ID   AT5F1_HUMAN             Reviewed;         256 AA.
AC   P24539; Q9BQ68; Q9BRU8;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=ATP synthase F(0) complex subunit B1, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase peripheral stalk-membrane subunit b {ECO:0000305};
DE   AltName: Full=ATP synthase proton-transporting mitochondrial F(0) complex subunit B1;
DE   AltName: Full=ATP synthase subunit b;
DE            Short=ATPase subunit b;
DE   Flags: Precursor;
GN   Name=ATP5PB {ECO:0000312|HGNC:HGNC:840}; Synonyms=ATP5F1;
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 [MRNA].
RX   PubMed=1831354; DOI=10.1016/0006-291x(91)90993-h;
RA   Higuti T., Tsurumi C., Osaka F., Kawamura Y., Tsujita H., Yoshihara Y.,
RA   Tani I., Tanaka K., Ichirara A.;
RT   "Molecular cloning of cDNA for the import precursor of human subunit B of
RT   H(+)-ATP synthase in mitochondria.";
RL   Biochem. Biophys. Res. Commun. 178:1014-1020(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, 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   [5]
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   [6]
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   [7]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER VAL-42, AND
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).
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. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements.
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 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P24539; P25705: ATP5F1A; NbExp=8; IntAct=EBI-1044810, EBI-351437;
CC       P24539; O75947: ATP5PD; NbExp=3; IntAct=EBI-1044810, EBI-724024;
CC       P24539; P54253: ATXN1; NbExp=3; IntAct=EBI-1044810, EBI-930964;
CC       P24539; Q14154: DELE1; NbExp=3; IntAct=EBI-1044810, EBI-2805660;
CC       P24539; Q9H410: DSN1; NbExp=3; IntAct=EBI-1044810, EBI-1001144;
CC       P24539; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-1044810, EBI-3893327;
CC       P24539; P42858: HTT; NbExp=3; IntAct=EBI-1044810, EBI-466029;
CC       P24539; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-1044810, EBI-8487781;
CC       P24539; Q9ULW8: PADI3; NbExp=3; IntAct=EBI-1044810, EBI-10488185;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
CC       {ECO:0000305}.
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DR   EMBL; X60221; CAA42782.1; -; mRNA.
DR   EMBL; AL390195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005366; AAH05366.1; -; mRNA.
DR   EMBL; BC005960; AAH05960.1; -; mRNA.
DR   EMBL; BC016350; AAH16350.1; -; mRNA.
DR   CCDS; CCDS836.1; -.
DR   PIR; JQ1144; JQ1144.
DR   RefSeq; NP_001679.2; NM_001688.4.
DR   PDB; 8H9F; EM; 2.69 A; K=43-256.
DR   PDB; 8H9G; EM; 2.95 A; K=43-256.
DR   PDB; 8H9J; EM; 3.26 A; K=43-256.
DR   PDB; 8H9K; EM; 3.51 A; K=43-256.
DR   PDB; 8H9M; EM; 3.00 A; K=43-256.
DR   PDB; 8H9N; EM; 3.56 A; K=43-256.
DR   PDB; 8H9Q; EM; 3.47 A; K=43-256.
DR   PDB; 8H9R; EM; 3.97 A; K=43-256.
DR   PDB; 8H9S; EM; 2.53 A; K=43-256.
DR   PDB; 8H9T; EM; 2.77 A; K=43-256.
DR   PDB; 8H9U; EM; 2.61 A; K=43-256.
DR   PDB; 8H9V; EM; 3.02 A; K=43-256.
DR   PDBsum; 8H9F; -.
DR   PDBsum; 8H9G; -.
DR   PDBsum; 8H9J; -.
DR   PDBsum; 8H9K; -.
DR   PDBsum; 8H9M; -.
DR   PDBsum; 8H9N; -.
DR   PDBsum; 8H9Q; -.
DR   PDBsum; 8H9R; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P24539; -.
DR   EMDB; EMD-34565; -.
DR   EMDB; EMD-34566; -.
DR   EMDB; EMD-34569; -.
DR   EMDB; EMD-34570; -.
DR   EMDB; EMD-34573; -.
DR   EMDB; EMD-34574; -.
DR   EMDB; EMD-34577; -.
DR   EMDB; EMD-34578; -.
DR   EMDB; EMD-34580; -.
DR   EMDB; EMD-34581; -.
DR   EMDB; EMD-34582; -.
DR   EMDB; EMD-34583; -.
DR   SMR; P24539; -.
DR   BioGRID; 107000; 356.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   CORUM; P24539; -.
DR   IntAct; P24539; 113.
DR   MINT; P24539; -.
DR   STRING; 9606.ENSP00000358737; -.
DR   TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   GlyGen; P24539; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P24539; -.
DR   MetOSite; P24539; -.
DR   PhosphoSitePlus; P24539; -.
DR   SwissPalm; P24539; -.
DR   BioMuta; ATP5F1; -.
DR   DMDM; 20455474; -.
DR   EPD; P24539; -.
DR   jPOST; P24539; -.
DR   MassIVE; P24539; -.
DR   PaxDb; 9606-ENSP00000358737; -.
DR   PeptideAtlas; P24539; -.
DR   ProteomicsDB; 54215; -.
DR   Pumba; P24539; -.
DR   TopDownProteomics; P24539; -.
DR   Antibodypedia; 33810; 209 antibodies from 32 providers.
DR   DNASU; 515; -.
DR   Ensembl; ENST00000369722.8; ENSP00000358737.3; ENSG00000116459.11.
DR   GeneID; 515; -.
DR   KEGG; hsa:515; -.
DR   MANE-Select; ENST00000369722.8; ENSP00000358737.3; NM_001688.5; NP_001679.2.
DR   AGR; HGNC:840; -.
DR   CTD; 515; -.
DR   GeneCards; ATP5PB; -.
DR   HGNC; HGNC:840; ATP5PB.
DR   HPA; ENSG00000116459; Tissue enhanced (skeletal muscle, tongue).
DR   MIM; 603270; gene.
DR   neXtProt; NX_P24539; -.
DR   OpenTargets; ENSG00000116459; -.
DR   PharmGKB; PA25130; -.
DR   VEuPathDB; HostDB:ENSG00000116459; -.
DR   eggNOG; KOG3976; Eukaryota.
DR   GeneTree; ENSGT00390000001958; -.
DR   HOGENOM; CLU_087186_1_0_1; -.
DR   InParanoid; P24539; -.
DR   OMA; KHMVDWI; -.
DR   OrthoDB; 2939076at2759; -.
DR   PhylomeDB; P24539; -.
DR   TreeFam; TF313250; -.
DR   BioCyc; MetaCyc:HS04013-MONOMER; -.
DR   PathwayCommons; P24539; -.
DR   Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; P24539; -.
DR   SIGNOR; P24539; -.
DR   BioGRID-ORCS; 515; 443 hits in 1166 CRISPR screens.
DR   ChiTaRS; ATP5F1; human.
DR   GeneWiki; ATP5F1; -.
DR   GenomeRNAi; 515; -.
DR   Pharos; P24539; Tbio.
DR   PRO; PR:P24539; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P24539; Protein.
DR   Bgee; ENSG00000116459; Expressed in heart right ventricle and 204 other cell types or tissues.
DR   ExpressionAtlas; P24539; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   Gene3D; 1.20.5.2210; -; 1.
DR   InterPro; IPR008688; ATP_synth_Bsub_B/MI25.
DR   InterPro; IPR013837; ATP_synth_F0_suB.
DR   PANTHER; PTHR12733:SF3; ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12733; MITOCHONDRIAL ATP SYNTHASE B CHAIN; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
DR   SUPFAM; SSF161060; ATP synthase B chain-like; 1.
DR   Genevisible; P24539; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0007744|PubMed:25944712"
FT   CHAIN           43..256
FT                   /note="ATP synthase F(0) complex subunit B1, mitochondrial"
FT                   /id="PRO_0000002513"
FT   MOD_RES         131
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         139
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         154
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   MOD_RES         221
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         233
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         244
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQQ7"
FT   VARIANT         152
FT                   /note="T -> M (in dbSNP:rs1264895)"
FT                   /id="VAR_033534"
FT   VARIANT         152
FT                   /note="T -> N (in dbSNP:rs1264895)"
FT                   /id="VAR_013176"
FT   CONFLICT        84
FT                   /note="I -> V (in Ref. 1; CAA42782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="E -> G (in Ref. 3; AAH05960)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="K -> R (in Ref. 3; AAH05960)"
FT                   /evidence="ECO:0000305"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           75..89
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           97..162
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           165..223
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           236..247
FT                   /evidence="ECO:0007829|PDB:8H9G"
SQ   SEQUENCE   256 AA;  28909 MW;  743B1C54BFFEBBBD CRC64;
     MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY GGKVRYGLIP
     EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF TALSVLGVMV YGIKKYGPFV
     ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI DTEKSQQALV QKRHYLFDVQ RNNIAMALEV
     TYRERLYRVY KEVKNRLDYH ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI
     ADLKLLAKKA QAQPVM
//