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Reviewed, UniProtKB/Swiss-Prot P24539 (AT5F1_HUMAN)

Last modified December 15, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP synthase subunit b, mitochondrial
Gene names
Name: ATP5F1
OrganismHomo sapiens (Human) [Complete 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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Sequence similarities

Belongs to the eukaryotic ATPase B chain family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DSTYKQ6XUX31EBI-1044810,EBI-1049520

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion
Chain43 – 256214ATP synthase subunit b, mitochondrial
PRO_0000002513

Amino acid modifications

Modified residue1151N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine By similarity
Modified residue1621N6-acetyllysine By similarity
Modified residue2211N6-acetyllysine Ref.5
Modified residue2331N6-acetyllysine Ref.5

Natural variations

Natural variant1521T → M: dbSNP rs1264895.
VAR_033534
Natural variant1521T → N: dbSNP rs1264895.
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
P24539-1 [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: 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. 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: 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

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.
IPIIPI00029133.
PIRJQ1144.
RefSeqNP_001679.2.
UniGeneHs.514870

3D structure databases

SMRP24539. Positions 121-225.
ModBaseSearch...

Protein-protein interaction databases

IntActP24539. 5 interactions.
STRINGP24539.

PTM databases

PhosphoSiteP24539.

Proteomic databases

PeptideAtlasP24539.
PRIDEP24539.

Genome annotation databases

EnsemblENST00000369722; ENSP00000358737; ENSG00000116459; Homo sapiens. [Genome view]
GeneID515.
KEGGhsa:515.
UCSCuc001ebc.1. human.

Organism-specific databases

CTD515.
GeneCardsGC01P111793.
H-InvDBHIX0000879.
HGNCHGNC:840. ATP5F1.
MIM603270. gene.
PharmGKBPA25130.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG716119.
HOVERGENP24539.
InParanoidP24539.
OMALQATRTF.
OrthoDBEOG9KSS4S.

Enzyme and pathway databases

ReactomeREACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
REACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpressP24539.
BgeeP24539.
CleanExHS_ATP5F1.
GenevestigatorP24539.
GermOnlineENSG00000116459. Homo sapiens.

Family and domain databases

InterProIPR008688. ATPase_F0-cplx_bsu_mt.
IPR013837. ATPase_F0-cplx_bsu_mt_met.
[Graphical view]
PANTHERPTHR12733. ATPase_F0_B_mt_met. 1 hit.
PfamPF05405. Mt_ATP-synt_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio2135.
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: December 15, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents