P4HA2

P4HA2
Identifiers
Aliases	P4HA2, prolyl 4-hydroxylase subunit alpha 2, MYP25, lncRNA-PE
External IDs	OMIM: 600608 MGI: 894286 HomoloGene: 55806 GeneCards: P4HA2
Gene location (Human) Chr. Chromosome 5 (human) Band 5q31.1 Start 132,190,147 bp End 132,295,315 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B1.3|11 32.13 cM Start 53,990,921 bp End 54,022,491 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium tibia body of pancreas islet of Langerhans bronchial epithelial cell smooth muscle tissue corpus epididymis ascending aorta periodontal fiber pituitary gland Top expressed in molar calvaria belly cord body of femur right lung lobe otic placode yolk sac placenta saccule uterus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding electron transfer activity L-ascorbic acid binding oxidoreductase activity protein binding oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen dioxygenase activity procollagen-proline 4-dioxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen metal ion binding Cellular component endoplasmic reticulum intracellular membrane-bounded organelle endoplasmic reticulum lumen nucleoplasm cytosol Biological process peptidyl-proline hydroxylation electron transport chain peptidyl-proline hydroxylation to 4-hydroxy-L-proline Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8974 18452 Ensembl ENSG00000072682 ENSMUSG00000018906 UniProt O15460 Q60716 RefSeq (mRNA) NM_001017974 NM_001142598 NM_001142599 NM_004199 NM_001365677 NM_001365678 NM_001365679 NM_001365680 NM_001365681 NM_001136076 NM_011031 RefSeq (protein) NP_001017974 NP_001136070 NP_001136071 NP_004190 NP_001352606 NP_001352607 NP_001352608 NP_001352609 NP_001352610 NP_001129548 NP_035161 Location (UCSC) Chr 5: 132.19 – 132.3 Mb Chr 11: 53.99 – 54.02 Mb PubMed search
Wikidata
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Prolyl 4-hydroxylase subunit alpha-2 is an enzyme that in humans is encoded by the P4HA2 gene.

This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits. The encoded protein is one of several different types of alpha subunits and provides the major part of the catalytic site of the active enzyme. In collagen and related proteins, prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline that is essential to the proper three-dimensional folding of newly synthesized procollagen chains. Alternatively spliced transcript variants encoding different isoforms have been described.

References

Notes

Further reading

• Helaakoski T, Annunen P, Vuori K, et al. (1995). "Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit". Proc. Natl. Acad. Sci. U.S.A. 92 (10): 4427–31. Bibcode:1995PNAS...92.4427H. doi:10.1073/pnas.92.10.4427. PMC 41957. PMID 7753822.
• Nokelainen M, Nissi R, Kukkola L, et al. (2001). "Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues". Eur. J. Biochem. 268 (20): 5300–9. doi:10.1046/j.0014-2956.2001.02464.x. PMID 11606192.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Hieta R, Kukkola L, Permi P, et al. (2003). "The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides". J. Biol. Chem. 278 (37): 34966–74. doi:10.1074/jbc.M303624200. PMID 12824157.
• Kukkola L, Hieta R, Kivirikko KI, Myllyharju J (2004). "Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme". J. Biol. Chem. 278 (48): 47685–93. doi:10.1074/jbc.M306806200. PMID 14500733.
• Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Grimmer C, Balbus N, Lang U, et al. (2006). "Regulation of Type II Collagen Synthesis during Osteoarthritis by Prolyl-4-Hydroxylases : Possible Influence of Low Oxygen Levels". Am. J. Pathol. 169 (2): 491–502. doi:10.2353/ajpath.2006.050738. PMC 1698781. PMID 16877351.
• Koivunen P, Hirsilä M, Kivirikko KI, Myllyharju J (2006). "The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases". J. Biol. Chem. 281 (39): 28712–20. doi:10.1074/jbc.M604628200. PMID 16885164.
• Teodoro JG, Parker AE, Zhu X, Green MR (2006). "p53-mediated inhibition of angiogenesis through up-regulation of a collagen prolyl hydroxylase". Science. 313 (5789): 968–71. Bibcode:2006Sci...313..968T. doi:10.1126/science.1126391. PMID 16917063. S2CID 34727093.