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Protein

Histamine H1 receptor

Gene

HRH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: ProtInc
  2. histamine receptor activity Source: UniProtKB

GO - Biological processi

  1. cellular response to histamine Source: UniProtKB
  2. eosinophil chemotaxis Source: InterPro
  3. G-protein coupled receptor signaling pathway Source: UniProtKB
  4. inflammatory response Source: ProtInc
  5. inositol phosphate-mediated signaling Source: BHF-UCL
  6. memory Source: Ensembl
  7. phospholipase C-activating G-protein coupled receptor signaling pathway Source: ProtInc
  8. positive regulation of inositol trisphosphate biosynthetic process Source: BHF-UCL
  9. positive regulation of vasoconstriction Source: InterPro
  10. regulation of synaptic plasticity Source: Ensembl
  11. regulation of vascular permeability Source: InterPro
  12. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_16903. Histamine receptors.
REACT_18283. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Histamine H1 receptor
Short name:
H1R
Short name:
HH1R
Gene namesi
Name:HRH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:5182. HRH1.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2929Extracellular1 PublicationAdd
BLAST
Transmembranei30 – 5223Helical; Name=1Add
BLAST
Topological domaini53 – 6210Cytoplasmic1 Publication
Transmembranei63 – 8321Helical; Name=2Add
BLAST
Topological domaini84 – 10118Extracellular1 PublicationAdd
BLAST
Transmembranei102 – 12322Helical; Name=3Add
BLAST
Topological domaini124 – 14320Cytoplasmic1 PublicationAdd
BLAST
Transmembranei144 – 16421Helical; Name=4Add
BLAST
Topological domaini165 – 18925Extracellular1 PublicationAdd
BLAST
Transmembranei190 – 21021Helical; Name=5Add
BLAST
Topological domaini211 – 416206Cytoplasmic1 PublicationAdd
BLAST
Transmembranei417 – 43822Helical; Name=6Add
BLAST
Topological domaini439 – 45012Extracellular1 PublicationAdd
BLAST
Transmembranei451 – 47020Helical; Name=7Add
BLAST
Topological domaini471 – 48717Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. integral component of plasma membrane Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Histamine H1 receptorPRO_0000069676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51N-linked (GlcNAc...)Sequence Analysis
Glycosylationi18 – 181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi100 ↔ 1801 PublicationPROSITE-ProRule annotation
Modified residuei140 – 1401Phosphothreonine1 Publication
Modified residuei142 – 1421Phosphothreonine1 Publication
Modified residuei279 – 2791Phosphothreonine1 Publication
Modified residuei396 – 3961Phosphoserine1 Publication
Modified residuei398 – 3981Phosphoserine1 Publication
Disulfide bondi441 ↔ 4441 PublicationPROSITE-ProRule annotation

Post-translational modificationi

Phosphorylation at sites in the second and third cytoplasmic loops independently contribute to agonist-induced receptor downregulation.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP35367.
PaxDbiP35367.
PRIDEiP35367.

PTM databases

PhosphoSiteiP35367.

Expressioni

Gene expression databases

BgeeiP35367.
CleanExiHS_HRH1.
GenevestigatoriP35367.

Organism-specific databases

HPAiHPA029740.

Interactioni

Protein-protein interaction databases

BioGridi109505. 1 interaction.
IntActiP35367. 1 interaction.
MINTiMINT-190077.
STRINGi9606.ENSP00000347299.

Structurei

Secondary structure

1
487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Helixi33 – 5422Combined sources
Helixi61 – 633Combined sources
Helixi64 – 7815Combined sources
Helixi80 – 8910Combined sources
Beta strandi90 – 923Combined sources
Helixi96 – 13035Combined sources
Turni135 – 1384Combined sources
Helixi141 – 15515Combined sources
Helixi156 – 1583Combined sources
Helixi159 – 1635Combined sources
Beta strandi177 – 1804Combined sources
Helixi188 – 19811Combined sources
Helixi200 – 21617Combined sources
Helixi408 – 44134Combined sources
Turni447 – 4493Combined sources
Helixi450 – 47122Combined sources
Helixi473 – 48311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RZEX-ray3.10A20-221[»]
A405-487[»]
ProteinModelPortaliP35367.
SMRiP35367. Positions 19-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1126Important for agonist binding
Regioni424 – 4285Important for agonist binding

