ATP5B

ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide
PDB rendering based on 1bmf.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1bmf​, 1cow​, 1e1q​, 1e1r​, 1e79​, 1efr​, 1h8e​, 1h8h​, 1mab​, 1nbm​, 1ohh​, 1qo1​, 1w0j​, 1w0k​, 2ck3​, 2f43​, 2jdi​
Identifiers
Symbols	ATP5B ; ATPMB; ATPSB; HEL-S-271
External IDs	OMIM: 102910 MGI: 107801 HomoloGene: 1273 GeneCards: ATP5B Gene
EC number	3.6.3.14
Gene ontology Molecular function • transporter activity • protein binding • ATP binding • ATPase activity • transmembrane transporter activity • MHC class I protein binding • proton-transporting ATP synthase activity, rotational mechanism • proton-transporting ATPase activity, rotational mechanism Cellular component • nucleus • mitochondrion • mitochondrial proton-transporting ATP synthase complex • mitochondrial proton-transporting ATP synthase, catalytic core • mitochondrial matrix • plasma membrane • cell surface • membrane • mitochondrial membrane • mitochondrial nucleoid • myelin sheath • extracellular exosome Biological process • angiogenesis • osteoblast differentiation • generation of precursor metabolites and energy • lipid metabolic process • ATP biosynthetic process • negative regulation of cell adhesion involved in substrate-bound cell migration • organelle organization • mitochondrion organization • ATP hydrolysis coupled proton transport • proton transport • respiratory electron transport chain • mitochondrial ATP synthesis coupled proton transport • cellular metabolic process • small molecule metabolic process • regulation of intracellular pH Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	506	11947
Ensembl	ENSG00000110955	ENSMUSG00000025393
UniProt	P06576	P56480
RefSeq (mRNA)	NM_001686	NM_016774
RefSeq (protein)	NP_001677	NP_058054
Location (UCSC)	Chr 12: 56.64 – 56.65 Mb	Chr 10: 128.08 – 128.09 Mb
PubMed search

ATP synthase subunit beta, mitochondrial is an enzyme that in humans is encoded by the ATP5B gene.^[1][2]

Function

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.^[2]

References

1. Neckelmann N, Warner CK, Chung A, Kudoh J, Minoshima S, Fukuyama R, Maekawa M, Shimizu Y, Shimizu N, Liu JD (Jan 1990). "The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression". Genomics 5 (4): 829–43. doi:10.1016/0888-7543(89)90125-0. PMID 2687158.
2. "Entrez Gene: ATP5B ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide".

Further reading

• Maguire D, Shah J, McCabe M (2007). "Assaying ATP synthase rotor activity". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology 578: 67–72. doi:10.1007/0-387-29540-2_11. ISBN 978-0-387-29543-5. PMID 16927672.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• 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, Singh G, Webster KA, Greenberg BD (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. doi:10.1007/BF00434661. 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, Cormand B, Iglesias R, Mampel T, Giralt M, Villarroya F (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, Enghild JJ, Højrup P, Everitt L, Hubchak S, Schnaper HW, Pizzo SV (1999). "Angiostatin binds ATP synthase on the surface of human endothelial cells". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 2811–6. doi:10.1073/pnas.96.6.2811. PMC 15851. 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, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. 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. doi:10.1016/S0005-2728(02)00262-1. PMID 12206899.
• Martinez LO, Jacquet S, Esteve JP, Rolland C, Cabezón E, Champagne E, Pineau T, Georgeaud V, Walker JE, Tercé F, Collet X, Perret B, Barbaras R (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, Zhi Y, Herterich S, Hoehn H, Gross HJ, Joenje H, Hoatlin ME, Mathew CG, Huber PA (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. doi:10.1016/S0014-4827(03)00261-1. 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. PMC 1134064. PMID 15242332.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (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.