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P24539 (AT5F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATP5F1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the eukaryotic ATPase B chain family.

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Cellular componentCF(0)
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 12110673. Source: GOC

ATP synthesis coupled proton transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

cellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial ATP synthesis coupled proton transport

Inferred by curator PubMed 12110673. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial matrix

Non-traceable author statement Ref.1. Source: UniProtKB

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrial proton-transporting ATP synthase complex, coupling factor F(o)

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_functionproton-transporting ATP synthase activity, rotational mechanism

Inferred from Biological aspect of Ancestor. Source: RefGenome

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion
Chain43 – 256214ATP synthase F(0) complex subunit B1, mitochondrial
PRO_0000002513

Amino acid modifications

Modified residue1311N6-succinyllysine By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1541N6-acetyllysine By similarity
Modified residue1621N6-acetyllysine By similarity
Modified residue2211N6-acetyllysine Ref.4
Modified residue2331N6-acetyllysine Ref.4
Modified residue2441N6-acetyllysine By similarity

Natural variations

Natural variant1521T → M.
Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
VAR_033534
Natural variant1521T → N.
Corresponds to variant rs1264895 [ dbSNP | Ensembl ].
VAR_013176

Experimental info

Sequence conflict841I → V in CAA42782. Ref.1
Sequence conflict911E → G in AAH05960. Ref.3
Sequence conflict1941K → R in AAH05960. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P24539 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: 743B1C54BFFEBBBD

FASTA25628,909
        10         20         30         40         50         60 
MLSRVVLSAA ATAAPSLKNA AFLGPGVLQA TRTFHTGQPH LVPVPPLPEY GGKVRYGLIP 

        70         80         90        100        110        120 
EEFFQFLYPK TGVTGPYVLG TGLILYALSK EIYVISAETF TALSVLGVMV YGIKKYGPFV 

       130        140        150        160        170        180 
ADFADKLNEQ KLAQLEEAKQ ASIQHIQNAI DTEKSQQALV QKRHYLFDVQ RNNIAMALEV 

       190        200        210        220        230        240 
TYRERLYRVY KEVKNRLDYH ISVQNMMRRK EQEHMINWVE KHVVQSISTQ QEKETIAKCI 

       250 
ADLKLLAKKA QAQPVM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJQ1144.
RefSeqNP_001679.2. NM_001688.4.
UniGeneHs.514870.

3D structure databases

ProteinModelPortalP24539.
SMRP24539. Positions 121-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107000. 18 interactions.
IntActP24539. 17 interactions.
MINTMINT-3010280.
STRING9606.ENSP00000358737.

PTM databases

PhosphoSiteP24539.

Polymorphism databases

DMDM20455474.

Proteomic databases

PaxDbP24539.
PeptideAtlasP24539.
PRIDEP24539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369722; ENSP00000358737; ENSG00000116459.
GeneID515.
KEGGhsa:515.
UCSCuc001ebc.3. human.

Organism-specific databases

CTD515.
GeneCardsGC01P111991.
HGNCHGNC:840. ATP5F1.
HPAHPA046067.
MIM603270. gene.
neXtProtNX_P24539.
PharmGKBPA25130.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245616.
HOGENOMHOG000007163.
HOVERGENHBG050604.
InParanoidP24539.
KOK02127.
OMAVINHETF.
OrthoDBEOG7V4B02.
PhylomeDBP24539.
TreeFamTF313250.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP24539.
BgeeP24539.
CleanExHS_ATP5F1.
GenevestigatorP24539.

Family and domain databases

InterProIPR008688. ATPase_B_chain/sub_B/MI25.
IPR013837. ATPase_F0_sub_B/B_chain.
[Graphical view]
PANTHERPTHR12733. PTHR12733. 1 hit.
PfamPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiATP5F1.
GenomeRNAi515.
NextBio2135.
PROP24539.
SOURCESearch...

Entry information

Entry nameAT5F1_HUMAN
AccessionPrimary (citable) accession number: P24539
Secondary accession number(s): Q9BQ68, Q9BRU8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM