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P01270

- PTHY_HUMAN

UniProt

P01270 - PTHY_HUMAN

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

Functioni

PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.1 Publication

GO - Molecular functioni

  1. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  2. hormone activity Source: ProtInc
  3. peptide hormone receptor binding Source: UniProtKB

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
  2. Rho protein signal transduction Source: Ensembl
  3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
  4. bone resorption Source: UniProtKB
  5. cAMP metabolic process Source: ProtInc
  6. cell-cell signaling Source: ProtInc
  7. cellular calcium ion homeostasis Source: Ensembl
  8. cellular macromolecule biosynthetic process Source: MGI
  9. hormone-mediated apoptotic signaling pathway Source: ProtInc
  10. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. positive regulation of bone mineralization Source: UniProtKB
  12. positive regulation of cAMP biosynthetic process Source: MGI
  13. positive regulation of glucose import Source: UniProtKB
  14. positive regulation of glycogen biosynthetic process Source: UniProtKB
  15. positive regulation of signal transduction Source: Ensembl
  16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  17. regulation of gene expression Source: MGI
  18. response to cadmium ion Source: Ensembl
  19. response to drug Source: Ensembl
  20. response to ethanol Source: Ensembl
  21. response to fibroblast growth factor Source: Ensembl
  22. response to lead ion Source: Ensembl
  23. response to parathyroid hormone Source: Ensembl
  24. response to vitamin D Source: Ensembl
  25. skeletal system development Source: ProtInc
  26. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Parathyroid hormone
Short name:
PTH
Alternative name(s):
Parathormone
Parathyrin
Gene namesi
Name:PTH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9606. PTH.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hypoparathyroidism, familial isolated (FIH) [MIM:146200]: A disorder characterized by hypocalcemia and hyperphosphatemia due to inadequate secretion of parathyroid hormone. Clinical features include seizures, tetany and cramps.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181C → R in FIH; dominant; leads to inefficient processing of the precursor; the expressed mutant hormone is trapped intracellularly in the endoplasmic reticulum resulting in apoptosis; mutant protein-expressing cells also show marked up-regulation of the endoplasmic reticulum stress-responsive hormones HSPA5 and EIF2AK3 and the proapoptotic transcription factor DDIT3. 3 Publications
VAR_006047
Natural varianti23 – 231S → P in FIH; recessive, might lead to inefficient processing of the precursor. 1 Publication
VAR_018464

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161A → R: Abolishes processing of the precursor; when associated with variant R-18. 1 Publication
Mutagenesisi51 – 511R → A: Reduced affinity for PTH1R. 1 Publication
Mutagenesisi54 – 541W → A: Strongly reduced affinity for PTH1R. 1 Publication
Mutagenesisi55 – 551L → A: Strongly reduced affinity for PTH1R. 1 Publication
Mutagenesisi58 – 581K → A: Reduced affinity for PTH1R. 1 Publication
Mutagenesisi59 – 591L → A: Strongly reduced affinity for PTH1R. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi146200. phenotype.
Orphaneti189466. Familial isolated hypoparathyroidism due to impaired PTH secretion.
PharmGKBiPA33951.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 Publications
Add
BLAST
Propeptidei26 – 316
PRO_0000023249
Chaini32 – 11584Parathyroid hormone
PRO_0000023250Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

PaxDbiP01270.
PeptideAtlasiP01270.
PRIDEiP01270.

PTM databases

PhosphoSiteiP01270.

Miscellaneous databases

PMAP-CutDBP01270.

Expressioni

Gene expression databases

BgeeiP01270.
CleanExiHS_PTH.
GenevestigatoriP01270.

Organism-specific databases

HPAiCAB000072.
CAB023409.

