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Reviewed, UniProtKB/Swiss-Prot P35367 (HRH1_HUMAN)

Last modified March 2, 2010. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Histamine H1 receptor

Short name=HH1R
Short name=H1R
Gene names
Name:HRH1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Potential sites of phosphorylation in the third cytoplasmic loop may play an important role in regulating signal transduction through the receptor molecule.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Histamine H1 receptor
PRO_0000069676

Regions

Topological domain1 – 2929Extracellular Potential
Transmembrane30 – 49201 Potential
Topological domain50 – 6314Cytoplasmic Potential
Transmembrane64 – 83202 Potential
Topological domain84 – 10118Extracellular Potential
Transmembrane102 – 123223 Potential
Topological domain124 – 14522Cytoplasmic Potential
Transmembrane146 – 165204 Potential
Topological domain166 – 18924Extracellular Potential
Transmembrane190 – 210215 Potential
Topological domain211 – 418208Cytoplasmic Potential
Transmembrane419 – 438206 Potential
Topological domain439 – 45012Extracellular Potential
Transmembrane451 – 470207 Potential
Topological domain471 – 48717Cytoplasmic Potential

Amino acid modifications

Modified residue2551Phosphoserine Ref.10
Modified residue2751Phosphoserine Ref.10 Ref.11
Modified residue2791Phosphothreonine Ref.11
Lipidation4451S-palmitoyl cysteine Potential
Glycosylation51N-linked (GlcNAc...) Potential
Glycosylation181N-linked (GlcNAc...) Potential
Disulfide bond100 ↔ 180 By similarity

Natural variations

Natural variant191K → N: dbSNP rs2067466.
VAR_049410
Natural variant2701G → E: dbSNP rs7651620.
VAR_033476
Natural variant3851D → E in a colorectal cancer sample; somatic mutation. Ref.12
VAR_035761

Experimental info

Sequence conflict3081V → E in AAH60802. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P35367-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: E5DB418A4C17A985

FASTA48755,784
        10         20         30         40         50         60 
MSLPNSSCLL EDKMCEGNKT TMASPQLMPL VVVLSTICLV TVGLNLLVLY AVRSERKLHT 

        70         80         90        100        110        120 
VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC LFWLSMDYVA STASIFSVFI 

       130        140        150        160        170        180 
LCIDRYRSVQ QPLRYLKYRT KTRASATILG AWFLSFLWVI PILGWNHFMQ QTSVRREDKC 

       190        200        210        220        230        240 
ETDFYDVTWF KVMTAIINFY LPTLLMLWFY AKIYKAVRQH CQHRELINRS LPSFSEIKLR 

       250        260        270        280        290        300 
PENPKGDAKK PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDREVDKL 

       310        320        330        340        350        360 
YCFPLDIVHM QAAAEGSSRD YVAVNRSHGQ LKTDEQGLNT HGASEISEDQ MLGDSQSFSR 

       370        380        390        400        410        420 
TDSDTTTETA PGKGKLRSGS NTGLDYIKFT WKRLRSHSRQ YVSGLHMNRE RKAAKQLGFI 

       430        440        450        460        470        480 
MAAFILCWIP YFIFFMVIAF CKNCCNEHLH MFTIWLGYIN STLNPLIYPL CNENFKKTFK 


RILHIRS 

« Hide

References

« Hide 'large scale' references
[1]"Genomic cloning, heterologous expression and pharmacological characterization of a human histamine H1 receptor."
de Backer M.D., Gommeren W., Moereels H., Nobels G., van Gompel P., Leysen J.E., Luyten W.H.M.L.
Biochem. Biophys. Res. Commun. 197:1601-1608(1993) [PubMed: 8280179] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of the human histamine H1 receptor gene."
Fukui K., Fujimoto K., Mizuguchi H., Sakamoto K., Horio Y., Takai S., Yamada K., Ito S.
Biochem. Biophys. Res. Commun. 201:894-901(1994) [PubMed: 8003029] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Stable expression of human H1-histamine-receptor cDNA in Chinese hamster ovary cells. Pharmacological characterisation of the protein, tissue distribution of messenger RNA and chromosomal localisation of the gene."
Moguilevsky N., Varsalona F., Noyer M., Gillard M., Guillaume J.P., Garcia L., Szpirer C., Szpirer J., Bollen A.
Eur. J. Biochem. 224:489-495(1994) [PubMed: 7925364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Rae J.L., Shepard A.R.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens epithelium.
[5]"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: 15014171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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 (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-275, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND THR-279, MASS SPECTROMETRY.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-385.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34897 mRNA. Translation: CAA84380.1.
X76786 Genomic DNA. Translation: CAA54182.1.
D14436 Genomic DNA. Translation: BAA03319.1.
D28481 mRNA. Translation: BAA05840.1.
AF026261 mRNA. Translation: AAB95156.1.
AB041380 Genomic DNA. Translation: BAA94465.1.
AY136743 mRNA. Translation: AAN01269.1.
AK289412 mRNA. Translation: BAF82101.1.
CH471055 Genomic DNA. Translation: EAW64092.1.
BC060802 mRNA. Translation: AAH60802.1.
IPIIPI00018147.
PIRJC2495.
RefSeqNP_000852.1.
NP_001091681.1.
NP_001091682.1.
NP_001091683.1.
UniGeneHs.1570

