Reviewed, UniProtKB/Swiss-Prot P24539 (AT5F1_HUMAN)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit b, mitochondrial

Gene names

Name:

ATP5F1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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
Gene Ontology (GO)
Biological process	mitochondrial ATP synthesis coupled proton transport Inferred by curator. Source: UniProtKB
Cellular component	mitochondrial matrix Ref.1 Non-traceable author statement. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DSTYK	Q6XUX3	1	EBI-1044810,EBI-1049520

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.5
	Modified residue	233	1	N6-acetyllysine Ref.5
Natural variations
	Natural variant	152	1	T → M: dbSNP rs1264895.		VAR_033534
	Natural variant	152	1	T → N: dbSNP rs1264895.		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)
	P24539-1 [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: 1831354] [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: 16710414] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.514870
3D structure databases
SMR	P24539. Positions 121-225.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24539. 5 interactions.
STRING	P24539.
PTM databases
PhosphoSite	P24539.
Proteomic databases
PeptideAtlas	P24539.
PRIDE	P24539.
Genome annotation databases
Ensembl	ENST00000369722; ENSP00000358737; ENSG00000116459; Homo sapiens. [Genome view]
GeneID	515.
KEGG	hsa:515.
UCSC	uc001ebc.1. human.
Organism-specific databases
CTD	515.
GeneCards	GC01P111793.
H-InvDB	HIX0000879.
HGNC	HGNC:840. ATP5F1.
MIM	603270. gene.
PharmGKB	PA25130.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG716119.
HOVERGEN	P24539.
InParanoid	P24539.
OMA	LQATRTF.
OrthoDB	EOG9KSS4S.
Enzyme and pathway databases
Reactome	REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways. REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	P24539.
Bgee	P24539.
CleanEx	HS_ATP5F1.
Genevestigator	P24539.
GermOnline	ENSG00000116459. Homo sapiens.
Family and domain databases
InterPro	IPR008688. ATPase_F0-cplx_bsu_mt. IPR013837. ATPase_F0-cplx_bsu_mt_met. [Graphical view]
PANTHER	PTHR12733. ATPase_F0_B_mt_met. 1 hit.
Pfam	PF05405. Mt_ATP-synt_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	December 15, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.