Interactioni

Subunit structurei

Interacts with PTH1R (via N-terminal extracellular domain).1 Publication

Protein-protein interaction databases

BioGridi111713. 6 interactions.
IntActiP01270. 2 interactions.
MINTiMINT-1403915.
STRINGi9606.ENSP00000282091.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 6431
Helixi65 – 673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWXNMR-A32-70[»]
1ET1X-ray0.90A/B32-65[»]
1ET2model-A32-65[»]
1FVYNMR-A32-62[»]
1HPHNMR-A32-68[»]
1HPYNMR-A32-65[»]
1HTHNMR-A32-65[»]
1ZWANMR-A32-65[»]
1ZWBNMR-A33-68[»]
1ZWDNMR-A34-68[»]
1ZWENMR-A35-68[»]
1ZWFNMR-A35-68[»]
1ZWGNMR-A35-68[»]
2L1XNMR-A32-65[»]
3C4MX-ray1.95C/D46-65[»]
DisProtiDP00637.
ProteinModelPortaliP01270.
SMRiP01270. Positions 32-70.

Miscellaneous databases

EvolutionaryTraceiP01270.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 6919Important for receptor binding
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41709.
HOGENOMiHOG000033707.
HOVERGENiHBG008319.
InParanoidiP01270.
KOiK05261.
OMAiEIQFMHN.
OrthoDBiEOG7ZGX5Q.
PhylomeDBiP01270.
TreeFamiTF336197.

Family and domain databases

InterProiIPR003625. PTH.
IPR001415. PTH/PTH-rel.
[Graphical view]
PANTHERiPTHR10541. PTHR10541. 1 hit.
PfamiPF01279. Parathyroid. 1 hit.
[Graphical view]
PIRSFiPIRSF001832. PTH. 1 hit.
SMARTiSM00087. PTH. 1 hit.
[Graphical view]
PROSITEiPS00335. PARATHYROID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01270-1 [UniParc]FASTAAdd to Basket

« Hide

MIPAKDMAKV MIVMLAICFL TKSDGKSVKK RSVSEIQLMH NLGKHLNSME    50
RVEWLRKKLQ DVHNFVALGA PLAPRDAGSQ RPRKKEDNVL VESHEKSLGE 100
ADKADVNVLT KAKSQ 115
Length:115
Mass (Da):12,861
Last modified:August 13, 1987 - v1
Checksum:i849015736A6E5597
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181C → R in FIH; dominant; leads to inefficient processing of the precursor; the expressed mutant hormone is trapped intracellularly in the endoplasmic reticulum resulting in apoptosis; mutant protein-expressing cells also show marked up-regulation of the endoplasmic reticulum stress-responsive hormones HSPA5 and EIF2AK3 and the proapoptotic transcription factor DDIT3. 3 Publications
VAR_006047
Natural varianti23 – 231S → P in FIH; recessive, might lead to inefficient processing of the precursor. 1 Publication
VAR_018464

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00597 mRNA. Translation: CAA23843.1.
J00301 Genomic DNA. Translation: AAA60215.1.
BC096142 mRNA. Translation: AAH96142.1.
BC096143 mRNA. Translation: AAH96143.1.
BC096144 mRNA. Translation: AAH96144.1.
BC096145 mRNA. Translation: AAH96145.1.
CCDSiCCDS7812.1.
PIRiA19339. PTHU.
RefSeqiNP_000306.1. NM_000315.2.
UniGeneiHs.37045.

Genome annotation databases

EnsembliENST00000282091; ENSP00000282091; ENSG00000152266.
ENST00000529816; ENSP00000433208; ENSG00000152266.
GeneIDi5741.
KEGGihsa:5741.
UCSCiuc001mlb.3. human.

Polymorphism databases

DMDMi131547.

