Protein-coding gene in the species Homo sapiens
P4HTM |
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Identifiers |
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Aliases | P4HTM, EGLN4, HIFPH4, P4H-TM, PH-4, PH4, PHD4, prolyl 4-hydroxylase, transmembrane, HIDEA |
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External IDs | OMIM: 614584; MGI: 1921693; HomoloGene: 41765; GeneCards: P4HTM; OMA:P4HTM - orthologs |
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Gene location (Human) |
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![Chromosome 3 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/3/39/Ideogram_human_chromosome_3.svg/300px-Ideogram_human_chromosome_3.svg.png) | Chr. | Chromosome 3 (human)[1] |
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| Band | 3p21.31|3p21.3 | Start | 48,989,889 bp[1] |
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End | 49,007,153 bp[1] |
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Gene location (Mouse) |
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![Chromosome 9 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/4/41/Ideogram_house_mouse_chromosome_9.svg/260px-Ideogram_house_mouse_chromosome_9.svg.png) | Chr. | Chromosome 9 (mouse)[2] |
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| Band | 9|9 F2 | Start | 108,456,061 bp[2] |
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End | 108,474,866 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - right uterine tube
- bronchial epithelial cell
- pituitary gland
- anterior pituitary
- prefrontal cortex
- right frontal lobe
- right hemisphere of cerebellum
- Brodmann area 9
- nucleus accumbens
- anterior cingulate cortex
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| Top expressed in | - substantia nigra
- nucleus accumbens
- temporal lobe
- facial motor nucleus
- prefrontal cortex
- ventromedial nucleus
- central gray substance of midbrain
- lateral septal nucleus
- anterior amygdaloid area
- paraventricular nucleus of hypothalamus
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| More reference expression data |
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BioGPS | |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | |
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NM_017732 NM_177938 NM_177939 |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 3: 48.99 – 49.01 Mb | Chr 9: 108.46 – 108.47 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene. [5]
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.
References
- ^ 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
- 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.