P4HA2

P4HA2
Identifiers
Aliases	P4HA2 , prolyl 4-hydroxylase subunit alpha 2, MYP25
External IDs	OMIM: 600608 MGI: 894286 HomoloGene: 55806 GeneCards: P4HA2
Gene location (Human)
Chr.	Chromosome 5 (human)
End	132,295,315 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	54,131,665 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• iron ion binding ; • electron transfer activity ; • L-ascorbic acid binding ; • oxidoreductase activity ; • GO:0001948 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
	8974
	18452
	ENSG00000072682
	ENSMUSG00000018906
	O15460
	Q60716
NM_001017974 ; NM_001142598 ; NM_001142599 ; NM_004199 ; NM_001365677 ;
	NM_001365678 ; NM_001365679 ; NM_001365680 ; NM_001365681
	NM_001136076 ; NM_011031
NP_001017974 ; NP_001136070 ; NP_001136071 ; NP_004190 ; NP_001352606 ;
	NP_001352607 ; NP_001352608 ; NP_001352609 ; NP_001352610
	NP_001129548 ; NP_035161
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 13, 2021

Prolyl 4-hydroxylase subunit alpha-2 is an enzyme that in humans is encoded by the P4HA2 gene.^[5]^[6]^[7]

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.^[7]

Related Research Articles

Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases. These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe²⁺, and ascorbate. This particular enzyme catalyzes the formation of (2S, 4R)-4-hydroxyproline, a compound that represents the most prevalent post-translational modification in the human proteome.

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit is an enzyme that in humans is encoded by the PPP1CC gene.

Protein disulfide-isomerase, also known as the beta-subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans encoded by the P4HB gene. The human P4HB gene is localized in chromosome 17q25. Unlike other prolyl 4-hydroxylase family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB is tightly regulated. Both dimer dissociation and substrate binding are likely to enhance its enzymatic activity during the catalysis process.

5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 gene.

Collagen alpha-1(VI) chain is a protein that in humans is encoded by the COL6A1 gene.

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

Collagen alpha-2(VI) chain is a protein that in humans is encoded by the COL6A2 gene.

Egl nine homolog 2 is a protein that in humans is encoded by the EGLN2 gene. ELGN2 is an alpha-ketoglutarate-dependent hydroxylase, a superfamily of non-haem iron-containing proteins.

Hypoxia-inducible factor prolyl hydroxylase 2 (HIF-PH2), or prolyl hydroxylase domain-containing protein 2 (PHD2), is an enzyme encoded by the EGLN1 gene. It is also known as Egl nine homolog 1. PHD2 is a α-ketoglutarate/2-oxoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins. In humans, PHD2 is one of the three isoforms of hypoxia-inducible factor-proline dioxygenase, which is also known as HIF prolyl-hydroxylase.

Voltage-gated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNAB1 gene.

Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene.

Acetylcholinesterase collagenic tail peptide also known as AChE Q subunit, acetylcholinesterase-associated collagen, or ColQ is the collagen-tail subunit of acetylcholinesterase found in the neuromuscular junction. In humans it is encoded by the COLQ gene.

Collagen alpha-1(XIII) chain is a protein that in humans is encoded by the COL13A1 gene.

Collagen alpha-1(XIX) chain is a protein that in humans is encoded by the COL19A1 gene.

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 is a protein that in humans is encoded by the GNG3 gene.

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.

Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial is an enzyme that in humans is encoded by the IDH3B gene.

Calcium-activated potassium channel subunit beta-4 is a protein that in humans is encoded by the KCNMB4 gene.

Collagen alpha-1(XXVI) chain is a protein that in humans is encoded by the EMID2 gene.

Prolyl 4-hydroxylase, transmembrane is a protein that in humans is encoded by the P4HTM gene.

References

Notes

1 2 3 GRCh38: Ensembl release 89: ENSG00000072682 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000018906 - 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.
↑ Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI (Aug 1997). "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer". J Biol Chem. 272 (28): 17342–8. doi: 10.1074/jbc.272.28.17342 . PMID 9211872.
↑ Frazer KA, Ueda Y, Zhu Y, Gifford VR, Garofalo MR, Mohandas N, Martin CH, Palazzolo MJ, Cheng JF, Rubin EM (Aug 1997). "Computational and biological analysis of 680 kb of DNA sequence from the human 5q31 cytokine gene cluster region". Genome Res. 7 (5): 495–512. doi: 10.1101/gr.7.5.495 . PMID 9149945.
1 2 "Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II".

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. 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. 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. doi:10.1126/science.1126391. PMID 16917063. S2CID 34727093.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000072682 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000018906 - 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.

[pmid9211872-5] Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI (Aug 1997). "Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer". J Biol Chem. 272 (28): 17342–8. doi: 10.1074/jbc.272.28.17342 . PMID 9211872.

[pmid9149945-6] Frazer KA, Ueda Y, Zhu Y, Gifford VR, Garofalo MR, Mohandas N, Martin CH, Palazzolo MJ, Cheng JF, Rubin EM (Aug 1997). "Computational and biological analysis of 680 kb of DNA sequence from the human 5q31 cytokine gene cluster region". Genome Res. 7 (5): 495–512. doi: 10.1101/gr.7.5.495 . PMID 9149945.

[entrez-7] 1 2 "Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II".

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