Cross-referencesi

Web resourcesi

Wikipedia

Parathyroid hormone entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
V00597 mRNA. Translation: CAA23843.1 .
J00301 Genomic DNA. Translation: AAA60215.1 .
BC096142 mRNA. Translation: AAH96142.1 .
BC096143 mRNA. Translation: AAH96143.1 .
BC096144 mRNA. Translation: AAH96144.1 .
BC096145 mRNA. Translation: AAH96145.1 .
CCDSi CCDS7812.1.
PIRi A19339. PTHU.
RefSeqi NP_000306.1. NM_000315.2.
UniGenei Hs.37045.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BWX NMR - A 32-70 [» ]
1ET1 X-ray 0.90 A/B 32-65 [» ]
1ET2 model - A 32-65 [» ]
1FVY NMR - A 32-62 [» ]
1HPH NMR - A 32-68 [» ]
1HPY NMR - A 32-65 [» ]
1HTH NMR - A 32-65 [» ]
1ZWA NMR - A 32-65 [» ]
1ZWB NMR - A 33-68 [» ]
1ZWD NMR - A 34-68 [» ]
1ZWE NMR - A 35-68 [» ]
1ZWF NMR - A 35-68 [» ]
1ZWG NMR - A 35-68 [» ]
2L1X NMR - A 32-65 [» ]
3C4M X-ray 1.95 C/D 46-65 [» ]
DisProti DP00637.
ProteinModelPortali P01270.
SMRi P01270. Positions 32-70.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111713. 6 interactions.
IntActi P01270. 2 interactions.
MINTi MINT-1403915.
STRINGi 9606.ENSP00000282091.

PTM databases

PhosphoSitei P01270.

Polymorphism databases

DMDMi 131547.

Proteomic databases

PaxDbi P01270.
PeptideAtlasi P01270.
PRIDEi P01270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282091 ; ENSP00000282091 ; ENSG00000152266 .
ENST00000529816 ; ENSP00000433208 ; ENSG00000152266 .
GeneIDi 5741.
KEGGi hsa:5741.
UCSCi uc001mlb.3. human.

Organism-specific databases

CTDi 5741.
GeneCardsi GC11M013470.
HGNCi HGNC:9606. PTH.
HPAi CAB000072.
CAB023409.
MIMi 146200. phenotype.
168450. gene.
neXtProti NX_P01270.
Orphaneti 189466. Familial isolated hypoparathyroidism due to impaired PTH secretion.
PharmGKBi PA33951.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41709.
HOGENOMi HOG000033707.
HOVERGENi HBG008319.
InParanoidi P01270.
KOi K05261.
OMAi EIQFMHN.
OrthoDBi EOG7ZGX5Q.
PhylomeDBi P01270.
TreeFami TF336197.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P01270.
GeneWikii Parathyroid_hormone.
GenomeRNAii 5741.
NextBioi 22348.
PMAP-CutDB P01270.
PROi P01270.
SOURCEi Search...

Gene expression databases

Bgeei P01270.
CleanExi HS_PTH.
Genevestigatori P01270.

