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{{Infobox_gene}}
{{Infobox_gene}}
'''Cytochrome c oxidase subunit 4 isoform 1, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''COX4I1'' [[gene]].<ref name="pmid2444497">{{cite journal | vauthors = Zeviani M, Nakagawa M, Herbert J, Lomax MI, Grossman LI, Sherbany AA, Miranda AF, DiMauro S, Schon EA | title = Isolation of a cDNA clone encoding subunit IV of human cytochrome c oxidase | journal = Gene | volume = 55 | issue = 2–3 | pages = 205–17 |date=Dec 1987 | pmid = 2444497 | pmc =  | doi =10.1016/0378-1119(87)90281-2 }}</ref><ref name="pmid2157630">{{cite journal | vauthors = Lomax MI, Welch MD, Darras BT, Francke U, Grossman LI | title = Novel use of a chimpanzee pseudogene for chromosomal mapping of human cytochrome c oxidase subunit IV | journal = Gene | volume = 86 | issue = 2 | pages = 209–16 |date=May 1990 | pmid = 2157630 | pmc =  | doi =10.1016/0378-1119(90)90281-U }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: COX4I1 cytochrome c oxidase subunit IV isoform 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1327| accessdate = }}</ref>
'''Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (COX4I1)''' is an [[enzyme]] that in humans is encoded by the ''COX4I1'' [[gene]]. COX4I1 is a nuclear-encoded [[Protein isoform|isoform]] of [[cytochrome c oxidase]] (COX) [[Protein subunit|subunit]] 4. Cytochrome c oxidase ([[Cytochrome c oxidase|complex IV]]) is a multi-subunit enzyme complex that couples the transfer of [[electron]]s from [[cytochrome c]] to molecular [[oxygen]] and contributes to a [[hydronium|proton]] [[electrochemical gradient]] across the [[inner mitochondrial membrane]], acting as the terminal enzyme of the [[Mitochondrion|mitochondrial]] [[electron transport chain|respiratory chain]].<ref name="entrez">{{cite web|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1327|title=Entrez Gene: COX4I1 cytochrome c oxidase subunit IV isoform 1|access-date=}}{{PD-notice}}</ref><ref name="pmid2444497">{{cite journal | vauthors = Zeviani M, Nakagawa M, Herbert J, Lomax MI, Grossman LI, Sherbany AA, Miranda AF, DiMauro S, Schon EA | title = Isolation of a cDNA clone encoding subunit IV of human cytochrome c oxidase | journal = Gene | volume = 55 | issue = 2-3 | pages = 205–17 | date = Dec 1987 | pmid = 2444497 | pmc =  | doi = 10.1016/0378-1119(87)90281-2 }}</ref><ref name="pmid2157630">{{cite journal | vauthors = Lomax MI, Welch MD, Darras BT, Francke U, Grossman LI | title = Novel use of a chimpanzee pseudogene for chromosomal mapping of human cytochrome c oxidase subunit IV | journal = Gene | volume = 86 | issue = 2 | pages = 209–16 | date = February 1990 | pmid = 2157630 | pmc =  | doi = 10.1016/0378-1119(90)90281-U }}</ref> [[Antibody|Antibodies]] against COX4 can be used to identify the inner membrane of [[Mitochondrion|mitochondria]] in [[Immunofluorescence|immunfluorescence]] studies.<ref>http://www.genetex.com/WebPage/Product/ProductDetail.aspx?catno=GTX101499&CampaignId=</ref> Mutations in COX4I1 have been associated with COX deficiency and [[Fanconi anemia]].<ref name=":1" /><ref name=":2" />


[[Cytochrome c oxidase]] (COX) is the terminal enzyme of the [[Mitochondrion|mitochondrial]] [[electron transport chain|respiratory chain]]. It is a multi-subunit enzyme complex that couples the transfer of [[electron]]s from [[cytochrome c]] to molecular [[oxygen]] and contributes to a [[hydronium|proton]] [[electrochemical gradient]] across the inner [[mitochondrial membrane]]. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the [[electron transfer]] and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit IV [[protein isoform|isoform]] 1 of the human mitochondrial respiratory chain enzyme. It is located at the 3' of the [[COX4NB|NOC4]] (neighbor of COX4) gene in a head-to-head orientation, and shares a promoter with it.<ref name="entrez" /> Antibodies against Cox4 can be used to identify the inner membrane of mitochondria in immunfluorescence studies.<ref>http://www.genetex.com/WebPage/Product/ProductDetail.aspx?catno=GTX101499&CampaignId=</ref>
== Structure ==
''COX4I1'' is located on the [[Locus (genetics)|q arm]] of [[chromosome 16]] in position 24.1 and has 6 [[exon]]s.<ref name="entrez" /> The ''COX4I1'' gene produces a 9.3 kDa [[protein]] composed of 83 [[amino acid]]s.<ref>{{Cite web|url=https://amino.heartproteome.org/web/protein/Q86WV2|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information|last=Yao|first=Daniel|website=amino.heartproteome.org|access-date=2018-08-03}}</ref><ref>{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–53 | date = October 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}</ref> ''COX4I1'' is expressed ubiquitously. The protein encoded by ''COX4I1'' belongs to the cytochrome c oxidase IV family. COX4I1 has a [[Signal peptide|transit peptide]] domain and [[acetyl]] and [[phosphoprotein]] [[amino acid]] modifications.<ref>{{Cite web|url=https://www.uniprot.org/uniprot/P13073|title=COX4I1 - Cytochrome c oxidase subunit 4 isoform 1, mitochondrial precursor - Homo sapiens (Human) - COX4I1 gene & protein|website=uniprot.org|language=en|access-date=2018-08-03}}{{CC-notice|cc=by4}}</ref><ref name=":3">{{cite journal | vauthors =  | title = UniProt: the universal protein knowledgebase | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D158-D169 | date = January 2017 | pmid = 27899622 | pmc = 5210571 | doi = 10.1093/nar/gkw1099 | url = https://doi.org/10.1093/nar/gkw1099 }}</ref> It is located at the [[3']] of the [[COX4NB|NOC4]] (neighbor of COX4) gene in a head-to-head orientation, and shares a [[Promoter (genetics)|promoter]] with it.<ref name="entrez" />


==References==
== Function ==
''COX4I1'' encodes a protein that is located in the [[inner mitochondrial membrane]] and is an isoform of the nuclear-encoded subunit IV of [[cytochrome c oxidase]] (complex IV), the terminal [[oxidase]] in [[Electron transport chain|mitochondrial electron transport]]. Complex IV is a multi-subunit enzyme complex that couples the transfer of [[electron]]s from [[cytochrome c]] to molecular [[oxygen]] and contributes to a [[hydronium|proton]] [[electrochemical gradient]] across the [[inner mitochondrial membrane]].<ref name="entrez" /> The expression of COX4I1, along with [[COX4I2]], may be regulated by oxygen levels, with reduced levels of oxygen leading to increased COX4I2 expression and COX4I1 degradation. This suggests a role for COX4I1 in the optimization of the electron transfer chain under different conditions.<ref name=":0">{{cite journal | vauthors = Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL | title = HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells | journal = Cell | volume = 129 | issue = 1 | pages = 111–22 | date = April 2007 | pmid = 17418790 | doi = 10.1016/j.cell.2007.01.047 }}</ref>
 
== Clinical Significance ==
Although relatively little is known about the function of ''COX4I1'', mutations in this gene have been associated with mitochondrial complex IV diseases with severe [[phenotype]]s. Among these, COX deficiency and [[Fanconi anemia]] have been suspected and linked to mutations in the ''COX4I1'' gene. Clinical features of pathogenic variants of ''COX4I1'' can include [[short stature]], poor weight gain, mild [[dysmorphic feature]]s, [[Intellectual disability|mental retardation]], [[Hereditary spastic paraplegia|spastic paraplegia]], severe [[epilepsy]], a narrow and arched [[palate]], malar hypoplasia, little [[Subcutaneous tissue|subcutaneous fat]], and [[arachnodactyly]]. The homozygous [[mutation]] K101N and a de novo 16q24.1 interstitial duplication have been found to cause defective COX4I1.<ref name=":1">{{cite journal | vauthors = Abu-Libdeh B, Douiev L, Amro S, Shahrour M, Ta-Shma A, Miller C, Elpeleg O, Saada A | title = Mutation in the COX4I1 gene is associated with short stature, poor weight gain and increased chromosomal breaks, simulating Fanconi anemia | journal = European Journal of Human Genetics | volume = 25 | issue = 10 | pages = 1142–1146 | date = October 2017 | pmid = 28766551 | pmc = 5602013 | doi = 10.1038/ejhg.2017.112 }}</ref><ref name=":2">{{cite journal | vauthors = Quéméner-Redon S, Bénech C, Audebert-Bellanger S, Friocourt G, Planes M, Parent P, Férec C | title = A small de novo 16q24.1 duplication in a woman with severe clinical features | journal = European Journal of Medical Genetics | volume = 56 | issue = 4 | pages = 211–5 | date = April 2013 | pmid = 23333879 | doi = 10.1016/j.ejmg.2013.01.001 }}</ref>
 
