtlasi P28222. baseline and differential.
Genevestigatori P28222.

Family and domain databases

Gene3Di 1.20.1070.10. 2 hits.
InterProi IPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24247:SF16. PTHR24247:SF16. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00513. 5HT1BRECEPTR.
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. "Molecular cloning and functional characterization of a human 5-HT1B serotonin receptor: a homologue of the rat 5-HT1B receptor with 5-HT1D-like pharmacological specificity."
    Hamblin M.W., Metcalf M.A., McGuffin R.W., Karpells S.
    Biochem. Biophys. Res. Commun. 184:752-759(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Cloning and expression of the human 5-HT1B-type receptor gene."
    Mochizuki D., Yuyama Y., Tsujita R., Komaki H., Sagai H.
    Biochem. Biophys. Res. Commun. 185:517-523(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  3. "Characterization of the human 5-hydroxytryptamine1B receptor."
    Jin H., Oksenberg D., Ashkenazi A., Peroutka S.J., Duncan A.M.V., Rozmahel R., Yang Y., Mengod G., Palacios J.M., O'Dowd B.F.
    J. Biol. Chem. 267:5735-5738(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Molecular cloning of a human serotonin receptor (S12) with a pharmacological profile resembling that of the 5-HT1D subtype."
    Levy F.O., Gudermann T., Perez-Reyes E., Birnbaumer M., Kaumann A.J., Birnbaumer L.
    J. Biol. Chem. 267:7553-7562(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  5. "Human serotonin 1D receptor is encoded by a subfamily of two distinct genes: 5-HT1D alpha and 5-HT1D beta."
    Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., Hartig P.R.
    Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Placenta.
  6. "A human serotonin 1D receptor variant (5HT1D beta) encoded by an intronless gene on chromosome 6."
    Demchyshyn L., Sunahara R.K., Miller K., Teitler M., Hoffman B.J., Kennedy J.L., Seeman P., van Tol H.H.M., Niznik H.B.
    Proc. Natl. Acad. Sci. U.S.A. 89:5522-5526(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Cloning and pharmacological characterization of a novel human 5-hydroxytryptamine1D receptor subtype."
    Veldman S.A., Bienkowski M.J.
    Mol. Pharmacol. 42:439-444(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  8. "Human-specific amino acid changes found in 103 protein-coding genes."
    Kitano T., Liu Y.-H., Ueda S., Saitou N.
    Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Isolation of complete coding sequence for 5-hydroxytryptamine (serotonin) receptor 1B (HTR1B)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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].
  12. "Human serotonin1B receptor expression in Sf9 cells: phosphorylation, palmitoylation, and adenylyl cyclase inhibition."
    Ng G.Y.K., George S.R., Zastawny R.L., Caron M., Bouvier M., Dennis M., O'Dowd B.F.
    Biochemistry 32:11727-11733(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION, PHOSPHORYLATION, FUNCTION.
  13. "Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone and heterodimers when co-expressed."
    Xie Z., Lee S.P., O'Dowd B.F., George S.R.
    FEBS Lett. 456:63-67(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  14. "Triptan-induced contractile (5-HT1B receptor) responses in human cerebral and coronary arteries: relationship to clinical effect."
    Edvinsson L., Uddman E., Wackenfors A., Davenport A., Longmore J., Malmsjo M.
    Clin. Sci. 109:335-342(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  15. Cited for: REVIEW.
  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.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-390 IN COMPLEXES WITH ERGOTAMINE AND DIHYDROERGOTAMINE, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DOMAIN, DISULFIDE BOND, MUTAGENESIS OF LEU-126; ASP-129; ILE-130; CYS-133; THR-134; VAL-200; VAL-201; THR-203; THR-209; SER-212; ALA-216; TRP-327; PHE-330; PHE-331; SER-334; MET-337; PHE-351; ASP-352; THR-355 AND TYR-359.
  19. "Identification of genetic variation in the human serotonin 1D beta receptor gene."
    Nothen M.M., Erdmann J., Shimron-Abarbanell D., Propping P.
    Biochem. Biophys. Res. Commun. 205:1194-1200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CYS-124.

Entry informationi

Entry namei5HT1B_HUMAN
AccessioniPrimary (citable) accession number: P28222
Secondary accession number(s): Q4VAY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 141 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

Miscellaneous

A residue in the 7th transmembrane region (Thr-355 in human, 'Asn-351' in mouse and rat) is important for species-specific sensitivity to various agonists.

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 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3