Family and domain databases

InterProi IPR003625. PTH.
IPR001415. PTH/PTH-rel.
[Graphical view ]
PANTHERi PTHR10541. PTHR10541. 1 hit.
Pfami PF01279. Parathyroid. 1 hit.
[Graphical view ]
PIRSFi PIRSF001832. PTH. 1 hit.
SMARTi SM00087. PTH. 1 hit.
[Graphical view ]
PROSITEi PS00335. PARATHYROID. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of cloned cDNAs encoding human preproparathyroid hormone."
    Hendy G.N., Kronenberg H.M., Potts J.T. Jr., Rich A.
    Proc. Natl. Acad. Sci. U.S.A. 78:7365-7369(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein."
    Karaplis A.C., Lim S.-K., Baba H., Arnold A., Kronenberg H.M.
    J. Biol. Chem. 270:1629-1635(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31, MUTAGENESIS OF ALA-16, VARIANT ARG-18.
  5. "Structural analysis of human proparathyroid hormone by a new microsequencing approach."
    Jacobs J.W., Kemper B., Niall H.D., Habener J.F., Potts J.T. Jr.
    Nature 249:155-157(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-37.
  6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-40.
  7. "The amino-acid sequence of the amino-terminal 37 residues of human parathyroid hormone."
    Niall H.D., Sauer R.T., Jacobs J.W., Keutmann H.T., Segre G.V., O'Riordan J.L.H., Aurbach G.D., Potts J.T. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 71:384-388(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-68.
  8. Cited for: PROTEIN SEQUENCE OF 61-83 AND 84-115.
  9. Keutmann H.T., Niall H.D., Jacobs J.W., Barling P.M., Hendy G.N., O'Riordan J.L.H., Potts J.T. Jr.
    (In) Talmadge R.V., Owen M., Parsons J.A. (eds.); Calcium-regulating hormones, pp.9-14, Excerpta Medica Foundation, Amsterdam (1975)
    Cited for: PROTEIN SEQUENCE OF 75-100.
  10. "A reinvestigation of the amino-terminal sequence of human parathyroid hormone."
    Keutmann H.T., Niall H.D., O'Riordan J.L.H., Potts J.T. Jr.
    Biochemistry 14:1842-1847(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  11. "Solid-phase synthesis of the biologically active N-terminal 1-34 peptide of human parathyroid hormone."
    Tregear G.W., van Rietschoten J., Green E., Niall H.D., Keutmann H.T., Parsons J.A., O'Riordan J.L.H., Potts J.T. Jr.
    Hoppe-Seyler's Z. Physiol. Chem. 355:415-421(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 32-65.
  12. Cited for: SYNTHESIS OF 32-65.
  13. "Stimulation of glucose transport in osteoblastic cells by parathyroid hormone and insulin-like growth factor I."
    Zoidis E., Ghirlanda-Keller C., Schmid C.
    Mol. Cell. Biochem. 348:33-42(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Investigation of the solution structure of the human parathyroid hormone fragment (1-34) by 1H NMR spectroscopy, distance geometry, and molecular dynamics calculations."
    Klaus W., Dieckmann T., Wray V., Schomburg D., Wingender E., Mayer H.
    Biochemistry 30:6936-6942(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 32-65.
  15. "Stabilized NMR structure of human parathyroid hormone(1-34)."
    Barden J.A., Cuthbertson R.M.
    Eur. J. Biochem. 215:315-321(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 32-65.
  16. Cited for: STRUCTURE BY NMR OF 32-68.
  17. "Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37)."
    Marx U.C., Adermann K., Bayer P., Forssmann W.-G., Rosch P.
    Biochem. Biophys. Res. Commun. 267:213-220(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 32-70.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 32-65.
  19. "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 46-65 IN COMPLEX WITH PTH1R, INTERACTION WITH PTH1R, MUTAGENESIS OF ARG-51; TRP-54; LEU-55; LYS-58 AND LEU-59.
  20. "Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism."
    Arnold A., Horst S.A., Gardella T.J., Baba H., Levine M.A., Kronenberg H.M.
    J. Clin. Invest. 86:1084-1087(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FIH ARG-18.
  21. "A novel mutation of the signal peptide of the preproparathyroid hormone gene associated with autosomal recessive familial isolated hypoparathyroidism."
    Sunthornthepvarakul T., Churesigaew S., Ngowngarmratana S.
    J. Clin. Endocrinol. Metab. 84:3792-3796(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FIH PRO-23.
  22. "Signal sequence mutation in autosomal dominant form of hypoparathyroidism induces apoptosis that is corrected by a chemical chaperone."
    Datta R., Waheed A., Shah G.N., Sly W.S.
    Proc. Natl. Acad. Sci. U.S.A. 104:19989-19994(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT FIH ARG-18.

Entry informationi

Entry nameiPTHY_HUMAN
AccessioniPrimary (citable) accession number: P01270
Secondary accession number(s): Q4VB48, Q9UD38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 151 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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