== Interactions ==
COX4I1 has 153 protein-protein interactions with 142 of them being co-complex interactions. COX4I1 has been found to interact with [[Syntenin-1|SDCBP]], [[Cytochrome c oxidase subunit I|MT-CO1]], [[IKBKE]], [[TMBIM4]], and [[MCL1]].<ref>{{cite web | url = https://www.ebi.ac.uk/intact/interactions?conversationContext=3&query=COX4I1 | title = 153 binary interactions found for search term COX4I1 | work = IntAct Molecular Interaction Database | publisher = EMBL-EBI | access-date = 2018-08-25 }}</ref>
[[Lon protease family|LON]], a mitochondrial [[protease]], has also been suggested to regulate the COX4 subunit isoforms by degrading COX4I1 under [[Hypoxic tissue|hypoxic]] conditions.<ref name=":0" />
 
== References ==
{{reflist}}
{{reflist}}


==External links==
== External links ==
* {{UCSC gene info|COX4I1}}
* {{UCSC gene info|COX4I1}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal | author=Lithgow T |title=Targeting of proteins to mitochondria |journal=FEBS Lett. |volume=476 |issue= 1–2 |pages= 22–6 |year= 2000 |pmid= 10878243 |doi=10.1016/S0014-5793(00)01663-X }}
* {{cite journal | vauthors = Kim MJ, Jardel C, Barthélémy C, Jan V, Bastard JP, Fillaut-Chapin S, Houry S, Capeau J, Lombès A | title = Mitochondrial DNA content, an inaccurate biomarker of mitochondrial alteration in human immunodeficiency virus-related lipodystrophy | journal = Antimicrobial Agents and Chemotherapy | volume = 52 | issue = 5 | pages = 1670–6 | date = May 2008 | pmid = 18332166 | pmc = 2346614 | doi = 10.1128/AAC.01449-07 | url = http://aac.asm.org/content/52/5/1670 }}
*{{cite journal | vauthors=Van Kuilenburg AB, Van Beeumen JJ, Demol H |title=Subunit IV of human cytochrome c oxidase, polymorphism and a putative isoform |journal=Biochim. Biophys. Acta |volume=1119 |issue= 2 |pages= 218–24 |year= 1992 |pmid= 1311608 |doi=10.1016/0167-4838(92)90395-T |display-authors=etal}}
* {{cite journal | vauthors = Lithgow T | title = Targeting of proteins to mitochondria | journal = FEBS Letters | volume = 476 | issue = 1-2 | pages = 22–6 | date = June 2000 | pmid = 10878243 | doi = 10.1016/S0014-5793(00)01663-X }}
*{{cite journal  | vauthors=Lomax MI, Hewett-Emmett D, Yang TL, Grossman LI |title=Rapid evolution of the human gene for cytochrome c oxidase subunit IV |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 12 |pages= 5266–70 |year= 1992 |pmid= 1319058 |doi=10.1073/pnas.89.12.5266  | pmc=49272  }}
* {{cite journal | vauthors = Van Kuilenburg AB, Van Beeumen JJ, Demol H, Van den Bogert C, Schouten I, Muijsers AO | title = Subunit IV of human cytochrome c oxidase, polymorphism and a putative isoform | journal = Biochimica et Biophysica Acta | volume = 1119 | issue = 2 | pages = 218–24 | date = February 1992 | pmid = 1311608 | doi = 10.1016/0167-4838(92)90395-T }}
*{{cite journal | vauthors=Romero N, Marsac C, Fardeau M |title=Immunohistochemical demonstration of fibre type-specific isozymes of cytochrome c oxidase in human skeletal muscle |journal=Histochemistry |volume=94 |issue= 2 |pages= 211–5 |year= 1990 |pmid= 2162812 |doi=10.1007/BF02440190 |display-authors=etal}}
* {{cite journal | vauthors = Romero N, Marsac C, Fardeau M, Droste M, Schneyder B, Kadenbach B | title = Immunohistochemical demonstration of fibre type-specific isozymes of cytochrome c oxidase in human skeletal muscle | journal = Histochemistry | volume = 94 | issue = 2 | pages = 211–5 | year = 1990 | pmid = 2162812 | doi = 10.1007/BF02440190 }}
*{{cite journal | vauthors=Bonne G, Seibel P, Possekel S |title=Expression of human cytochrome c oxidase subunits during fetal development |journal=Eur. J. Biochem. |volume=217 |issue= 3 |pages= 1099–107 |year= 1993 |pmid= 8223633 |doi=10.1111/j.1432-1033.1993.tb18342.x |display-authors=etal}}
* {{cite journal | vauthors = Bonne G, Seibel P, Possekel S, Marsac C, Kadenbach B | title = Expression of human cytochrome c oxidase subunits during fetal development | journal = European Journal of Biochemistry | volume = 217 | issue = 3 | pages = 1099–107 | date = November 1993 | pmid = 8223633 | doi = 10.1111/j.1432-1033.1993.tb18342.x }}
