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P4HTM
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| P4HTM | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | P4HTM, EGLN4, HIFPH4, P4H-TM, PH-4, PH4, PHD4, prolyl 4-hydroxylase, transmembrane, HIDEA | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 614584; MGI: 1921693; GeneCards: P4HTM | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene.[5]
Function
[edit]The product of this gene belongs to the family of prolyl 4-hydroxylases. This protein is a prolyl hydroxylase that may be involved in the degradation of hypoxia-inducible transcription factors under normoxia. It plays a role in adaptation to hypoxia and may be related to cellular oxygen sensing. Alternatively spliced variants encoding different isoforms have been identified.
References
[edit]- ^ a b c GRCh38: Ensembl release 89: ENSG00000178467 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006675 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: Prolyl 4-hydroxylase, transmembrane". Retrieved 2017-10-03.
Further reading
[edit]- Oehme F, Ellinghaus P, Kolkhof P, Smith TJ, Ramakrishnan S, Hütter J, Schramm M, Flamme I (2002). "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochem. Biophys. Res. Commun. 296 (2): 343–9. doi:10.1016/s0006-291x(02)00862-8. PMID 12163023.
- Hirsilä M, Koivunen P, Günzler V, Kivirikko KI, Myllyharju J (2003). "Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor". J. Biol. Chem. 278 (33): 30772–80. doi:10.1074/jbc.M304982200. PMID 12788921.
- Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J (2004). "The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues". J. Biol. Chem. 279 (50): 52255–61. doi:10.1074/jbc.M410007200. PMID 15456751.
- Hirota K, Semenza GL (2005). "Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases". Biochem. Biophys. Res. Commun. 338 (1): 610–6. doi:10.1016/j.bbrc.2005.08.193. PMID 16154531.
- Iwahashi M, Muragaki Y, Ino K (2012). "Human prolyl hydroxylase expression in uterine leiomyoma during the menstrual cycle". Reprod. Biol. Endocrinol. 10: 111. doi:10.1186/1477-7827-10-111. PMC 3566935. PMID 23241241.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.