P4HTM

P4HTM
Identifiers
Aliases	P4HTM, EGLN4, HIFPH4, P4H-TM, PH-4, PH4, PHD4, prolyl 4-hydroxylase, transmembrane, HIDEA
External IDs	OMIM: 614584 MGI: 1921693 HomoloGene: 41765 GeneCards: P4HTM
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.31|3p21.3 Start 48,989,889 bp End 49,007,153 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F2 Start 108,456,061 bp End 108,474,866 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube bronchial epithelial cell pituitary gland anterior pituitary prefrontal cortex Brodmann area 9 nucleus accumbens postcentral gyrus caudate nucleus hypothalamus Top expressed in substantia nigra nucleus accumbens temporal lobe facial motor nucleus prefrontal cortex ventromedial nucleus paraventricular nucleus of hypothalamus mammillary body subiculum superior colliculus More reference expression data BioGPS n/a
Gene ontology Molecular function 2-oxoglutarate-dependent dioxygenase activity iron ion binding L-ascorbic acid binding oxidoreductase activity dioxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen metal ion binding calcium ion binding procollagen-proline 4-dioxygenase activity Cellular component integral component of membrane endoplasmic reticulum membrane endoplasmic reticulum membrane Biological process regulation of erythrocyte differentiation peptidyl-proline hydroxylation to 4-hydroxy-L-proline Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 54681 74443 Ensembl ENSG00000178467 ENSMUSG00000006675 UniProt Q9NXG6 Q8BG58 RefSeq (mRNA) NM_017732 NM_177938 NM_177939 NM_028944 NM_001357465 RefSeq (protein) NP_808807 NP_808808 NP_083220 NP_001344394 Location (UCSC) Chr 3: 48.99 – 49.01 Mb Chr 9: 108.46 – 108.47 Mb PubMed search
Wikidata
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Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene.

Function

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.

Further reading

• 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.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.