*{{cite journal | vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}}
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–13 | date = April 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
*{{cite journal | vauthors=Wu W, Goodman M, Lomax MI, Grossman LI |title=Molecular evolution of cytochrome c oxidase subunit IV: evidence for positive selection in simian primates |journal=J. Mol. Evol. |volume=44 |issue= 5 |pages= 477–91 |year= 1997 |pmid= 9115172 |doi=10.1007/PL00006172 }}
* {{cite journal | vauthors = Wu W, Goodman M, Lomax MI, Grossman LI | title = Molecular evolution of cytochrome c oxidase subunit IV: evidence for positive selection in simian primates | journal = Journal of Molecular Evolution | volume = 44 | issue = 5 | pages = 477–91 | date = May 1997 | pmid = 9115172 | doi = 10.1007/PL00006172 }}
*{{cite journal | vauthors=Bachman NJ, Wu W, Schmidt TR |title=The 5' region of the COX4 gene contains a novel overlapping gene, NOC4 |journal=Mamm. Genome |volume=10 |issue= 5 |pages= 506–12 |year= 1999 |pmid= 10337626 |doi=10.1007/s003359901031 |display-authors=etal}}
* {{cite journal | vauthors = Bachman NJ, Wu W, Schmidt TR, Grossman LI, Lomax MI | title = The 5' region of the COX4 gene contains a novel overlapping gene, NOC4 | journal = Mammalian Genome | volume = 10 | issue = 5 | pages = 506–12 | date = May 1999 | pmid = 10337626 | doi = 10.1007/s003359901031 }}
*{{cite journal | vauthors=Hüttemann M, Kadenbach B, Grossman LI |title=Mammalian subunit IV isoforms of cytochrome c oxidase |journal=Gene |volume=267 |issue= 1 |pages= 111–23 |year= 2001 |pmid= 11311561 |doi=10.1016/S0378-1119(01)00385-7 }}
* {{cite journal | vauthors = Hüttemann M, Kadenbach B, Grossman LI | title = Mammalian subunit IV isoforms of cytochrome c oxidase | journal = Gene | volume = 267 | issue = 1 | pages = 111–23 | date = April 2001 | pmid = 11311561 | doi = 10.1016/S0378-1119(01)00385-7 }}
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
* {{cite journal | vauthors = Williams SL, Valnot I, Rustin P, Taanman JW | title = Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1 | journal = The Journal of Biological Chemistry | volume = 279 | issue = 9 | pages = 7462–9 | date = February 2004 | pmid = 14607829 | doi = 10.1074/jbc.M309232200 }}
*{{cite journal  | vauthors=Williams SL, Valnot I, Rustin P, Taanman JW |title=Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1 |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 7462–9 |year= 2004 |pmid= 14607829 |doi= 10.1074/jbc.M309232200 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |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 |display-authors=etal}}
*{{cite journal  | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948 |display-authors=etal}}
*{{cite journal  | vauthors=Fukuda R, Zhang H, Kim JW |title=HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells |journal=Cell |volume=129 |issue= 1 |pages= 111–22 |year= 2007 |pmid= 17418790 |doi= 10.1016/j.cell.2007.01.047 |display-authors=etal}}
{{refend}}
{{refend}}


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Revision as of 17:14, 8 September 2018

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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UniProt

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Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (COX4I1) is an enzyme that in humans is encoded by the COX4I1 gene. COX4I1 is a nuclear-encoded isoform of cytochrome c oxidase (COX) subunit 4. Cytochrome c oxidase (complex IV) is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane, acting as the terminal enzyme of the mitochondrial respiratory chain.[1][2][3] Antibodies against COX4 can be used to identify the inner membrane of mitochondria in immunfluorescence studies.[4] Mutations in COX4I1 have been associated with COX deficiency and Fanconi anemia.[5][6]

Structure

COX4I1 is located on the q arm of chromosome 16 in position 24.1 and has 6 exons.[1] The COX4I1 gene produces a 9.3 kDa protein composed of 83 amino acids.[7][8] COX4I1 is expressed ubiquitously. The protein encoded by COX4I1 belongs to the cytochrome c oxidase IV family. COX4I1 has a transit peptide domain and acetyl and phosphoprotein amino acid modifications.[9][10] It is located at the 3' of the NOC4 (neighbor of COX4) gene in a head-to-head orientation, and shares a promoter with it.[1]

Function

COX4I1 encodes a protein that is located in the inner mitochondrial membrane and is an isoform of the nuclear-encoded subunit IV of cytochrome c oxidase (complex IV), the terminal oxidase in mitochondrial electron transport. Complex IV is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane.[1] The expression of COX4I1, along with COX4I2, may be regulated by oxygen levels, with reduced levels of oxygen leading to increased COX4I2 expression and COX4I1 degradation. This suggests a role for COX4I1 in the optimization of the electron transfer chain under different conditions.[11]

Clinical Significance

Although relatively little is known about the function of COX4I1, mutations in this gene have been associated with mitochondrial complex IV diseases with severe phenotypes. Among these, COX deficiency and Fanconi anemia have been suspected and linked to mutations in the COX4I1 gene. Clinical features of pathogenic variants of COX4I1 can include short stature, poor weight gain, mild dysmorphic features, mental retardation, spastic paraplegia, severe epilepsy, a narrow and arched palate, malar hypoplasia, little subcutaneous fat, and arachnodactyly. The homozygous mutation K101N and a de novo 16q24.1 interstitial duplication have been found to cause defective COX4I1.[5][6]

Interactions

COX4I1 has 153 protein-protein interactions with 142 of them being co-complex interactions. COX4I1 has been found to interact with SDCBP, MT-CO1, IKBKE, TMBIM4, and MCL1.[12] 

LON, a mitochondrial protease, has also been suggested to regulate the COX4 subunit isoforms by degrading COX4I1 under hypoxic conditions.[11]

References

  1. ↑ 1.0 1.1 1.2 1.3 "Entrez Gene: COX4I1 cytochrome c oxidase subunit IV isoform 1". This article incorporates text from this source, which is in the public domain.
  2. ↑ Zeviani M, Nakagawa M, Herbert J, Lomax MI, Grossman LI, Sherbany AA, Miranda AF, DiMauro S, Schon EA (Dec 1987). "Isolation of a cDNA clone encoding subunit IV of human cytochrome c oxidase". Gene. 55 (2–3): 205–17. doi:10.1016/0378-1119(87)90281-2. PMID 2444497.
  3. ↑ Lomax MI, Welch MD, Darras BT, Francke U, Grossman LI (February 1990). "Novel use of a chimpanzee pseudogene for chromosomal mapping of human cytochrome c oxidase subunit IV". Gene. 86 (2): 209–16. doi:10.1016/0378-1119(90)90281-U. PMID 2157630.
  4. ↑ http://www.genetex.com/WebPage/Product/ProductDetail.aspx?catno=GTX101499&CampaignId=
  5. ↑ 5.0 5.1 Abu-Libdeh B, Douiev L, Amro S, Shahrour M, Ta-Shma A, Miller C, Elpeleg O, Saada A (October 2017). "Mutation in the COX4I1 gene is associated with short stature, poor weight gain and increased chromosomal breaks, simulating Fanconi anemia". European Journal of Human Genetics. 25 (10): 1142–1146. doi:10.1038/ejhg.2017.112. PMC 5602013. PMID 28766551.
  6. ↑ 6.0 6.1 Quéméner-Redon S, Bénech C, Audebert-Bellanger S, Friocourt G, Planes M, Parent P, Férec C (April 2013). "A small de novo 16q24.1 duplication in a woman with severe clinical features". European Journal of Medical Genetics. 56 (4): 211–5. doi:10.1016/j.ejmg.2013.01.001. PMID 23333879.
  7. ↑ Yao, Daniel. "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information". amino.heartproteome.org. Retrieved 2018-08-03.
  8. ↑ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (October 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
  9. ↑ "COX4I1 - Cytochrome c oxidase subunit 4 isoform 1, mitochondrial precursor - Homo sapiens (Human) - COX4I1 gene & protein". uniprot.org. Retrieved 2018-08-03.File:CC-BY-icon-80x15.png This article incorporates text available under the CC BY 4.0 license.
  10. ↑ "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
  11. ↑ 11.0 11.1 Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL (April 2007). "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells". Cell. 129 (1): 111–22. doi:10.1016/j.cell.2007.01.047. PMID 17418790.
  12. ↑ "153 binary interactions found for search term COX4I1". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.

External links

Further reading

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

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