ATPB_HUMAN
ID ATPB_HUMAN Reviewed; 529 AA.
AC P06576; A8K4X0; Q14283;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 3.
DT 03-AUG-2022, entry version 246.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000305};
DE EC=7.1.2.2;
DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000312|HGNC:HGNC:830};
DE Flags: Precursor;
GN Name=ATP5F1B {ECO:0000312|HGNC:HGNC:830};
GN Synonyms=ATP5B {ECO:0000312|HGNC:HGNC:830}, ATPMB,
GN ATPSB {ECO:0000312|HGNC:HGNC:830};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2687158; DOI=10.1016/0888-7543(89)90125-0;
RA Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R.,
RA Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C.;
RT "The human ATP synthase beta subunit gene: sequence analysis, chromosome
RT assignment, and differential expression.";
RL Genomics 5:829-843(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-274.
RX PubMed=2900241; DOI=10.1016/s0021-9258(18)37950-x;
RA Ohta S., Tomura H., Matsuda K., Kagawa Y.;
RT "Gene structure of the human mitochondrial adenosine triphosphate synthase
RT beta subunit.";
RL J. Biol. Chem. 263:11257-11262(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-274.
RX PubMed=2870059; DOI=10.1093/oxfordjournals.jbchem.a135452;
RA Ohta S., Kagawa Y.;
RT "Human F1-ATPase: molecular cloning of cDNA for the beta subunit.";
RL J. Biochem. 99:135-141(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [8]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259; 265-279;
RP 282-345; 388-422; 433-456 AND 490-519, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
RX PubMed=2896550; DOI=10.1007/bf00434661;
RA Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A.,
RA Greenberg B.D.;
RT "Sequence analysis of cDNAs for the human and bovine ATP synthase beta
RT subunit: mitochondrial DNA genes sustain seventeen times more mutations.";
RL Curr. Genet. 12:81-90(1987).
RN [10]
RP PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [11]
RP PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259; 265-279;
RP 282-345; 407-422 AND 463-480, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TTC5.
RX PubMed=25168243; DOI=10.1038/cdd.2014.135;
RA Maniam S., Coutts A.S., Stratford M.R., McGouran J., Kessler B.,
RA La Thangue N.B.;
RT "Cofactor Strap regulates oxidative phosphorylation and mitochondrial p53
RT activity through ATP synthase.";
RL Cell Death Differ. 22:156-163(2015).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH MTLN.
RX PubMed=32243843; DOI=10.1016/j.stemcr.2020.03.002;
RA Friesen M., Warren C.R., Yu H., Toyohara T., Ding Q., Florido M.H.C.,
RA Sayre C., Pope B.D., Goff L.A., Rinn J.L., Cowan C.A.;
RT "Mitoregulin Controls beta-Oxidation in Human and Mouse Adipocytes.";
RL Stem Cell Reports 14:590-602(2020).
RN [20]
RP VARIANT VAL-130.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ. Interacts with PPIF. Interacts with BCL2L1 isoform BCL-X(L);
CC the interaction mediates the association of BCL2L1 isoform BCL-X(L)
CC with the mitochondrial membrane F(1)F(0) ATP synthase and enhances
CC neurons metabolic efficiency. Interacts with CLN5 and PPT1. Interacts
CC with S100A1; this interaction increases F1-ATPase activity (By
CC similarity). Interacts with MTLN (PubMed:32243843). Interacts with
CC TTC5/STRAP; the interaction results in decreased mitochondrial ATP
CC production (PubMed:25168243). {ECO:0000250|UniProtKB:P00829,
CC ECO:0000250|UniProtKB:P10719, ECO:0000250|UniProtKB:P56480,
CC ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:32243843}.
CC -!- INTERACTION:
CC P06576; P25705: ATP5F1A; NbExp=6; IntAct=EBI-356231, EBI-351437;
CC P06576; Q9UII2: ATP5IF1; NbExp=2; IntAct=EBI-356231, EBI-718459;
CC P06576; Q8N5M1: ATPAF2; NbExp=7; IntAct=EBI-356231, EBI-1166928;
CC P06576; P54253: ATXN1; NbExp=3; IntAct=EBI-356231, EBI-930964;
CC P06576; Q13895: BYSL; NbExp=3; IntAct=EBI-356231, EBI-358049;
CC P06576; Q8N448: LNX2; NbExp=4; IntAct=EBI-356231, EBI-2340947;
CC P06576; P63104: YWHAZ; NbExp=2; IntAct=EBI-356231, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00829}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00829}; Matrix side
CC {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; M27132; AAA51809.1; -; Genomic_DNA.
DR EMBL; M19483; AAA51808.1; -; Genomic_DNA.
DR EMBL; M19482; AAA51808.1; JOINED; Genomic_DNA.
DR EMBL; X03559; CAA27246.1; -; mRNA.
DR EMBL; D00022; BAA00016.1; -; mRNA.
DR EMBL; AK291085; BAF83774.1; -; mRNA.
DR EMBL; CH471054; EAW96952.1; -; Genomic_DNA.
DR EMBL; BC016512; AAH16512.1; -; mRNA.
