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P56480 (ATPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 subunit beta, mitochondrial

EC=3.6.3.14
Gene names
Name:Atp5b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.7

Subcellular location

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

Post-translational modification

Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice. HAMAP-Rule MF_01347

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence caution

The sequence AAH37127.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

ATP synthesis coupled proton transport

Inferred from electronic annotation. Source: InterPro

angiogenesis

Inferred from electronic annotation. Source: Ensembl

lipid metabolic process

Inferred from mutant phenotype PubMed 17612527. Source: MGI

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

Inferred from mutant phenotype PubMed 17612527. Source: MGI

regulation of intracellular pH

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial nucleoid

Inferred from electronic annotation. Source: Ensembl

mitochondrial proton-transporting ATP synthase complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

proton-transporting ATP synthase complex, catalytic core F(1)

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion By similarity
Chain47 – 529483ATP synthase subunit beta, mitochondrial HAMAP-Rule MF_01347
PRO_0000002444

Regions

Nucleotide binding206 – 2138ATP By similarity

Amino acid modifications

Modified residue1241N6-acetyllysine; alternate Ref.9
Modified residue1241N6-succinyllysine; alternate Ref.8
Modified residue1331N6-acetyllysine; alternate Ref.9
Modified residue1331N6-succinyllysine; alternate Ref.8
Modified residue1611N6-acetyllysine; alternate Ref.9
Modified residue1611N6-succinyllysine; alternate Ref.8
Modified residue1981N6-acetyllysine Ref.9
Modified residue2591N6-acetyllysine; alternate Ref.9
Modified residue2591N6-succinyllysine; alternate Ref.8
Modified residue2641N6-acetyllysine; alternate Ref.9
Modified residue2641N6-succinyllysine; alternate Ref.8
Modified residue4261N6-acetyllysine Ref.9
Modified residue4801N6-acetyllysine Ref.9
Modified residue4851N6-acetyllysine Ref.9
Modified residue5221N6-acetyllysine; alternate Ref.8 Ref.9
Modified residue5221N6-succinyllysine; alternate Ref.8
Modified residue5291Phosphoserine Ref.6

Experimental info

Sequence conflict251A → V in AAB86421. Ref.1
Sequence conflict431A → V in BAE35088. Ref.2
Sequence conflict761D → G in BAE40961. Ref.2
Sequence conflict921D → E in AAB86421. Ref.1
Sequence conflict1341I → V in BAE31497. Ref.2
Sequence conflict2391R → K in AAB86421. Ref.1
Sequence conflict2711Q → R in BAE38888. Ref.2
Sequence conflict2711Q → R in BAE39301. Ref.2
Sequence conflict279 – 2802RA → PT in AAB86421. Ref.1
Sequence conflict2881T → A in BAE31497. Ref.2
Sequence conflict2881T → A in BAE31630. Ref.2
Sequence conflict3751T → N in BAE30095. Ref.2
Sequence conflict3831T → S in BAB22802. Ref.2
Sequence conflict433 – 4342SL → FF in AAB86421. Ref.1
Sequence conflict4661Q → H in BAB22802. Ref.2
Sequence conflict4691Q → R in BAE39797. Ref.2
Sequence conflict5181A → V in BAE35331. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P56480 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: F3E1100C390A78A7

FASTA52956,300
        10         20         30         40         50         60 
MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA SAAPKAGTAT 

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

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

       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 NIVGNEHYDV 

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

       490        500        510        520 
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHGS 

