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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
{{Infobox protein family
| update_page = yes
| Symbol = ATP-synt_F6
| require_manual_inspection = no
| Name = Mitochondrial ATP synthase coupling factor 6 (F6)
| update_protein_box = yes
| image = PDB 1vzs EBI.jpg
| update_summary = yes
| width =
| update_citations = yes
| caption = solution structure of subunit f6 from the peripheral stalk region of atp synthase from bovine heart mitochondria
| Pfam = PF05511
| Pfam_clan = 
| InterPro = IPR008387
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
'''ATP synthase-coupling factor 6, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''ATP5J'' [[gene]].<ref name="pmid1830479">{{cite journal | vauthors = Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I, Tanaka K, Ichihara A | title = Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria | journal = Biochemical and Biophysical Research Communications | volume = 178 | issue = 2 | pages = 793–9 | date = Jul 1991 | pmid = 1830479 | pmc =  | doi = 10.1016/0006-291X(91)90178-A }}</ref><ref name="pmid1825642">{{cite journal | vauthors = Javed AA, Ogata K, Sanadi DR | title = Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6 | journal = Gene | volume = 97 | issue = 2 | pages = 307–10 | date = Jan 1991 | pmid = 1825642 | pmc =  | doi = 10.1016/0378-1119(91)90068-M }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6 | url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=522 }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
 
| image =
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and F0 interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.<ref name="entrez"/>
| image_source =
 
| PDB =
The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between [[mitochondrial]], [[chloroplast]] and [[bacterial]] [[F-ATPase]]s. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D.<ref name="pmid16045926">{{cite journal | vauthors = Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D | title = Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit | journal = Journal of Molecular Biology | volume = 351 | issue = 4 | pages = 824–38 | date = Aug 2005 | pmid = 16045926 | doi = 10.1016/j.jmb.2005.06.012 }}</ref> There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and [[photosynthetic]] [[bacterium|bacteria]].
| Name = ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6
 
