P4HA2: Difference between revisions

P4HA2
Identifiers
Aliases	P4HA2, prolyl 4-hydroxylase subunit alpha 2, MYP25, lncRNA-PE
External IDs	OMIM: 600608; MGI: 894286; HomoloGene: 55806; GeneCards: P4HA2; OMA:P4HA2 - orthologs
Gene location (Human)
Chr.	Chromosome 5 (human)
End	132,295,315 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	54,022,491 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; tibia; ; body of pancreas; ; islet of Langerhans; ; bronchial epithelial cell; ; cartilage tissue; ; apex of heart; ; smooth muscle tissue; ; right auricle; ; corpus epididymis;
	Top expressed in
	molar; ; calvaria; ; epithelium of lens; ; belly cord; ; gastrula; ; body of femur; ; stroma of bone marrow; ; right lung lobe; ; otic placode; ; muscle of thigh;
	More reference expression data
	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
	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

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Revision as of 15:06, 3 June 2016

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

Template:PBB Summary

References

Notes

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000072682 – Ensembl, May 2017
^ ^a ^b ^c 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.
^ Cite error: The named reference entrez was invoked but never defined (see the help page).

Further reading

Template:PBB Further reading

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This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

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

[refGRCm38Ensembl-2] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[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] Cite error: The named reference entrez was invoked but never defined (see the help page).

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+{{Multiple issues|
+{{Underlinked|date=June 2016}}
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-'''Prolyl 4-hydroxylase subunit alpha-2''' is an [[enzyme]] that in humans is encoded by the ''P4HA2'' [[gene]].<ref name="pmid9211872">{{cite journal | author = Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI | title = 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 | journal = J Biol Chem | volume = 272 | issue = 28 | pages = 17342–8 |date=Aug 1997 | pmid = 9211872 | pmc =  | doi =10.1074/jbc.272.28.17342  }}</ref><ref name="pmid9149945">{{cite journal | author = Frazer KA, Ueda Y, Zhu Y, Gifford VR, Garofalo MR, Mohandas N, Martin CH, Palazzolo MJ, Cheng JF, Rubin EM | title = Computational and biological analysis of 680 kb of DNA sequence from the human 5q31 cytokine gene cluster region | journal = Genome Res | volume = 7 | issue = 5 | pages = 495–512 |date=Aug 1997 | pmid = 9149945 | pmc =  | doi =  10.1101/gr.7.5.495}}</ref><ref name="entrez"/>
+'''Prolyl 4-hydroxylase subunit alpha-2''' is an [[enzyme]] that in humans is encoded by the ''P4HA2'' [[gene]].<ref name="pmid9211872">{{cite journal | vauthors = Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI | title = 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 | journal = J Biol Chem | volume = 272 | issue = 28 | pages = 17342–8 |date=Aug 1997 | pmid = 9211872 | pmc =  | doi =10.1074/jbc.272.28.17342  }}</ref><ref name="pmid9149945">{{cite journal | vauthors = Frazer KA, Ueda Y, Zhu Y, Gifford VR, Garofalo MR, Mohandas N, Martin CH, Palazzolo MJ, Cheng JF, Rubin EM | title = Computational and biological analysis of 680 kb of DNA sequence from the human 5q31 cytokine gene cluster region | journal = Genome Res | volume = 7 | issue = 5 | pages = 495–512 |date=Aug 1997 | pmid = 9149945 | pmc =  | doi =  10.1101/gr.7.5.495}}</ref><ref name="entrez"/>
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 *{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
 *{{cite journal   |vauthors=Hieta R, Kukkola L, Permi P, etal |title=The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 34966–74 |year= 2003 |pmid= 12824157 |doi= 10.1074/jbc.M303624200 }}
-*{{cite journal  | author=Kukkola L, Hieta R, Kivirikko KI, Myllyharju J |title=Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 47685–93 |year= 2004 |pmid= 14500733 |doi= 10.1074/jbc.M306806200 }}
+*{{cite journal  | vauthors=Kukkola L, Hieta R, Kivirikko KI, Myllyharju J |title=Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 47685–93 |year= 2004 |pmid= 14500733 |doi= 10.1074/jbc.M306806200 }}
 *{{cite journal   |vauthors=Lehner B, Semple JI, Brown SE, etal |title=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 |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=10.1016/S0888-7543(03)00235-0  }}
 *{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
 *{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 }}
 *{{cite journal   |vauthors=Grimmer C, Balbus N, Lang U, etal |title=Regulation of Type II Collagen Synthesis during Osteoarthritis by Prolyl-4-Hydroxylases : Possible Influence of Low Oxygen Levels |journal=Am. J. Pathol. |volume=169 |issue= 2 |pages= 491–502 |year= 2006 |pmid= 16877351 |doi=10.2353/ajpath.2006.050738  | pmc=1698781  }}
-*{{cite journal  | author=Koivunen P, Hirsilä M, Kivirikko KI, Myllyharju J |title=The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases |journal=J. Biol. Chem. |volume=281 |issue= 39 |pages= 28712–20 |year= 2006 |pmid= 16885164 |doi= 10.1074/jbc.M604628200 }}
+*{{cite journal  | vauthors=Koivunen P, Hirsilä M, Kivirikko KI, Myllyharju J |title=The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases |journal=J. Biol. Chem. |volume=281 |issue= 39 |pages= 28712–20 |year= 2006 |pmid= 16885164 |doi= 10.1074/jbc.M604628200 }}
-*{{cite journal  | author=Teodoro JG, Parker AE, Zhu X, Green MR |title=p53-mediated inhibition of angiogenesis through up-regulation of a collagen prolyl hydroxylase |journal=Science |volume=313 |issue= 5789 |pages= 968–71 |year= 2006 |pmid= 16917063 |doi= 10.1126/science.1126391 }}
+*{{cite journal  | vauthors=Teodoro JG, Parker AE, Zhu X, Green MR |title=p53-mediated inhibition of angiogenesis through up-regulation of a collagen prolyl hydroxylase |journal=Science |volume=313 |issue= 5789 |pages= 968–71 |year= 2006 |pmid= 16917063 |doi= 10.1126/science.1126391 }}
 }}
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