P28222 (5HT1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HTR1B
Synonyms:	HTR1DB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Phosphorylated. Desensitization of the receptor may be mediated by its phosphorylation. Ref.12 Palmitoylated. Ref.12
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor internalization Inferred from electronic annotation. Source: Compara G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Traceable author statement Ref.4. Source: ProtInc bone remodeling Inferred from electronic annotation. Source: Compara cellular response to temperature stimulus Inferred from electronic annotation. Source: Compara drinking behavior Inferred from electronic annotation. Source: Compara negative regulation of cAMP biosynthetic process Inferred from direct assay PubMed 8882600. Source: UniProtKB negative regulation of synaptic transmission, GABAergic Inferred from electronic annotation. Source: Compara negative regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara protein kinase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of dopamine secretion Inferred from electronic annotation. Source: Compara response to cocaine Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to mineralocorticoid stimulus Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement Ref.6. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.4. Source: ProtInc
Molecular_function	drug binding Inferred from electronic annotation. Source: Compara serotonin binding Inferred from electronic annotation. Source: Compara serotonin receptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	5-hydroxytryptamine receptor 1B		PRO_0000068916
Regions
	Topological domain	1 – 49	49	Extracellular By similarity
	Transmembrane	50 – 73	24	Helical; Name=1; By similarity
	Topological domain	74 – 86	13	Cytoplasmic By similarity
	Transmembrane	87 – 109	23	Helical; Name=2; By similarity
	Topological domain	110 – 119	10	Extracellular By similarity
	Transmembrane	120 – 145	26	Helical; Name=3; By similarity
	Topological domain	146 – 165	20	Cytoplasmic By similarity
	Transmembrane	166 – 187	22	Helical; Name=4; By similarity
	Topological domain	188 – 205	18	Extracellular By similarity
	Transmembrane	206 – 229	24	Helical; Name=5; By similarity
	Topological domain	230 – 315	86	Cytoplasmic By similarity
	Transmembrane	316 – 340	25	Helical; Name=6; By similarity
	Topological domain	341 – 347	7	Extracellular By similarity
	Transmembrane	348 – 373	26	Helical; Name=7; By similarity
	Topological domain	374 – 390	17	Cytoplasmic By similarity
Amino acid modifications
	Lipidation	388	1	S-palmitoyl cysteine Potential
	Glycosylation	24	1	N-linked (GlcNAc...) Potential
	Glycosylation	32	1	N-linked (GlcNAc...) Potential
	Disulfide bond	122 ↔ 199		By similarity
Natural variations
	Natural variant	124	1	F → C. Ref.13 Corresponds to variant rs130060 [ dbSNP | Ensembl ].		VAR_011715
	Natural variant	219	1	F → L. Corresponds to variant rs130061 [ dbSNP | Ensembl ].		VAR_011831
	Natural variant	367	1	I → V. Corresponds to variant rs130063 [ dbSNP | Ensembl ].		VAR_011832
	Natural variant	374	1	E → K. Corresponds to variant rs130064 [ dbSNP | Ensembl ].		VAR_011833

Sequences

	Sequence		Length	Mass (Da)
	P28222 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: CD874DC7EB44CF12	FASTA	390	43,568
	10 20 30 40 50 60 MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT 70 80 90 100 110 120 LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV 130 140 150 160 170 180 VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI 190 200 210 220 230 240 SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL 250 260 270 280 290 300 KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE 310 320 330 340 350 360 KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL 370 380 390 NSLINPIIYT MSNEDFKQAF HKLIRFKCTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].
[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].
[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].
[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].
[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]. 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].
[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].
[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.
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00002184.

PIR

JN0268.

RefSeq

NP_000854.1. NM_000863.1.

UniGene

Hs.123016.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G1X	model	-	A	1-390	[»]
4IAQ	X-ray	2.80	A	33-390	[»]
4IAR	X-ray	2.70	A	33-390	[»]

ProteinModelPortal

P28222.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000358963.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P28222.

Polymorphism databases

DMDM

112821.

Proteomic databases

PaxDb

P28222.

PRIDE

P28222.

Protocols and materials databases

DNASU

3351.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369947; ENSP00000358963; ENSG00000135312.

GeneID

3351.

KEGG

hsa:3351.

UCSC

uc003pil.1. human.

Organism-specific databases

CTD

3351.

GeneCards

GC06M078171.

HGNC

HGNC:5287. HTR1B.

HPA

HPA049046.

MIM

182131. gene.

neXtProt

NX_P28222.

PharmGKB

PA29549.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG249628.

HOGENOM

HOG000239242.

HOVERGEN

HBG106962.

InParanoid

P28222.

KO

K04153.

OMA

IALPWKV.

OrthoDB

EOG4R7VB6.

PhylomeDB

P28222.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

Bgee

P28222.

CleanEx

HS_HTR1B.

Genevestigator

P28222.

GermOnline

ENSG00000135312. Homo sapiens.

Family and domain databases

InterPro

IPR002147. 5HT1B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00513. 5HT1BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P28222.

ChEMBL

CHEMBL1898.

DrugBank

DB00918. Almotriptan.
DB01191. Dexfenfluramine.
DB00320. Dihydroergotamine.
DB00216. Eletriptan.
DB00696. Ergotamine.
DB00998. Frovatriptan.
DB00952. Naratriptan.
DB00960. Pindolol.
DB00571. Propranolol.
DB00953. Rizatriptan.
DB00669. Sumatriptan.
DB00285. Venlafaxine.
DB00315. Zolmitriptan.

GenomeRNAi

3351.

NextBio

13252.

SOURCE

Search...

Entry information

Entry name

5HT1B_HUMAN

Accession

Primary (citable) accession number: P28222
Secondary accession number(s): Q4VAY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.