| HGNCid = 847
== References ==
| Symbol = ATP5J
{{reflist}}
| AltSymbols =; ATP5A; ATPM; ATP5; CF6; F6
| OMIM = 603152
| ECnumber = 
| Homologene = 1272
| MGIid = 107777
| GeneAtlas_image1 = PBB_GE_ATP5J_202325_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0046933 |text = hydrogen ion transporting ATP synthase activity, rotational mechanism}} {{GNF_GO|id=GO:0046961 |text = hydrogen ion transporting ATPase activity, rotational mechanism}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}} {{GNF_GO|id=GO:0045263 |text = proton-transporting ATP synthase complex, coupling factor F(o)}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015986 |text = ATP synthesis coupled proton transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 522
    | Hs_Ensembl = ENSG00000154723
    | Hs_RefseqProtein = NP_001003696
    | Hs_RefseqmRNA = NM_001003696
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 26018663
    | Hs_GenLoc_end = 26029836
    | Hs_Uniprot = P18859
    | Mm_EntrezGene = 11957
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_016755
    | Mm_RefseqProtein = NP_058035
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6''', also known as '''ATP5J''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=522| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==External links==
{{PBB_Summary
* {{UCSC gene info|ATP5J}}
| section_title =  
| summary_text = Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and F0 interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=522| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Kinosita K, Yasuda R, Noji H | title = F1-ATPase: a highly efficient rotary ATP machine | journal = Essays in Biochemistry | volume = 35 | issue =  | pages = 3–18 | year = 2003 | pmid = 12471886 | doi =  }}
| citations =
* {{cite journal | vauthors = Oster G, Wang H | title = Rotary protein motors | journal = Trends in Cell Biology | volume = 13 | issue = 3 | pages = 114–21 | date = Mar 2003 | pmid = 12628343 | doi = 10.1016/S0962-8924(03)00004-7 }}
*{{cite journal | author=Kinosita K, Yasuda R, Noji H |title=F1-ATPase: a highly efficient rotary ATP machine. |journal=Essays Biochem. |volume=35 |issue=  |pages= 3-18 |year= 2003 |pmid= 12471886 |doi=  }}
* {{cite journal | vauthors = Leyva JA, Bianchet MA, Amzel LM | title = Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review) | journal = Molecular Membrane Biology | volume = 20 | issue = 1 | pages = 27–33 | year = 2003 | pmid = 12745923 | doi = 10.1080/0968768031000066532 }}
*{{cite journal | author=Oster G, Wang H |title=Rotary protein motors. |journal=Trends Cell Biol. |volume=13 |issue= 3 |pages= 114-21 |year= 2003 |pmid= 12628343 |doi= }}
* {{cite journal | vauthors = Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R | title = Human liver protein map: a reference database established by microsequencing and gel comparison | journal = Electrophoresis | volume = 13 | issue = 12 | pages = 992–1001 | date = Dec 1992 | pmid = 1286669 | doi = 10.1002/elps.11501301201 }}
*{{cite journal | author=Leyva JA, Bianchet MA, Amzel LM |title=Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). |journal=Mol. Membr. Biol. |volume=20 |issue= 1 |pages= 27-33 |year= 2003 |pmid= 12745923 |doi= }}
* {{cite journal | vauthors = Yan WL, Lerner TJ, Haines JL, Gusella JF | title = Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3) | journal = Genomics | volume = 24 | issue = 2 | pages = 375–7 | date = Nov 1994 | pmid = 7698763 | doi = 10.1006/geno.1994.1631 }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
* {{cite journal | vauthors = Elston T, Wang H, Oster G | title = Energy transduction in ATP synthase | journal = Nature | volume = 391 | issue = 6666 | pages = 510–3 | date = Jan 1998 | pmid = 9461222 | doi = 10.1038/35185 }}
*{{cite journal  | author=Javed AA, Ogata K, Sanadi DR |title=Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6. |journal=Gene |volume=97 |issue= 2 |pages= 307-10 |year= 1991 |pmid= 1825642 |doi=  }}
* {{cite journal | vauthors = Webster KA, Oliver NA, Wallace DC | title = Assignment of an oligomycin-resistance locus to human chromosome 10 | journal = Somatic Cell Genetics | volume = 8 | issue = 2 | pages = 223–44 | date = Mar 1982 | pmid = 9732751 | doi = 10.1007/BF01538679 }}
*{{cite journal  | author=Higuti T, Tsurumi C, Kawamura Y, ''et al.'' |title=Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 793-9 |year= 1991 |pmid= 1830479 |doi=  }}
* {{cite journal | vauthors = Wang H, Oster G | title = Energy transduction in the F1 motor of ATP synthase | journal = Nature | volume = 396 | issue = 6708 | pages = 279–82 | date = Nov 1998 | pmid = 9834036 | doi = 10.1038/24409 }}
*{{cite journal | author=Yan WL, Lerner TJ, Haines JL, Gusella JF |title=Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3). |journal=Genomics |volume=24 |issue= 2 |pages= 375-7 |year= 1995 |pmid= 7698763 |doi= 10.1006/geno.1994.1631 }}
* {{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
*{{cite journal | author=Elston T, Wang H, Oster G |title=Energy transduction in ATP synthase. |journal=Nature |volume=391 |issue= 6666 |pages= 510-3 |year= 1998 |pmid= 9461222 |doi= 10.1038/35185 }}
* {{cite journal | vauthors = Osanai T, Nakamura M, Sasaki S, Tomita H, Saitoh M, Osawa H, Yamabe H, Murakami S, Magota K, Okumura K | title = Plasma concentration of coupling factor 6 and cardiovascular events in patients with end-stage renal disease | journal = Kidney International | volume = 64 | issue = 6 | pages = 2291–7 | date = Dec 2003 | pmid = 14633154 | doi = 10.1046/j.1523-1755.2003.00334.x }}
*{{cite journal | author=Webster KA, Oliver NA, Wallace DC |title=Assignment of an oligomycin-resistance locus to human chromosome 10. |journal=Somatic Cell Genet. |volume=8 |issue= 2 |pages= 223-44 |year= 1998 |pmid= 9732751 |doi= }}
* {{cite journal | vauthors = Cross RL | title = Molecular motors: turning the ATP motor | journal = Nature | volume = 427 | issue = 6973 | pages = 407–8 | date = Jan 2004 | pmid = 14749816 | doi = 10.1038/427407b }}
*{{cite journal | author=Wang H, Oster G |title=Energy transduction in the F1 motor of ATP synthase. |journal=Nature |volume=396 |issue= 6708 |pages= 279-82 |year= 1998 |pmid= 9834036 |doi= 10.1038/24409 }}
* {{cite journal | vauthors = Jacobs LJ, de Coo IF, Nijland JG, Galjaard RJ, Los FJ, Schoonderwoerd K, Niermeijer MF, Geraedts JP, Scholte HR, Smeets HJ | title = Transmission and prenatal diagnosis of the T9176C mitochondrial DNA mutation | journal = Molecular Human Reproduction | volume = 11 | issue = 3 | pages = 223–8 | date = Mar 2005 | pmid = 15709156 | doi = 10.1093/molehr/gah152 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal | author=Osanai T, Nakamura M, Sasaki S, ''et al.'' |title=Plasma concentration of coupling factor 6 and cardiovascular events in patients with end-stage renal disease. |journal=Kidney Int. |volume=64 |issue= 6 |pages= 2291-7 |year= 2004 |pmid= 14633154 |doi= 10.1046/j.1523-1755.2003.00334.x }}
*{{cite journal | author=Cross RL |title=Molecular motors: turning the ATP motor. |journal=Nature |volume=427 |issue= 6973 |pages= 407-8 |year= 2004 |pmid= 14749816 |doi= 10.1038/427407b }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal  | author=Jacobs LJ, de Coo IF, Nijland JG, ''et al.'' |title=Transmission and prenatal diagnosis of the T9176C mitochondrial DNA mutation. |journal=Mol. Hum. Reprod. |volume=11 |issue= 3 |pages= 223-8 |year= 2005 |pmid= 15709156 |doi= 10.1093/molehr/gah152 }}
}}
{{refend}}
{{refend}}
{{InterPro content|IPR008387}}


