Nothing Special   »   [go: up one dir, main page]

Jump to content

P4HA2: Difference between revisions

From Wikipedia, the free encyclopedia
Content deleted Content added
m general clean up, added orphan tag using AWB
Importing Wikidata short description: "Protein-coding gene in the species Homo sapiens"
 
(15 intermediate revisions by 10 users not shown)
Line 1: Line 1:
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Orphan|date=October 2015}}


{{PBB|geneid=8974}}
{{Infobox_gene}}


'''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 | doi =10.1074/jbc.272.28.17342 | doi-access = free }}</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 | doi = 10.1101/gr.7.5.495| doi-access = free }}</ref><ref name="entrez"/>


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.<ref name="entrez">{{cite web | title = Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8974}}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8974| accessdate = }}</ref>
}}


==References==
==References==
Line 17: Line 13:
'''Further reading'''
'''Further reading'''
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal |vauthors=Helaakoski T, Annunen P, Vuori K, etal |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 10 |pages= 4427–31 |year= 1995 |pmid= 7753822 |doi=10.1073/pnas.92.10.4427 | pmc=41957 |bibcode=1995PNAS...92.4427H |doi-access=free }}
{{PBB_Further_reading
*{{cite journal |vauthors=Nokelainen M, Nissi R, Kukkola L, etal |title=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 |journal=Eur. J. Biochem. |volume=268 |issue= 20 |pages= 5300–9 |year= 2001 |pmid= 11606192 |doi=10.1046/j.0014-2956.2001.02464.x |doi-access=free }}
| citations =
*{{cite journal |vauthors=Helaakoski T, Annunen P, Vuori K, etal |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 10 |pages= 4427–31 |year= 1995 |pmid= 7753822 |doi=10.1073/pnas.92.10.4427 | pmc=41957 }}
*{{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 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal |vauthors=Nokelainen M, Nissi R, Kukkola L, etal |title=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 |journal=Eur. J. Biochem. |volume=268 |issue= 20 |pages= 5300–9 |year= 2001 |pmid= 11606192 |doi=10.1046/j.0014-2956.2001.02464.x }}
*{{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 |doi-access= free }}
*{{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=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 |doi-access= free }}
*{{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=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=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=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=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 |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 |doi-access= free }}
*{{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 |bibcode=2006Sci...313..968T |s2cid=34727093 }}
}}
{{refend}}
{{refend}}


<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}





Latest revision as of 09:51, 17 October 2022

P4HA2
Identifiers
AliasesP4HA2, prolyl 4-hydroxylase subunit alpha 2, MYP25, lncRNA-PE
External IDsOMIM: 600608; MGI: 894286; HomoloGene: 55806; GeneCards: P4HA2; OMA:P4HA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001136076
NM_011031

RefSeq (protein)

NP_001129548
NP_035161

Location (UCSC)Chr 5: 132.19 – 132.3 MbChr 11: 53.99 – 54.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

References

[edit]

Notes

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000072682Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018906Ensembl, 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. ^ 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.
  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.
  7. ^ a b "Entrez Gene: P4HA2 procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), alpha polypeptide II".

Further reading