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Q03431

- PTH1R_HUMAN

UniProt

Q03431 - PTH1R_HUMAN

Protein

Parathyroid hormone/parathyroid hormone-related peptide receptor

Gene

PTH1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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.2 Publications

    GO - Molecular functioni

    1. parathyroid hormone receptor activity Source: UniProtKB
    2. peptide hormone binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein self-association Source: UniProtKB

    GO - Biological processi

    1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
    2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: UniProtKB
    3. aging Source: Ensembl
    4. bone mineralization Source: Ensembl
    5. bone resorption Source: Ensembl
    6. cell maturation Source: Ensembl
    7. chondrocyte differentiation Source: Ensembl
    8. G-protein coupled receptor signaling pathway Source: ProtInc
    9. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
    10. negative regulation of cell proliferation Source: Ensembl
    11. osteoblast development Source: Ensembl
    12. phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
    13. positive regulation of cell proliferation Source: Ensembl
    14. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    15. positive regulation of inositol phosphate biosynthetic process Source: BHF-UCL
    16. skeletal system development Source: ProtInc

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_18372. Class B/2 (Secretin family receptors).
    REACT_19327. G alpha (s) signalling events.
    SignaLinkiQ03431.

    Protein family/group databases

    TCDBi9.A.14.4.11. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PTH1R
    Synonyms:PTHR, PTHR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9608. PTH1R.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical plasma membrane Source: BHF-UCL
    2. basolateral plasma membrane Source: BHF-UCL
    3. brush border membrane Source: Ensembl
    4. cytoplasm Source: ProtInc
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of plasma membrane Source: UniProtKB
    7. nucleus Source: ProtInc
    8. plasma membrane Source: Reactome
    9. receptor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti223 – 2231H → R in JMC; constitutively activated. 2 Publications
    VAR_003582
    Natural varianti410 – 4101T → P in JMC; constitutively activated. 1 Publication
    VAR_003583
    Natural varianti410 – 4101T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. 1 Publication
    VAR_038811
    Natural varianti458 – 4581I → R in JMC. 1 Publication
    VAR_016064
    Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]: Severe skeletal dysplasia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321P → L in BOCD. 1 Publication
    VAR_016062
    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.1 Publication
    Note: The disease may be caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501R → C in ENCHOM; Ollier type; unknown pathological significance. 1 Publication
    Corresponds to variant rs121434601 [ dbSNP | Ensembl ].
    VAR_016063
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1351I → K: Abolishes hormone binding and homodimerization. 1 Publication
    Mutagenesisi137 – 1371D → A: Abolishes hormone binding. No effect on homodimerization. 1 Publication
    Mutagenesisi474 – 4741W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-477. 1 Publication
    Mutagenesisi477 – 4771W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-474. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi125350. phenotype.
    156400. phenotype.
    166000. phenotype.
    215045. phenotype.
    600002. phenotype.
    Orphaneti50945. Chondrodysplasia, Blomstrand type.
    1077. Dental ankylosis.
    79106. Eiken syndrome.
    296. Enchondromatosis.
    33067. Metaphyseal chondrodysplasia, Jansen type.
    PharmGKBiPA33953.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 593567Parathyroid hormone/parathyroid hormone-related peptide receptorPRO_0000012845Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 117
    Disulfide bondi108 ↔ 148
    Disulfide bondi131 ↔ 170
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ03431.
    PRIDEiQ03431.

    2D gel databases

    REPRODUCTION-2DPAGEQ03431.

    PTM databases

    PhosphoSiteiQ03431.

    Miscellaneous databases

    PMAP-CutDBQ03431.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ03431.
    BgeeiQ03431.
    CleanExiHS_PTH1R.
    GenevestigatoriQ03431.

    Organism-specific databases

    HPAiCAB016053.
    HPA007978.

    Interactioni

    Subunit structurei

    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 GNB1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352224EBI-2860297,EBI-491549

    Protein-protein interaction databases

    BioGridi111717. 8 interactions.
    IntActiQ03431. 2 interactions.
    MINTiMINT-258057.
    STRINGi9606.ENSP00000321999.

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 5522
    Beta strandi126 – 1305
    Beta strandi143 – 1486
    Beta strandi152 – 1543
    Beta strandi160 – 1634
    Turni168 – 1736
    Helixi180 – 1856
    Helixi188 – 1969

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ03431.
    SMRiQ03431. Positions 24-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03431.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 188162ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini213 – 2197CytoplasmicSequence Analysis
    Topological domaini240 – 28243ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini307 – 32014CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini343 – 36119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini383 – 40927CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini429 – 44012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini464 – 593130CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei189 – 21224Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei220 – 23920Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei283 – 30624Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei321 – 34222Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei362 – 38221Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei410 – 42819Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei441 – 46323Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi474 – 4774Important for interaction with G proteins

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG293423.
    HOGENOMiHOG000008248.
    HOVERGENiHBG008318.
    KOiK04585.
    OMAiWIIQVPI.
    OrthoDBiEOG7TF78W.
    PhylomeDBiQ03431.
    TreeFamiTF315710.

    Family and domain databases

    InterProiIPR017981. 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]
    PANTHERiPTHR12011:SF24. PTHR12011:SF24. 1 hit.
    PfamiPF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view]
    PRINTSiPR00249. GPCRSECRETIN.
    PR00393. PTRHORMONER.
    SMARTiSM00008. HormR. 1 hit.
    [Graphical view]
    PROSITEiPS00649. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q03431-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK    50
    RLKEVLQRPA SIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTG 100
    SRYRGRPCLP EWDHILCWPL GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR 150
    NGSWELVPGH NRTWANYSEC VKFLTNETRE REVFDRLGMI YTVGYSVSLA 200
    SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK DAVLYSGATL 250
    DEAERLTEEE LRAIAQAPPP PATAAAGYAG CRVAVTFFLY FLATNYYWIL 300
    VEGLYLHSLI FMAFFSEKKY LWGFTVFGWG LPAVFVAVWV SVRATLANTG 350
    CWDLSSGNKK WIIQVPILAS IVLNFILFIN IVRVLATKLR ETNAGRCDTR 400
    QQYRKLLKST LVLMPLFGVH YIVFMATPYT EVSGTLWQVQ MHYEMLFNSF 450
    QGFFVAIIYC FCNGEVQAEI KKSWSRWTLA LDFKRKARSG SSSYSYGPMV 500
    SHTSVTNVGP RVGLGLPLSP RLLPTATTNG HPQLPGHAKP GTPALETLET 550
    TPPAMAAPKD DGFLNGSCSG LDEEASGPER PPALLQEEWE TVM 593
    Length:593
    Mass (Da):66,361
    Last modified:October 1, 1993 - v1
    Checksum:iDA1400640A6C7F2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti471 – 4711K → N(PubMed:8397094)Curated
    Sequence conflicti473 – 4731S → C(PubMed:8397094)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321P → L in BOCD. 1 Publication
    VAR_016062
    Natural varianti150 – 1501R → C in ENCHOM; Ollier type; unknown pathological significance. 1 Publication
    Corresponds to variant rs121434601 [ dbSNP | Ensembl ].
    VAR_016063
    Natural varianti223 – 2231H → R in JMC; constitutively activated. 2 Publications
    VAR_003582
    Natural varianti410 – 4101T → P in JMC; constitutively activated. 1 Publication
    VAR_003583
    Natural varianti410 – 4101T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. 1 Publication
    VAR_038811
    Natural varianti458 – 4581I → R in JMC. 1 Publication
    VAR_016064

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04308 mRNA. Translation: AAA36525.1.
    X68596 mRNA. Translation: CAA48589.1.
    U22409
    , 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.
    CCDSiCCDS2747.1.
    PIRiI38139. A49191.
    RefSeqiNP_000307.1. NM_000316.2.
    NP_001171673.1. NM_001184744.1.
    XP_005265399.1. XM_005265342.1.
    UniGeneiHs.1019.

    Genome annotation databases

    EnsembliENST00000313049; ENSP00000321999; ENSG00000160801.
    ENST00000418619; ENSP00000411424; ENSG00000160801.
    ENST00000430002; ENSP00000413774; ENSG00000160801.
    ENST00000449590; ENSP00000402723; ENSG00000160801.
    GeneIDi5745.
    KEGGihsa:5745.
    UCSCiuc003cqm.3. human.