{{gene-21-stub}}
{{gene-21-stub}}
{{WikiDoc Sources}}

Revision as of 02:08, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
Mitochondrial ATP synthase coupling factor 6 (F6)
File:PDB 1vzs EBI.jpg
solution structure of subunit f6 from the peripheral stalk region of atp synthase from bovine heart mitochondria
Identifiers
SymbolATP-synt_F6
PfamPF05511
InterProIPR008387

ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the ATP5J gene.[1][2][3]

Function

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the F0 complex, required for F1 and F0 interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.[3]

The F6 subunit is part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In mitochondria, the peripheral stalk is composed of one copy each of subunits OSCP (oligomycin sensitivity conferral protein), F6, B and D.[4] There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria.

References

  1. ↑ Higuti T, Tsurumi C, Kawamura Y, Tsujita H, Osaka F, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Jul 1991). "Molecular cloning of cDNA for the import precursor of human coupling factor 6 of H(+)-ATP synthase in mitochondria". Biochemical and Biophysical Research Communications. 178 (2): 793–9. doi:10.1016/0006-291X(91)90178-A. PMID 1830479.
  2. ↑ Javed AA, Ogata K, Sanadi DR (Jan 1991). "Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded precursor of coupling factor 6". Gene. 97 (2): 307–10. doi:10.1016/0378-1119(91)90068-M. PMID 1825642.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP5J ATP synthase, H+ transporting, mitochondrial F0 complex, subunit F6".
  4. ↑ Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (Aug 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". Journal of Molecular Biology. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926.

External links

Further reading

  • Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays in Biochemistry. 35: 3–18. PMID 12471886.
  • Oster G, Wang H (Mar 2003). "Rotary protein motors". Trends in Cell Biology. 13 (3): 114–21. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
  • Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Molecular Membrane Biology. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923.
  • Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (Dec 1992). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669.
  • Yan WL, Lerner TJ, Haines JL, Gusella JF (Nov 1994). "Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3)". Genomics. 24 (2): 375–7. doi:10.1006/geno.1994.1631. PMID 7698763.
  • Elston T, Wang H, Oster G (Jan 1998). "Energy transduction in ATP synthase". Nature. 391 (6666): 510–3. doi:10.1038/35185. PMID 9461222.
  • Webster KA, Oliver NA, Wallace DC (Mar 1982). "Assignment of an oligomycin-resistance locus to human chromosome 10". Somatic Cell Genetics. 8 (2): 223–44. doi:10.1007/BF01538679. PMID 9732751.
  • Wang H, Oster G (Nov 1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. doi:10.1038/24409. PMID 9834036.
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Osanai T, Nakamura M, Sasaki S, Tomita H, Saitoh M, Osawa H, Yamabe H, Murakami S, Magota K, Okumura K (Dec 2003). "Plasma concentration of coupling factor 6 and cardiovascular events in patients with end-stage renal disease". Kidney International. 64 (6): 2291–7. doi:10.1046/j.1523-1755.2003.00334.x. PMID 14633154.
  • Cross RL (Jan 2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. doi:10.1038/427407b. PMID 14749816.
  • Jacobs LJ, de Coo IF, Nijland JG, Galjaard RJ, Los FJ, Schoonderwoerd K, Niermeijer MF, Geraedts JP, Scholte HR, Smeets HJ (Mar 2005). "Transmission and prenatal diagnosis of the T9176C mitochondrial DNA mutation". Molecular Human Reproduction. 11 (3): 223–8. doi:10.1093/molehr/gah152. PMID 15709156.
This article incorporates text from the public domain Pfam and InterPro: IPR008387


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