DR EMBL; X05606; CAA29095.1; -; mRNA.
DR CCDS; CCDS8924.1; -.
DR PIR; A33370; A33370.
DR RefSeq; NP_001677.2; NM_001686.3.
DR AlphaFoldDB; P06576; -.
DR SMR; P06576; -.
DR BioGRID; 106994; 525.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P06576; -.
DR IntAct; P06576; 193.
DR MINT; P06576; -.
DR STRING; 9606.ENSP00000262030; -.
DR ChEMBL; CHEMBL2062350; -.
DR DrugBank; DB07384; 1-ACETYL-2-CARBOXYPIPERIDINE.
DR DrugBank; DB07394; AUROVERTIN B.
DR DrugBank; DB08949; Inositol nicotinate.
DR DrugBank; DB08629; N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A] PYRIMIDINE.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR DrugBank; DB08399; Piceatannol.
DR DrugBank; DB04216; Quercetin.
DR TCDB; 3.A.2.1.15; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR CarbonylDB; P06576; -.
DR GlyGen; P06576; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P06576; -.
DR MetOSite; P06576; -.
DR PhosphoSitePlus; P06576; -.
DR SwissPalm; P06576; -.
DR BioMuta; ATP5B; -.
DR DMDM; 114549; -.
DR DOSAC-COBS-2DPAGE; P06576; -.
DR OGP; P06576; -.
DR REPRODUCTION-2DPAGE; IPI00303476; -.
DR REPRODUCTION-2DPAGE; P06576; -.
DR SWISS-2DPAGE; P06576; -.
DR UCD-2DPAGE; P06576; -.
DR CPTAC; CPTAC-315; -.
DR CPTAC; CPTAC-316; -.
DR EPD; P06576; -.
DR jPOST; P06576; -.
DR MassIVE; P06576; -.
DR PaxDb; P06576; -.
DR PeptideAtlas; P06576; -.
DR PRIDE; P06576; -.
DR ProteomicsDB; 51907; -.
DR TopDownProteomics; P06576; -.
DR Antibodypedia; 877; 555 antibodies from 36 providers.
DR DNASU; 506; -.
DR Ensembl; ENST00000262030.8; ENSP00000262030.3; ENSG00000110955.9.
DR GeneID; 506; -.
DR KEGG; hsa:506; -.
DR MANE-Select; ENST00000262030.8; ENSP00000262030.3; NM_001686.4; NP_001677.2.
DR CTD; 506; -.
DR DisGeNET; 506; -.
DR GeneCards; ATP5F1B; -.
DR HGNC; HGNC:830; ATP5F1B.
DR HPA; ENSG00000110955; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 102910; gene.
DR neXtProt; NX_P06576; -.
DR OpenTargets; ENSG00000110955; -.
DR PharmGKB; PA25122; -.
DR VEuPathDB; HostDB:ENSG00000110955; -.
DR eggNOG; KOG1350; Eukaryota.
DR GeneTree; ENSGT00550000074800; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P06576; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 495235at2759; -.
DR PhylomeDB; P06576; -.
DR TreeFam; TF105640; -.
DR BioCyc; MetaCyc:HS03358-MON; -.
DR PathwayCommons; P06576; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P06576; -.
DR SIGNOR; P06576; -.
DR BioGRID-ORCS; 506; 556 hits in 1093 CRISPR screens.
DR ChiTaRS; ATP5B; human.
DR GeneWiki; ATP5B; -.
DR GenomeRNAi; 506; -.
DR Pharos; P06576; Tbio.
DR PRO; PR:P06576; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P06576; protein.
DR Bgee; ENSG00000110955; Expressed in apex of heart and 198 other tissues.
DR ExpressionAtlas; P06576; baseline and differential.
DR Genevisible; P06576; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:CAFA.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043532; F:angiostatin binding; IPI:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:CAFA.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; IMP:UniProtKB.
DR GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:CAFA.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IC:ComplexPortal.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Glycoprotein; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide; Translocase;
KW Transport.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19892738"
FT CHAIN 48..529
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002443"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 133
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 133
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 161
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 259
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 259
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 264
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10719"
FT MOD_RES 480
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 522
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56480"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 106
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VARIANT 130
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074188"
FT VARIANT 274
FT /note="E -> Q (in dbSNP:rs1042001)"
FT /evidence="ECO:0000269|PubMed:2870059,
FT ECO:0000269|PubMed:2900241"
FT /id="VAR_048371"
FT CONFLICT 1..6
FT /note="MLGFVG -> MTSLWGKGTGCKLFKF (in Ref. 3; BAA00016/
FT CAA27246)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..40
FT /note="APTAV -> VRRRF (in Ref. 2; AAA51808)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..40
FT /note="APTAV -> VRRRS (in Ref. 3; BAA00016/CAA27246)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..132
FT /note="API -> DQL (in Ref. 2; AAA51808)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="H -> D (in Ref. 2; AAA51808)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="Q -> H (in Ref. 2; AAA51808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 56560 MW; 960C616A2252B91A CRC64;
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS
