P4HTM

Protein-coding gene in the species Homo sapiens
P4HTM
Identifiers
AliasesP4HTM, EGLN4, HIFPH4, P4H-TM, PH-4, PH4, PHD4, prolyl 4-hydroxylase, transmembrane, HIDEA
External IDsOMIM: 614584; MGI: 1921693; HomoloGene: 41765; GeneCards: P4HTM; OMA:P4HTM - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for P4HTM
Genomic location for P4HTM
Band3p21.31|3p21.3Start48,989,889 bp[1]
End49,007,153 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for P4HTM
Genomic location for P4HTM
Band9|9 F2Start108,456,061 bp[2]
End108,474,866 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
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
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
SpeciesHumanMouse
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 MbChr 9: 108.46 – 108.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000178467 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000006675 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "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.


  • v
  • t
  • e

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