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG318797.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000273869.
HOVERGENiHBG101103.
InParanoidiP35367.
KOiK04149.
OMAiYIKFTWK.
OrthoDBiEOG70CR7W.
PhylomeDBiP35367.
TreeFamiTF333432.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000921. Histamine_H1_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00530. HISTAMINEH1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35367-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLPNSSCLL EDKMCEGNKT TMASPQLMPL VVVLSTICLV TVGLNLLVLY
60 70 80 90 100
AVRSERKLHT VGNLYIVSLS VADLIVGAVV MPMNILYLLM SKWSLGRPLC
110 120 130 140 150
LFWLSMDYVA STASIFSVFI LCIDRYRSVQ QPLRYLKYRT KTRASATILG
160 170 180 190 200
AWFLSFLWVI PILGWNHFMQ QTSVRREDKC ETDFYDVTWF KVMTAIINFY
210 220 230 240 250
LPTLLMLWFY AKIYKAVRQH CQHRELINRS LPSFSEIKLR PENPKGDAKK
260 270 280 290 300
PGKESPWEVL KRKPKDAGGG SVLKSPSQTP KEMKSPVVFS QEDDREVDKL
310 320 330 340 350
YCFPLDIVHM QAAAEGSSRD YVAVNRSHGQ LKTDEQGLNT HGASEISEDQ
360 370 380 390 400
MLGDSQSFSR TDSDTTTETA PGKGKLRSGS NTGLDYIKFT WKRLRSHSRQ
410 420 430 440 450
YVSGLHMNRE RKAAKQLGFI MAAFILCWIP YFIFFMVIAF CKNCCNEHLH
460 470 480
MFTIWLGYIN STLNPLIYPL CNENFKKTFK RILHIRS
Length:487
Mass (Da):55,784
Last modified:June 1, 1994 - v1
Checksum:iE5DB418A4C17A985
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081V → E in AAH60802. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191K → N.
Corresponds to variant rs2067466 [ dbSNP | Ensembl ].
VAR_049410
Natural varianti270 – 2701G → E.
Corresponds to variant rs7651620 [ dbSNP | Ensembl ].
VAR_033476
Natural varianti385 – 3851D → E in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035761

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2604.1.
PIRiJC2495.
RefSeqiNP_000852.1. NM_000861.3.
NP_001091681.1. NM_001098211.1.
NP_001091682.1. NM_001098212.1.
NP_001091683.1. NM_001098213.1.
UniGeneiHs.1570.

Genome annotation databases

EnsembliENST00000397056; ENSP00000380247; ENSG00000196639.
ENST00000431010; ENSP00000397028; ENSG00000196639.
ENST00000438284; ENSP00000406705; ENSG00000196639.
GeneIDi3269.
KEGGihsa:3269.
UCSCiuc003bwb.4. human.

Polymorphism databases

DMDMi547645.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2604.1.
PIRiJC2495.
RefSeqiNP_000852.1. NM_000861.3.
NP_001091681.1. NM_001098211.1.
NP_001091682.1. NM_001098212.1.
NP_001091683.1. NM_001098213.1.
UniGeneiHs.1570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RZEX-ray3.10A20-221[»]
A405-487[»]
ProteinModelPortaliP35367.
SMRiP35367. Positions 19-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109505. 1 interaction.
IntActiP35367. 1 interaction.
MINTiMINT-190077.
STRINGi9606.ENSP00000347299.