3D structure databases

SMRP35367. Positions 27-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGP35367.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35367.

Proteomic databases

PRIDEP35367.

Genome annotation databases

EnsemblENST00000355172; ENSP00000347299; ENSG00000196639; Homo sapiens. [Genome view]
ENST00000397056; ENSP00000380247; ENSG00000196639; Homo sapiens. [Genome view]
ENST00000431010; ENSP00000397028; ENSG00000196639; Homo sapiens. [Genome view]
ENST00000438284; ENSP00000406705; ENSG00000196639; Homo sapiens. [Genome view]
GeneID3269.
KEGGhsa:3269.
UCSCuc003bwb.2. human.

Organism-specific databases

CTD3269.
GeneCardsGC03P011223.
H-InvDBHIX0030701.
HGNCHGNC:5182. HRH1.
MIM600167. gene.
PharmGKBPA29456.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13104.
HOGENOMHBG447339.
HOVERGENHBG101103.
InParanoidP35367.
OMALHMFTIW.
OrthoDBEOG9M94B3.
PhylomeDBP35367.

Enzyme and pathway databases

ReactomeREACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpressP35367.
BgeeP35367.
CleanExHS_HRH1.
GenevestigatorP35367.
GermOnlineENSG00000196639. Homo sapiens.

Family and domain databases

InterProIPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
IPR000921. Histamine_H1_recept.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00530. HISTAMINEH1R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP35367.
DrugBankDB01615. Aceprometazine.
DB00637. Astemizole.
DB00719. Azatadine.
DB00972. Azelastine.
DB00767. Benzquinamide.
DB04890. Bepotastine.
DB01237. Bromodiphenhydramine.
DB00835. Brompheniramine.
DB00354. Buclizine.
DB00748. Carbinoxamine.
DB00341. Cetirizine.
DB04837. Chlophedianol.
DB01114. Chlorpheniramine.
DB01239. Chlorprothixene.
DB00568. Cinnarizine.
DB00283. Clemastine.
DB00363. Clozapine.
DB01176. Cyclizine.
DB00434. Cyproheptadine.
DB01151. Desipramine.
DB00967. Desloratadine.
DB00405. Dexbrompheniramine.
DB00985. Dimenhydrinate.
DB01075. Diphenhydramine.
DB01146. Diphenylpyraline.
DB01142. Doxepin.
DB00366. Doxylamine.
DB01084. Emedastine.
DB00751. Epinastine.
DB00950. Fexofenadine.
DB04841. Flunarizine.
DB00667. Histamine Phosphate.
DB00557. Hydroxyzine.
DB00920. Ketotifen.
DB01106. Levocabastine.
DB00455. Loratadine.
DB00934. Maprotiline.
DB00737. Meclizine.
DB01071. Mequitazine.
DB00902. Methdilazine.
DB01403. Methotrimeprazine.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB00716. Nedocromil.
DB00334. Olanzapine.
DB00768. Olopatadine.
DB01173. Orphenadrine.
DB00885. Pemirolast.
DB01619. Phenindamine.
DB01620. Pheniramine.
DB00433. Prochlorperazine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB00342. Terfenadine.
DB00372. Thiethylperazine.
DB00656. Trazodone.
DB01246. Trimeprazine.
DB00792. Tripelennamine.
DB00427. Triprolidine.
DB00246. Ziprasidone.
NextBio12981.
SOURCESearch...

Entry information

Entry nameHRH1_HUMAN
AccessionPrimary (citable) accession number: P35367
Secondary accession number(s): A8K047, Q6P9E5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 2, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents