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P06576 (ATPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit beta, mitochondrial

EC=3.6.3.14
Gene names
Name:ATP5B
Synonyms:ATPMB, ATPSB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 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. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. HAMAP-Rule MF_01347

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347

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. Interacts with PPIF. Interacts with BCL2L1 isoform BCL-X(L);the interaction mediates the association of BCL2L1 isoform BCL-X(L)with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency By similarity.

Subcellular location

Mitochondrion. Mitochondrion inner membrane. Note: Peripheral membrane protein. HAMAP-Rule MF_01347

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

ATP catabolic process

Inferred from direct assay PubMed 12110673. Source: GOC

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

angiogenesis

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

generation of precursor metabolites and energy

Non-traceable author statement Ref.3. Source: UniProtKB

lipid metabolic process

Inferred from electronic annotation. Source: Ensembl

mitochondrial ATP synthesis coupled proton transport

Inferred by curator PubMed 12110673. Source: UniProtKB

negative regulation of cell adhesion involved in substrate-bound cell migration

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from direct assay PubMed 16210410. Source: UniProt

proton transport

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

regulation of intracellular pH

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcell surface

Inferred from direct assay PubMed 17510399. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

membrane

Inferred from direct assay PubMed 16210410. Source: UniProt

mitochondrial matrix

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

mitochondrial membrane

Inferred from direct assay PubMed 8006588. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrial proton-transporting ATP synthase, catalytic core

Non-traceable author statement Ref.3. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 10077593. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MHC class I protein binding

Inferred from direct assay PubMed 17643490. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11410595. Source: UniProtKB

proton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from mutant phenotype PubMed 17510399. Source: UniProtKB

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

transporter activity

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAZP631042EBI-356231,EBI-347088

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Ref.7
Chain48 – 529482ATP synthase subunit beta, mitochondrial HAMAP-Rule MF_01347
PRO_0000002443

Regions

Nucleotide binding206 – 2138ATP By similarity

Amino acid modifications

Modified residue1241N6-acetyllysine; alternate By similarity
Modified residue1241N6-succinyllysine; alternate By similarity
Modified residue1331N6-acetyllysine; alternate Ref.12
Modified residue1331N6-succinyllysine; alternate By similarity
Modified residue1611N6-acetyllysine; alternate By similarity
Modified residue1611N6-succinyllysine; alternate By similarity
Modified residue1981N6-acetyllysine Ref.12
Modified residue2591N6-acetyllysine; alternate By similarity
Modified residue2591N6-succinyllysine; alternate By similarity
Modified residue2641N6-acetyllysine; alternate By similarity
Modified residue2641N6-succinyllysine; alternate By similarity
Modified residue4261N6-acetyllysine Ref.12
Modified residue4801N6-acetyllysine By similarity
Modified residue4851N6-acetyllysine By similarity
Modified residue5221N6-acetyllysine; alternate By similarity
Modified residue5221N6-succinyllysine; alternate By similarity
Modified residue5291Phosphoserine By similarity

Natural variations

Natural variant2741E → Q. Ref.2 Ref.3
Corresponds to variant rs1042001 [ dbSNP | Ensembl ].
VAR_048371

Experimental info

Sequence conflict1 – 66MLGFVG → MTSLWGKGTGCKLFKF in BAA00016. Ref.3
Sequence conflict1 – 66MLGFVG → MTSLWGKGTGCKLFKF in CAA27246. Ref.3
Sequence conflict36 – 405APTAV → VRRRF in AAA51808. Ref.2
Sequence conflict36 – 405APTAV → VRRRS in BAA00016. Ref.3
Sequence conflict36 – 405APTAV → VRRRS in CAA27246. Ref.3
Sequence conflict130 – 1323API → DQL in AAA51808. Ref.2
Sequence conflict3781H → D in AAA51808. Ref.2
Sequence conflict4351Q → H in AAA51808. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06576 [UniParc].

Last modified April 1, 1990. Version 3.
Checksum: 960C616A2252B91A

FASTA52956,560
        10         20         30         40         50         60 
MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT SPSPKAGAAT 

        70         80         90        100        110        120 
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV 

       130        140        150        160        170        180 
RGQKVLDSGA PIKIPVGPET LGRIMNVIGE PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 

       190        200        210        220        230        240 
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT 

       250        260        270        280        290        300 
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 

       310        320        330        340        350        360 
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI 

       370        380        390        400        410        420 
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV 

       430        440        450        460        470        480 
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHMGK 

       490        500        510        520 
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHSS 

« Hide

References

« Hide 'large scale' references
[1]"The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression."
Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C.
Genomics 5:829-843(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit."
Ohta S., Tomura H., Matsuda K., Kagawa Y.
J. Biol. Chem. 263:11257-11262(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-274.
[3]"Human F1-ATPase: molecular cloning of cDNA for the beta subunit."
Ohta S., Kagawa Y.
J. Biochem. 99:135-141(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-274.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Placenta.
[7]"Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
Xu G., Shin S.B., Jaffrey S.R.
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63.
Tissue: Leukemic T-cell.
[8]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259; 265-279; 282-345; 388-422; 433-456 AND 490-519, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations."
Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A., Greenberg B.D.
Curr. Genet. 12:81-90(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
[10]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324.
Tissue: Adipocyte.
[11]Bienvenut W.V.
Submitted (MAR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259; 265-279; 282-345; 407-422 AND 463-480, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[12]"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-133; LYS-198 AND LYS-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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
M27132 Genomic DNA. Translation: AAA51809.1.
M19483, M19482 Genomic DNA. Translation: AAA51808.1.
X03559 mRNA. Translation: CAA27246.1.
D00022 mRNA. Translation: BAA00016.1.
AK291085 mRNA. Translation: BAF83774.1.
CH471054 Genomic DNA. Translation: EAW96952.1.
BC016512 mRNA. Translation: AAH16512.1.
X05606 mRNA. Translation: CAA29095.1.
CCDSCCDS8924.1.
PIRA33370.
RefSeqNP_001677.2. NM_001686.3.
UniGeneHs.406510.

3D structure databases

ProteinModelPortalP06576.
SMRP06576. Positions 60-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106994. 84 interactions.
IntActP06576. 37 interactions.
MINTMINT-5004016.
STRING9606.ENSP00000262030.

Chemistry

ChEMBLCHEMBL2062350.

PTM databases

PhosphoSiteP06576.

Polymorphism databases

DMDM114549.

2D gel databases

DOSAC-COBS-2DPAGEP06576.
OGPP06576.
REPRODUCTION-2DPAGEIPI00303476.
P06576.
SWISS-2DPAGEP06576.
UCD-2DPAGEP06576.

Proteomic databases

MaxQBP06576.
PaxDbP06576.
PRIDEP06576.

Protocols and materials databases

DNASU506.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262030; ENSP00000262030; ENSG00000110955.
GeneID506.
KEGGhsa:506.
UCSCuc001slr.3. human.

Organism-specific databases

CTD506.
GeneCardsGC12M057031.
HGNCHGNC:830. ATP5B.
HPACAB017527.
HPA001520.
HPA001528.
MIM102910. gene.
neXtProtNX_P06576.
PharmGKBPA25122.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0055.
HOGENOMHOG000009605.
HOVERGENHBG004307.
InParanoidP06576.
KOK02133.
OMAVSEILVT.
OrthoDBEOG73V6K6.
PhylomeDBP06576.
TreeFamTF105640.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
REACT_200751. Organelle biogenesis and maintenance.

Gene expression databases

ArrayExpressP06576.
BgeeP06576.
CleanExHS_ATP5B.
GenevestigatorP06576.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01347. ATP_synth_beta_bact.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5B. human.
GeneWikiATP5B.
GenomeRNAi506.
NextBio2109.
PROP06576.
SOURCESearch...

Entry information

Entry nameATPB_HUMAN
AccessionPrimary (citable) accession number: P06576
Secondary accession number(s): A8K4X0, Q14283
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 176 of the entry and version 3 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 12

Human chromosome 12: entries, gene names and cross-references to MIM