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Protein

ATP synthase F(0) complex subunit B1, mitochondrial

Gene

ATP5F1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements.

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: GO_Central
  2. cellular metabolic process Source: Reactome
  3. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  4. respiratory electron transport chain Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. substantia nigra development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase F(0) complex subunit B1, mitochondrial
Alternative name(s):
ATP synthase proton-transporting mitochondrial F(0) complex subunit B1
ATP synthase subunit b
Short name:
ATPase subunit b
Gene namesi
Name:ATP5F1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:840. ATP5F1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane Source: UniProtKB
  3. mitochondrial inner membrane Source: Reactome
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  6. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: GO_Central
  7. mitochondrion Source: UniProtKB
  8. nucleoplasm Source: HPA
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionAdd
BLAST
Chaini43 – 256214ATP synthase F(0) complex subunit B1, mitochondrialPRO_0000002513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311N6-succinyllysineBy similarity
Modified residuei139 – 1391N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei162 – 1621N6-acetyllysineBy similarity
Modified residuei221 – 2211N6-acetyllysine1 Publication
Modified residuei233 – 2331N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP24539.
PaxDbiP24539.
PeptideAtlasiP24539.
PRIDEiP24539.

PTM databases

PhosphoSiteiP24539.

Expressioni

Gene expression databases

BgeeiP24539.
CleanExiHS_ATP5F1.
ExpressionAtlasiP24539. baseline and differential.
GenevestigatoriP24539.

Organism-specific databases

HPAiHPA046067.
HPA057347.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 (By similarity).By similarity

Protein-protein interaction databases

BioGridi107000. 39 interactions.
IntActiP24539. 18 interactions.
MINTiMINT-3010280.
STRINGi9606.ENSP00000358737.

Structurei

3D structure databases

ProteinModelPortaliP24539.
SMRiP24539. Positions 121-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic ATPase B chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG245616.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiP24539.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG7V4B02.
PhylomeDBiP24539.
TreeFamiTF313250.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24539-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY
60 70 80 90 100
GGKVRYGLIP EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF
110 120 130 140 150
TALSVLGVMV YGIKKYGPFV ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI
160 170 180 190 200
DTEKSQQALV QKRHYLFDVQ RNNIAMALEV TYRERLYRVY KEVKNRLDYH
210 220 230 240 250
ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI ADLKLLAKKA

QAQPVM
Length:256
Mass (Da):28,909
Last modified:May 2, 2002 - v2
Checksum:i743B1C54BFFEBBBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841I → V in CAA42782 (PubMed:1831354).Curated
Sequence conflicti91 – 911E → G in AAH05960 (PubMed:15489334).Curated
Sequence conflicti194 – 1941K → R in AAH05960 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521T → M.
Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
VAR_033534
Natural varianti152 – 1521T → N.
Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
VAR_013176

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60221 mRNA. Translation: CAA42782.1.
AL390195 Genomic DNA. Translation: CAC36042.1.
BC005366 mRNA. Translation: AAH05366.1.
BC005960 mRNA. Translation: AAH05960.1.
BC016350 mRNA. Translation: AAH16350.1.
CCDSiCCDS836.1.
PIRiJQ1144.
RefSeqiNP_001679.2. NM_001688.4.
UniGeneiHs.514870.

Genome annotation databases

EnsembliENST00000369722; ENSP00000358737; ENSG00000116459.
GeneIDi515.
KEGGihsa:515.
UCSCiuc001ebc.3. human.

Polymorphism databases

DMDMi20455474.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60221 mRNA. Translation: CAA42782.1.
AL390195 Genomic DNA. Translation: CAC36042.1.
BC005366 mRNA. Translation: AAH05366.1.
BC005960 mRNA. Translation: AAH05960.1.
BC016350 mRNA. Translation: AAH16350.1.
CCDSiCCDS836.1.
PIRiJQ1144.
RefSeqiNP_001679.2. NM_001688.4.
UniGeneiHs.514870.

3D structure databases

ProteinModelPortaliP24539.
SMRiP24539. Positions 121-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107000. 39 interactions.
IntActiP24539. 18 interactions.
MINTiMINT-3010280.
STRINGi9606.ENSP00000358737.

PTM databases

PhosphoSiteiP24539.

Polymorphism databases

DMDMi20455474.

Proteomic databases

MaxQBiP24539.
PaxDbiP24539.
PeptideAtlasiP24539.
PRIDEiP24539.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369722; ENSP00000358737; ENSG00000116459.
GeneIDi515.
KEGGihsa:515.
UCSCiuc001ebc.3. human.

Organism-specific databases

CTDi515.
GeneCardsiGC01P111991.
HGNCiHGNC:840. ATP5F1.
HPAiHPA046067.
HPA057347.
MIMi603270. gene.
neXtProtiNX_P24539.
PharmGKBiPA25130.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG245616.
HOGENOMiHOG000007163.
HOVERGENiHBG050604.
InParanoidiP24539.
KOiK02127.
OMAiVINHETF.
OrthoDBiEOG7V4B02.
PhylomeDBiP24539.
TreeFamiTF313250.

Enzyme and pathway databases

ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

GeneWikiiATP5F1.
GenomeRNAii515.
NextBioi2135.
PROiP24539.
SOURCEiSearch...

Gene expression databases

BgeeiP24539.
CleanExiHS_ATP5F1.
ExpressionAtlasiP24539. baseline and differential.
GenevestigatoriP24539.

Family and domain databases

InterProiIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERiPTHR12733. PTHR12733. 1 hit.
PfamiPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria."
    Higuti T., Tsurumi C., Osaka F., Kawamura Y., Tsujita H., Yoshihara Y., Tani I., Tanaka K., Ichirara A.
    Biochem. Biophys. Res. Commun. 178:1014-1020(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAT5F1_HUMAN
AccessioniPrimary (citable) accession number: P24539
Secondary accession number(s): Q9BQ68, Q9BRU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 2, 2002
Last modified: March 4, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.