    Polymorphism databases

    DMDMi417555.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04308 mRNA. Translation: AAA36525.1 .
    X68596 mRNA. Translation: CAA48589.1 .
    U22409
    , 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 .
    CCDSi CCDS2747.1.
    PIRi I38139. A49191.
    RefSeqi NP_000307.1. NM_000316.2.
    NP_001171673.1. NM_001184744.1.
    XP_005265399.1. XM_005265342.1.
    UniGenei Hs.1019.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BL1 NMR - A 168-197 [» ]
    1ET2 model - S 168-469 [» ]
    1ET3 model - S 168-469 [» ]
    3C4M X-ray 1.95 A/B 29-187 [» ]
    3H3G X-ray 1.94 A 29-187 [» ]
    3KJ5 X-ray 3.00 C 474-481 [» ]
    3L2J X-ray 3.24 A/B 29-187 [» ]
    ProteinModelPortali Q03431.
    SMRi Q03431. Positions 24-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111717. 8 interactions.
    IntActi Q03431. 2 interactions.
    MINTi MINT-258057.
    STRINGi 9606.ENSP00000321999.

    Chemistry

    BindingDBi Q03431.
    ChEMBLi CHEMBL1793.
    GuidetoPHARMACOLOGYi 331.

    Protein family/group databases

    TCDBi 9.A.14.4.11. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q03431.

    Polymorphism databases

    DMDMi 417555.

    2D gel databases

    REPRODUCTION-2DPAGE Q03431.

    Proteomic databases

    PaxDbi Q03431.
    PRIDEi Q03431.

    Protocols and materials databases

    DNASUi 5745.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313049 ; ENSP00000321999 ; ENSG00000160801 .
    ENST00000418619 ; ENSP00000411424 ; ENSG00000160801 .
    ENST00000430002 ; ENSP00000413774 ; ENSG00000160801 .
    ENST00000449590 ; ENSP00000402723 ; ENSG00000160801 .
    GeneIDi 5745.
    KEGGi hsa:5745.
    UCSCi uc003cqm.3. human.

    Organism-specific databases

    CTDi 5745.
    GeneCardsi GC03P046895.
    HGNCi HGNC:9608. PTH1R.
    HPAi CAB016053.
    HPA007978.
    MIMi 125350. phenotype.
    156400. phenotype.
    166000. phenotype.
    168468. gene.
    215045. phenotype.
    600002. phenotype.
    neXtProti NX_Q03431.
    Orphaneti 50945. Chondrodysplasia, Blomstrand type.
    1077. Dental ankylosis.
    79106. Eiken syndrome.
    296. Enchondromatosis.
    33067. Metaphyseal chondrodysplasia, Jansen type.
    PharmGKBi PA33953.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293423.
    HOGENOMi HOG000008248.
    HOVERGENi HBG008318.
    KOi K04585.
    OMAi WIIQVPI.
    OrthoDBi EOG7TF78W.
    PhylomeDBi Q03431.
    TreeFami TF315710.

    Enzyme and pathway databases

    Reactomei REACT_18372. Class B/2 (Secretin family receptors).
    REACT_19327. G alpha (s) signalling events.
    SignaLinki Q03431.

    Miscellaneous databases

    EvolutionaryTracei Q03431.
    GeneWikii Parathyroid_hormone_1_receptor.
    GenomeRNAii 5745.
    NextBioi 22372.
    PMAP-CutDB Q03431.
    PROi Q03431.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03431.
    Bgeei Q03431.
    CleanExi HS_PTH1R.
    Genevestigatori Q03431.

    Family and domain databases

    InterProi IPR017981. 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 ]
    PANTHERi PTHR12011:SF24. PTHR12011:SF24. 1 hit.
    Pfami PF00002. 7tm_2. 1 hit.
    PF02793. HRM. 1 hit.
    [Graphical view ]
    PRINTSi PR00249. GPCRSECRETIN.
    PR00393. PTRHORMONER.
    SMARTi SM00008. HormR. 1 hit.
    [Graphical view ]
    PROSITEi PS00649. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiPTH1R_HUMAN
    AccessioniPrimary (citable) accession number: Q03431
    Secondary accession number(s): Q2M1U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 154 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