Chemistry

BindingDBiP35367.
ChEMBLiCHEMBL231.
DrugBankiDB01615. Aceprometazine.
DB06766. Alcaftadine.
DB01246. Alimemazine.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB08799. Antazoline.
DB01238. Aripiprazole.
DB06216. Asenapine.
DB00637. Astemizole.
DB00719. Azatadine.
DB00972. Azelastine.
DB00245. Benzatropine.
DB04890. Bepotastine.
DB06698. Betahistine.
DB01237. Bromodiphenhydramine.
DB00835. Brompheniramine.
DB00354. Buclizine.
DB00748. Carbinoxamine.
DB00341. Cetirizine.
DB08936. Chlorcyclizine.
DB08800. Chloropyramine.
DB01114. Chlorphenamine.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB00568. Cinnarizine.
DB00215. Citalopram.
DB00283. Clemastine.
DB04837. Clofedanol.
DB00363. Clozapine.
DB01176. Cyclizine.
DB00434. Cyproheptadine.
DB01151. Desipramine.
DB00967. Desloratadine.
DB00405. Dexbrompheniramine.
DB00985. Dimenhydrinate.
DB08801. Dimetindene.
DB01075. Diphenhydramine.
DB01146. Diphenylpyraline.
DB01142. Doxepin.
DB00366. Doxylamine.
DB01084. Emedastine.
DB00751. Epinastine.
DB01175. Escitalopram.
DB00950. Fexofenadine.
DB04841. Flunarizine.
DB00667. Histamine Phosphate.
DB00557. Hydroxyzine.
DB04946. Iloperidone.
DB00458. Imipramine.
DB08802. Isothipendyl.
DB00920. Ketotifen.
DB01106. Levocabastine.
DB00455. Loratadine.
DB00408. Loxapine.
DB00934. Maprotiline.
DB00737. Meclizine.
DB06691. Mepyramine.
DB01071. Mequitazine.
DB00902. Methdilazine.
DB01403. Methotrimeprazine.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB00768. Olopatadine.
DB01173. Orphenadrine.
DB01267. Paliperidone.
DB01619. Phenindamine.
DB01620. Pheniramine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB00797. Tolazoline.
DB00656. Trazodone.
DB00726. Trimipramine.
DB00792. Tripelennamine.
DB00427. Triprolidine.
DB00246. Ziprasidone.
GuidetoPHARMACOLOGYi262.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP35367.

Polymorphism databases

DMDMi547645.

Proteomic databases

MaxQBiP35367.
PaxDbiP35367.
PRIDEiP35367.

Protocols and materials databases

DNASUi3269.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397056; ENSP00000380247; ENSG00000196639.
ENST00000431010; ENSP00000397028; ENSG00000196639.
ENST00000438284; ENSP00000406705; ENSG00000196639.
GeneIDi3269.
KEGGihsa:3269.
UCSCiuc003bwb.4. human.

Organism-specific databases

CTDi3269.
GeneCardsiGC03P011113.
HGNCiHGNC:5182. HRH1.
HPAiHPA029740.
MIMi600167. gene.
neXtProtiNX_P35367.
PharmGKBiPA29456.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG318797.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000273869.
HOVERGENiHBG101103.
InParanoidiP35367.
KOiK04149.
OMAiYIKFTWK.
OrthoDBiEOG70CR7W.
PhylomeDBiP35367.
TreeFamiTF333432.

Enzyme and pathway databases

ReactomeiREACT_16903. Histamine receptors.
REACT_18283. G alpha (q) signalling events.

Miscellaneous databases

ChiTaRSiHRH1. human.
GeneWikiiHistamine_H1_receptor.
GenomeRNAii3269.
NextBioi12981.
PROiP35367.
SOURCEiSearch...

Gene expression databases

BgeeiP35367.
CleanExiHS_HRH1.
GenevestigatoriP35367.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000921. Histamine_H1_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00530. HISTAMINEH1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. 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] [Europe PMC] [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] [Europe PMC] [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.
    , 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].
  8. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  10. "Two threonine residues and two serine residues in the second and third intracellular loops are both involved in histamine H1 receptor downregulation."
    Horio S., Kato T., Ogawa M., Fujimoto K., Fukui H.
    FEBS Lett. 573:226-230(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-140; THR-142; SER-396 AND SER-398.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 20-487 IN COMPLEX WITH ANTAGONIST, DISULFIDE BOND, SUBCELLULAR LOCATION, TOPOLOGY.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-385.

Entry informationi

Entry nameiHRH1_HUMAN
AccessioniPrimary (citable) accession number: P35367
Secondary accession number(s): A8K047, Q6P9E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 4, 2015
This is version 138 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.