« Hide

References

« Hide 'large scale' references
[1]"A novel principle for conferring selectivity to poly(A)-binding proteins: interdependence of two ATP synthase beta-subunit mRNA-binding proteins."
Andersson U., Antonicka H., Houstek J., Cannon B.
Biochem. J. 346:33-39(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c and C57BL/6J.
Tissue: Amnion, Bone marrow, Embryonic stem cell, Heart, Kidney, Liver, Spinal ganglion and Sympathetic ganglion.
[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].
Strain: Czech II and FVB/N.
Tissue: Mammary tumor, Retina and Salivary gland.
[4]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-509.
Tissue: Liver.
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 162-198; 202-239; 242-259; 265-279; 282-345; 352-422; 433-456 AND 463-489, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels."
Chinopoulos C., Konrad C., Kiss G., Metelkin E., Torocsik B., Zhang S.F., Starkov A.A.
FEBS J. 278:1112-1125(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIF.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-522, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-124; LYS-133; LYS-161; LYS-259; LYS-264 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[9]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124; LYS-133; LYS-161; LYS-198; LYS-259; LYS-264; LYS-426; LYS-480; LYS-485 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030559 mRNA. Translation: AAB86421.1.
AK003460 mRNA. Translation: BAB22802.1.
AK010314 mRNA. Translation: BAB26846.1.
AK084009 mRNA. Translation: BAC39095.1.
AK145684 mRNA. Translation: BAE26587.1.
AK148891 mRNA. Translation: BAE28692.1.
AK150599 mRNA. Translation: BAE29691.1.
AK151081 mRNA. Translation: BAE30095.1.
AK151600 mRNA. Translation: BAE30540.1.
AK152788 mRNA. Translation: BAE31497.1.
AK152976 mRNA. Translation: BAE31630.1.
AK153099 mRNA. Translation: BAE31720.1.
AK159444 mRNA. Translation: BAE35088.1.
AK159737 mRNA. Translation: BAE35331.1.
AK159978 mRNA. Translation: BAE35529.1.
AK160199 mRNA. Translation: BAE35689.1.
AK160608 mRNA. Translation: BAE35911.1.
AK164383 mRNA. Translation: BAE37764.1.
AK166525 mRNA. Translation: BAE38829.1.
AK166603 mRNA. Translation: BAE38888.1.
AK166979 mRNA. Translation: BAE39161.1.
AK167119 mRNA. Translation: BAE39267.1.
AK167160 mRNA. Translation: BAE39301.1.
AK167728 mRNA. Translation: BAE39769.1.
AK167764 mRNA. Translation: BAE39797.1.
AK168692 mRNA. Translation: BAE40537.1.
AK168941 mRNA. Translation: BAE40749.1.
AK169184 mRNA. Translation: BAE40961.1.
BC018392 mRNA. Translation: AAH18392.1.
BC037127 mRNA. Translation: AAH37127.1. Different initiation.
BC046616 mRNA. Translation: AAH46616.1.
DQ403100 mRNA. Translation: ABD77233.1.
RefSeqNP_058054.2. NM_016774.3.
UniGeneMm.238973.

3D structure databases

ProteinModelPortalP56480.
SMRP56480. Positions 51-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198254. 5 interactions.
IntActP56480. 31 interactions.
MINTMINT-4996869.

PTM databases

PhosphoSiteP56480.

2D gel databases

COMPLUYEAST-2DPAGEP56480.
REPRODUCTION-2DPAGEIPI00468481.
P56480.
SWISS-2DPAGEP56480.
UCD-2DPAGEP56480.

Proteomic databases

PaxDbP56480.
PRIDEP56480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393.
GeneID11947.
KEGGmmu:11947.
UCSCuc007hle.1. mouse.

Organism-specific databases

CTD506.
MGIMGI:107801. Atp5b.

Phylogenomic databases

eggNOGCOG0055.
GeneTreeENSGT00550000074800.
HOVERGENHBG004307.
InParanoidP56480.
KOK02133.
OMAEPYAKGG.
OrthoDBEOG73V6K6.
PhylomeDBP56480.
TreeFamTF105640.

Gene expression databases

BgeeP56480.
GenevestigatorP56480.

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]
PANTHERPTHR15184:SF8. PTHR15184:SF8. 1 hit.
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. mouse.
NextBio280061.
PROP56480.
SOURCESearch...

Entry information

Entry nameATPB_MOUSE
AccessionPrimary (citable) accession number: P56480
Secondary accession number(s): Q0QEP4 expand/collapse secondary AC list , Q3TFD7, Q3TIP9, Q3TK44, Q3TWD5, Q3TX28, Q3U6U4, Q3U774, Q3UB69, Q3UF69, Q8CI65, Q8VEJ5, Q9CTI7, Q9CWX7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot