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Q03431 (PTH1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Parathyroid hormone/parathyroid hormone-related peptide receptor
Alternative name(s):
PTH/PTHrP type I receptor
Short name=PTH/PTHr receptor
Parathyroid hormone 1 receptor
Short name=PTH1 receptor
Gene names
Name:PTH1R
Synonyms:PTHR, PTHR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. Ref.10 Ref.12

Subunit structure

Interacts (via N-terminal extracellular domain) with PTHLH and PTH. Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer. Interacts (via C-terminus) with the heterodimer formed by GNG2 and GNB1. Ref.10 Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.12.

Tissue specificity

Expressed in most tissues. Most abundant in kidney, bone and liver.

Involvement in disease

Jansen metaphyseal chondrodysplasia (JMC) [MIM:156400]: Rare autosomal dominant disorder characterized by a short-limbed dwarfism associated with hypercalcemia and normal or low serum concentrations of the two parathyroid hormones.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15 Ref.17 Ref.20

Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]: Severe skeletal dysplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Enchondromatosis multiple (ENCHOM) [MIM:166000]: A condition characterized by multiple formation of enchondromas, benign neoplasms derived from mesodermal cells that form cartilage. Enchondromas remain within the substance of a cartilage or bone. Clinical problems caused by enchondromas include skeletal deformity and the potential for malignant change to osteosarcoma.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19

Eiken skeletal dysplasia (EISD) [MIM:600002]: A rare skeletal dysplasia characterized by severely retarded ossification, principally of the epiphyses, pelvis, hands and feet, as well as by abnormal modeling of the bones in hands and feet, abnormal persistence of cartilage in the pelvis and mild growth retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

Primary failure of tooth eruption (PFE) [MIM:125350]: Rare condition that has high penetrance and variable expressivity and in which tooth retention occurs without evidence of any obvious mechanical interference. Instead, malfunction of the eruptive mechanism itself appears to cause nonankylosed permanent teeth to fail to erupt, although the eruption pathway has been cleared by bone resorption.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DiseaseDisease mutation
Dwarfism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement Ref.16. Source: ProtInc

G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger

Traceable author statement PubMed 9927325. Source: ProtInc

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from direct assay Ref.11. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

bone mineralization

Inferred from electronic annotation. Source: Ensembl

bone resorption

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

osteoblast development

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred by curator PubMed 19608645. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of inositol phosphate biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

skeletal system development

Traceable author statement Ref.16. Source: ProtInc

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 10709993. Source: ProtInc

integral component of plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Traceable author statement PubMed 10709993. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionparathyroid hormone receptor activity

Inferred from direct assay Ref.11. Source: UniProtKB

peptide hormone binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23124878. Source: IntAct

protein self-association

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352224EBI-2860297,EBI-491549

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 593567Parathyroid hormone/parathyroid hormone-related peptide receptor
PRO_0000012845

Regions

Topological domain27 – 188162Extracellular Potential
Transmembrane189 – 21224Helical; Name=1; Potential
Topological domain213 – 2197Cytoplasmic Potential
Transmembrane220 – 23920Helical; Name=2; Potential
Topological domain240 – 28243Extracellular Potential
Transmembrane283 – 30624Helical; Name=3; Potential
Topological domain307 – 32014Cytoplasmic Potential
Transmembrane321 – 34222Helical; Name=4; Potential
Topological domain343 – 36119Extracellular Potential
Transmembrane362 – 38221Helical; Name=5; Potential
Topological domain383 – 40927Cytoplasmic Potential
Transmembrane410 – 42819Helical; Name=6; Potential
Topological domain429 – 44012Extracellular Potential
Transmembrane441 – 46323Helical; Name=7; Potential
Topological domain464 – 593130Cytoplasmic Potential
Motif474 – 4774Important for interaction with G proteins

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation1761N-linked (GlcNAc...) Potential
Disulfide bond48 ↔ 117 Ref.7 Ref.9 Ref.11
Disulfide bond108 ↔ 148 Ref.7 Ref.9 Ref.11
Disulfide bond131 ↔ 170 Ref.7 Ref.9 Ref.11

Natural variations

Natural variant1321P → L in BOCD. Ref.16
VAR_016062
Natural variant1501R → C in ENCHOM; Ollier type; unknown pathological significance. Ref.18 Ref.19
Corresponds to variant rs121434601 [ dbSNP | Ensembl ].
VAR_016063
Natural variant2231H → R in JMC; constitutively activated. Ref.13 Ref.14 Ref.15
VAR_003582
Natural variant4101T → P in JMC; constitutively activated. Ref.14 Ref.15
VAR_003583
Natural variant4101T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. Ref.20
VAR_038811
Natural variant4581I → R in JMC. Ref.17
VAR_016064

Experimental info

Mutagenesis1351I → K: Abolishes hormone binding and homodimerization. Ref.12
Mutagenesis1371D → A: Abolishes hormone binding. No effect on homodimerization. Ref.12
Mutagenesis4741W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-477. Ref.10
Mutagenesis4771W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-474. Ref.10
Sequence conflict4711K → N Ref.2
Sequence conflict4731S → C Ref.2

Secondary structure

................. 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03431 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: DA1400640A6C7F2B

FASTA59366,361
        10         20         30         40         50         60 
MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK RLKEVLQRPA 

        70         80         90        100        110        120 
SIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTG SRYRGRPCLP EWDHILCWPL 

       130        140        150        160        170        180 
GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR NGSWELVPGH NRTWANYSEC VKFLTNETRE 

       190        200        210        220        230        240 
REVFDRLGMI YTVGYSVSLA SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK 

       250        260        270        280        290        300 
DAVLYSGATL DEAERLTEEE LRAIAQAPPP PATAAAGYAG CRVAVTFFLY FLATNYYWIL 

       310        320        330        340        350        360 
VEGLYLHSLI FMAFFSEKKY LWGFTVFGWG LPAVFVAVWV SVRATLANTG CWDLSSGNKK 

       370        380        390        400        410        420 
WIIQVPILAS IVLNFILFIN IVRVLATKLR ETNAGRCDTR QQYRKLLKST LVLMPLFGVH 

       430        440        450        460        470        480 
YIVFMATPYT EVSGTLWQVQ MHYEMLFNSF QGFFVAIIYC FCNGEVQAEI KKSWSRWTLA 

       490        500        510        520        530        540 
LDFKRKARSG SSSYSYGPMV SHTSVTNVGP RVGLGLPLSP RLLPTATTNG HPQLPGHAKP 

       550        560        570        580        590 
GTPALETLET TPPAMAAPKD DGFLNGSCSG LDEEASGPER PPALLQEEWE TVM 

« Hide

References

« Hide 'large scale' references
[1]"Identical complementary deoxyribonucleic acids encode a human renal and bone parathyroid hormone (PTH)/PTH-related peptide receptor."
Schipani E., Karga H., Karaplis A.C., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H.
Endocrinology 132:2157-2165(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"Cloning and functional expression of a human parathyroid hormone receptor."
Schneider H., Feyen J.-H., Rao Movva N.
Eur. J. Pharmacol. 246:149-155(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene."
Schipani E., Weinstein L.S., Bergwitz C., Iida-Klein A., Kong X.F., Stuhrmann M., Kruse K., Whyte M.P., Murray T., Schmidtke J., Dop C., Brickman A.S., Crawford J.D., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H.
J. Clin. Endocrinol. Metab. 80:1611-1621(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Characterization of cDNA and genomic DNA encoding the human PTH/PTHrP receptor."
Levine M.A.
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[5]"Isolation of cDNA coding for parathyroid hormone receptor 1 (PTHR1)."
King M.M., Aronstam R.S., Sharma S.V.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[6]"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: Cerebellum.
[7]"The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern."
Grauschopf U., Lilie H., Honold K., Wozny M., Reusch D., Esswein A., Schafer W., Rucknagel K.P., Rudolph R.
Biochemistry 39:8878-8887(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS IN EXTRACELLULAR DOMAIN.
[8]"Binding domain of human parathyroid hormone receptor: from conformation to function."
Pellegrini M., Bisello A., Rosenblatt M., Chorev M., Mierke D.F.
Biochemistry 37:12737-12743(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 168-198.
[9]"Molecular recognition of parathyroid hormone by its G protein-coupled receptor."
Pioszak A.A., Xu H.E.
Proc. Natl. Acad. Sci. U.S.A. 105:5034-5039(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTH, DISULFIDE BONDS.
[10]"Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 474-481 IN COMPLEX WITH GNG2 AND GNB1, FUNCTION, SUBUNIT, MUTAGENESIS OF TRP-474 AND TRP-477.
[11]"Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides."
Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E.
J. Biol. Chem. 284:28382-28391(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTHLH, DISULFIDE BONDS.
[12]"Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation."
Pioszak A.A., Harikumar K.G., Parker N.R., Miller L.J., Xu H.E.
J. Biol. Chem. 285:12435-12444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 29-187, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-135 AND ASP-137.
[13]"A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia."
Schipani E., Kruse K., Jueppner H.
Science 268:98-100(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JMC ARG-223.
[14]"Constitutively activated receptors for parathyroid hormone and parathyroid hormone-related peptide in Jansen's metaphyseal chondrodysplasia."
Schipani E., Langman C.B., Parfitt A.M., Jensen G.S., Kikuchi S., Kooh S.W., Cole W.G., Jueppner H.
N. Engl. J. Med. 335:708-714(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JMC ARG-223 AND PRO-410.
[15]"Constitutive activation of the cyclic adenosine 3',5'-monophosphate signaling pathway by parathyroid hormone (PTH)/PTH-related peptide receptors mutated at the two loci for Jansen's metaphyseal chondrodysplasia."
Schipani E., Jensen G.S., Pincus J., Nissenson R.A., Gardella T.J., Jueppner H.
Mol. Endocrinol. 11:851-858(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS JMC ARG-223 AND PRO-410.
[16]"A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia."
Zhang P., Jobert A.-S., Couvineau A., Silve C.
J. Clin. Endocrinol. Metab. 83:3365-3368(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BOCD LEU-132.
[17]"A novel parathyroid hormone (PTH)/PTH-related peptide receptor mutation in Jansen's metaphyseal chondrodysplasia."
Schipani E., Langman C.B., Hunzelman J., Le Merrer M., Loke K.Y., Dillon M.J., Silve C., Jueppner H.
J. Clin. Endocrinol. Metab. 84:3052-3057(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JMC ARG-458.
[18]"A mutant PTH/PTHrP type I receptor in enchondromatosis."
Hopyan S., Gokgoz N., Poon R., Gensure R.C., Yu C., Cole W.G., Bell R.S., Jueppner H., Andrulis I.L., Wunder J.S., Alman B.A.
Nat. Genet. 30:306-310(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENCHOM CYS-150.
[19]"Enchondromatosis (Ollier disease, Maffucci syndrome) is not caused by the PTHR1 mutation p.R150C."
Rozeman L.B., Sangiorgi L., Briaire-de Bruijn I.H., Mainil-Varlet P., Bertoni F., Cleton-Jansen A.-M., Hogendoorn P.C.W., Bovee J.V.M.G.
Hum. Mutat. 24:466-473(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF THE ASSOCIATION OF CYS-150 WITH ENCHOM.
[20]"A form of Jansen's metaphyseal chondrodysplasia with limited metabolic and skeletal abnormalities is caused by a novel activating parathyroid hormone (PTH)/PTH-related peptide receptor mutation."
Bastepe M., Raas-Rothschild A., Silver J., Weissman I., Wientroub S., Jueppner H., Gillis D.
J. Clin. Endocrinol. Metab. 89:3595-3600(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JMC ARG-410, CHARACTERIZATION OF VARIANT JMC ARG-410.
[21]"Recessive mutations in PTHR1 cause contrasting skeletal dysplasias in Eiken and Blomstrand syndromes."
Duchatelet S., Ostergaard E., Cortes D., Lemainque A., Julier C.
Hum. Mol. Genet. 14:1-5(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EISD.
[22]"PTHR1 loss-of-function mutations in familial, nonsyndromic primary failure of tooth eruption."
Decker E., Stellzig-Eisenhauer A., Fiebig B.S., Rau C., Kress W., Saar K., Rueschendorf F., Hubner N., Grimm T., Weber B.H.F.
Am. J. Hum. Genet. 83:781-786(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PRIMARY FAILURE OF TOOTH ERUPTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04308 mRNA. Translation: AAA36525.1.
X68596 mRNA. Translation: CAA48589.1.
U22409 expand/collapse EMBL AC list , U22401, U22402, U22403, U22404, U22405, U22406, U22407, U22408 Genomic DNA. Translation: AAB60657.1.
U17418 mRNA. Translation: AAA56774.1.
AY449732 mRNA. Translation: AAR18076.1.
BC112221 mRNA. Translation: AAI12222.1.
BC112247 mRNA. Translation: AAI12248.1.
CCDSCCDS2747.1.
PIRA49191. I38139.
RefSeqNP_000307.1. NM_000316.2.
NP_001171673.1. NM_001184744.1.
XP_005265399.1. XM_005265342.1.
UniGeneHs.1019.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BL1NMR-A168-197[»]
1ET2model-S168-469[»]
1ET3model-S168-469[»]
3C4MX-ray1.95A/B29-187[»]
3H3GX-ray1.94A29-187[»]
3KJ5X-ray3.00C474-481[»]
3L2JX-ray3.24A/B29-187[»]
ProteinModelPortalQ03431.
SMRQ03431. Positions 24-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111717. 8 interactions.
IntActQ03431. 2 interactions.
MINTMINT-258057.
STRING9606.ENSP00000321999.

Chemistry

BindingDBQ03431.
ChEMBLCHEMBL1793.
GuidetoPHARMACOLOGY331.

Protein family/group databases

TCDB9.A.14.4.11. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

PTM databases

PhosphoSiteQ03431.

Polymorphism databases

DMDM417555.

2D gel databases

REPRODUCTION-2DPAGEQ03431.

Proteomic databases

PaxDbQ03431.
PRIDEQ03431.

Protocols and materials databases

DNASU5745.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313049; ENSP00000321999; ENSG00000160801.
ENST00000418619; ENSP00000411424; ENSG00000160801.
ENST00000430002; ENSP00000413774; ENSG00000160801.
ENST00000449590; ENSP00000402723; ENSG00000160801.
GeneID5745.
KEGGhsa:5745.
UCSCuc003cqm.3. human.

Organism-specific databases

CTD5745.
GeneCardsGC03P046895.
HGNCHGNC:9608. PTH1R.
HPACAB016053.
HPA007978.
MIM125350. phenotype.
156400. phenotype.
166000. phenotype.
168468. gene.
215045. phenotype.
600002. phenotype.
neXtProtNX_Q03431.
Orphanet50945. Chondrodysplasia, Blomstrand type.
1077. Dental ankylosis.
79106. Eiken syndrome.
296. Enchondromatosis.
33067. Metaphyseal chondrodysplasia, Jansen type.
PharmGKBPA33953.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293423.
HOGENOMHOG000008248.
HOVERGENHBG008318.
KOK04585.
OMAWIIQVPI.
OrthoDBEOG7TF78W.
PhylomeDBQ03431.
TreeFamTF315710.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ03431.

Gene expression databases

ArrayExpressQ03431.
BgeeQ03431.
CleanExHS_PTH1R.
GenevestigatorQ03431.

Family and domain databases

InterProIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR002170. GPCR_2_parathyroid_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PANTHERPTHR12011:SF24. PTHR12011:SF24. 1 hit.
PfamPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSPR00249. GPCRSECRETIN.
PR00393. PTRHORMONER.
SMARTSM00008. HormR. 1 hit.
[Graphical view]
PROSITEPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ03431.
GeneWikiParathyroid_hormone_1_receptor.
GenomeRNAi5745.
NextBio22372.
PMAP-CutDBQ03431.
PROQ03431.
SOURCESearch...

Entry information

Entry namePTH1R_HUMAN
AccessionPrimary (citable) accession number: Q03431
Secondary accession number(s): Q2M1U3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries