P24539 (AT5F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit b, mitochondrial
Short name=ATPase subunit b

Gene names

Name:

ATP5F1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial ATP synthesis coupled proton transport Inferred by curator PubMed 12110673. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Non-traceable author statement Ref.1. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	proton-transporting ATP synthase activity, rotational mechanism Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Mitochondrion
	Chain	43 – 256	214	ATP synthase subunit b, mitochondrial		PRO_0000002513
Amino acid modifications
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	131	1	N6-acetyllysine By similarity
	Modified residue	162	1	N6-acetyllysine By similarity
	Modified residue	221	1	N6-acetyllysine Ref.4
	Modified residue	233	1	N6-acetyllysine Ref.4
Natural variations
	Natural variant	152	1	T → M. Corresponds to variant rs1264895 [ dbSNP | Ensembl ].		VAR_033534
	Natural variant	152	1	T → N. Corresponds to variant rs1264895 [ dbSNP | Ensembl ].		VAR_013176
Experimental info
	Sequence conflict	84	1	I → V in CAA42782. Ref.1
	Sequence conflict	91	1	E → G in AAH05960. Ref.3
	Sequence conflict	194	1	K → R in AAH05960. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P24539 [UniParc]. Last modified May 2, 2002. Version 2. Checksum: 743B1C54BFFEBBBD	FASTA	256	28,909
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
[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.
IPI	IPI00029133.
PIR	JQ1144.
RefSeq	NP_001679.2. NM_001688.4.
UniGene	Hs.514870.
3D structure databases
ProteinModelPortal	P24539.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24539. 15 interactions.
MINT	MINT-3010280.
STRING	9606.ENSP00000358737.
PTM databases
PhosphoSite	P24539.
Polymorphism databases
DMDM	20455474.
Proteomic databases
PaxDb	P24539.
PeptideAtlas	P24539.
PRIDE	P24539.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369722; ENSP00000358737; ENSG00000116459.
GeneID	515.
KEGG	hsa:515.
UCSC	uc001ebc.3. human.
Organism-specific databases
CTD	515.
GeneCards	GC01P111991.
HGNC	HGNC:840. ATP5F1.
HPA	HPA046067.
MIM	603270. gene.
neXtProt	NX_P24539.
PharmGKB	PA25130.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG245616.
HOGENOM	HOG000007163.
HOVERGEN	HBG050604.
InParanoid	P24539.
KO	K02127.
OMA	VINHETF.
OrthoDB	EOG4K3KXB.
PhylomeDB	P24539.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P24539.
Bgee	P24539.
CleanEx	HS_ATP5F1.
Genevestigator	P24539.
GermOnline	ENSG00000116459. Homo sapiens.
Family and domain databases
InterPro	IPR008688. ATPase_B_chain/sub_B/MI25. IPR013837. ATPase_F0_sub_B/B_chain. [Graphical view]
PANTHER	PTHR12733. PTHR12733. 1 hit.
Pfam	PF05405. Mt_ATP-synt_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	515.
NextBio	2135.
SOURCE	Search...

Entry information

Entry name

AT5F1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.