ATP5B

From Wikipedia, the free encyclopedia

ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide

PDB rendering based on 1bmf.

Available structures: 1bmf, 1cow, 1e1q, 1e1r, 1e79, 1efr, 1h8e, 1h8h, 1mab, 1nbm, 1ohh, 1qo1, 1w0j, 1w0k, 2ck3, 2f43, 2jdi

Identifiers

Symbol(s)

ATP5B; ATPMB; ATPSB; MGC5231

External IDs

OMIM: 102910 MGI: 107801 HomoloGene: 1273

Gene ontology
Molecular Function:	• nucleotide binding • transporter activity • protein binding • ATP binding • hydrogen-exporting ATPase activity, phosphorylative mechanism • hydrolase activity • nucleoside-triphosphatase activity • metal ion binding • hydrogen ion transporting ATP synthase activity, rotational mechanism • hydrogen ion transporting ATPase activity, rotational mechanism
Cellular Component:	• mitochondrion • mitochondrial proton-transporting ATP synthase complex • mitochondrial proton-transporting ATP synthase, catalytic core • proton-transporting ATP synthase complex, catalytic core F(1)
Biological Process:	• generation of precursor metabolites and energy • ion transport • ATP synthesis coupled proton transport • proton transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001686 (mRNA)
NP_001677 (protein)

NM_016774 (mRNA)
NP_058054 (protein)

Location

Chr 12: 55.32 - 55.33 Mb

Chr 10: 127.49 - 127.49 Mb

Pubmed search

[1]

[2]

ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide, also known as ATP5B, is a human gene.^[1]

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core.^[1]

[edit] References

^ ^a ^b Entrez Gene: ATP5B ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide.

[edit] Further reading

Maguire D, Shah J, McCabe M (2007). "Assaying ATP synthase rotor activity.". Adv. Exp. Med. Biol. 578: 67–72. PMID 16927672.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. PMID 1602151.
Neckelmann N, Warner CK, Chung A, et al. (1990). "The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression.". Genomics 5 (4): 829–43. PMID 2687158.
Ohta S, Kagawa Y (1986). "Human F1-ATPase: molecular cloning of cDNA for the beta subunit.". J. Biochem. 99 (1): 135–41. PMID 2870059.
Wallace DC, Ye JH, Neckelmann SN, et al. (1988). "Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations.". Curr. Genet. 12 (2): 81–90. PMID 2896550.
Ohta S, Tomura H, Matsuda K, Kagawa Y (1988). "Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit.". J. Biol. Chem. 263 (23): 11257–62. PMID 2900241.
Villena JA, Martin I, Viñas O, et al. (1995). "ETS transcription factors regulate the expression of the gene for the human mitochondrial ATP synthase beta-subunit.". J. Biol. Chem. 269 (51): 32649–54. PMID 7798271.
Abrahams JP, Leslie AG, Lutter R, Walker JE (1994). "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.". Nature 370 (6491): 621–8. doi:10.1038/370621a0. PMID 8065448.
Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase.". Nature 391 (6666): 510–3. doi:10.1038/35185. PMID 9461222.
Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase.". Nature 396 (6708): 279–82. doi:10.1038/24409. PMID 9834036.
Moser TL, Stack MS, Asplin I, et al. (1999). "Angiostatin binds ATP synthase on the surface of human endothelial cells.". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 2811–6. PMID 10077593.
Wang ZG, White PS, Ackerman SH (2001). "Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria.". J. Biol. Chem. 276 (33): 30773–8. doi:10.1074/jbc.M104133200. PMID 11410595.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. PMID 11790298.
Ackerman SH (2002). "Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in mitochondria.". Biochim. Biophys. Acta 1555 (1-3): 101–5. PMID 12206899.
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. PMID 12477932.
Martinez LO, Jacquet S, Esteve JP, et al. (2003). "Ectopic beta-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis.". Nature 421 (6918): 75–9. doi:10.1038/nature01250. PMID 12511957.
Reuter TY, Medhurst AL, Waisfisz Q, et al. (2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport.". Exp. Cell Res. 289 (2): 211–21. PMID 14499622.
Cross RL (2004). "Molecular motors: turning the ATP motor.". Nature 427 (6973): 407–8. doi:10.1038/427407b. PMID 14749816.
Aboulaich N, Vainonen JP, Strålfors P, Vener AV (2005). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.". Biochem. J. 383 (Pt 2): 237–48. doi:10.1042/BJ20040647. PMID 15242332.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.