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P56480

- ATPB_MOUSE

UniProt

P56480 - ATPB_MOUSE

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Protein

ATP synthase subunit beta, mitochondrial

Gene
Atp5b
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: Ensembl
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. ATP hydrolysis coupled proton transport Source: InterPro
  3. ATP synthesis coupled proton transport Source: InterPro
  4. lipid metabolic process Source: MGI
  5. negative regulation of cell adhesion involved in substrate-bound cell migration Source: MGI
  6. regulation of intracellular pH Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199101. Mitochondrial protein import.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:Atp5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:107801. Atp5b.

Subcellular locationi

Mitochondrion. Mitochondrion inner membrane
Note: Peripheral membrane protein.UniRule annotation

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial nucleoid Source: Ensembl
  4. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  5. mitochondrion Source: MGI
  6. plasma membrane Source: Ensembl
  7. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646Mitochondrion By similarityAdd
BLAST
Chaini47 – 529483ATP synthase subunit beta, mitochondrialUniRule annotationPRO_0000002444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061O-linked (GlcNAc) By similarity
Modified residuei124 – 1241N6-acetyllysine; alternate1 Publication
Modified residuei124 – 1241N6-succinyllysine; alternate1 Publication
Modified residuei133 – 1331N6-acetyllysine; alternate1 Publication
Modified residuei133 – 1331N6-succinyllysine; alternate1 Publication
Modified residuei161 – 1611N6-acetyllysine; alternate1 Publication
Modified residuei161 – 1611N6-succinyllysine; alternate1 Publication
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei259 – 2591N6-acetyllysine; alternate1 Publication
Modified residuei259 – 2591N6-succinyllysine; alternate1 Publication
Modified residuei264 – 2641N6-acetyllysine; alternate1 Publication
Modified residuei264 – 2641N6-succinyllysine; alternate1 Publication
Modified residuei426 – 4261N6-acetyllysine1 Publication
Modified residuei480 – 4801N6-acetyllysine1 Publication
Modified residuei485 – 4851N6-acetyllysine1 Publication
Modified residuei522 – 5221N6-acetyllysine; alternate2 Publications
Modified residuei522 – 5221N6-succinyllysine; alternate1 Publication
Modified residuei529 – 5291Phosphoserine1 Publication

Post-translational modificationi

Acetylation of Lys-133 is observed in liver mitochondria from fasted mice but not from fed mice.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP56480.
PaxDbiP56480.
PRIDEiP56480.

2D gel databases

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

PTM databases

PhosphoSiteiP56480.

Expressioni

Gene expression databases

BgeeiP56480.
GenevestigatoriP56480.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi198254. 6 interactions.
IntActiP56480. 32 interactions.
MINTiMINT-4996869.

Structurei

3D structure databases

ProteinModelPortaliP56480.
SMRiP56480. Positions 51-527.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0055.
GeneTreeiENSGT00550000074800.
HOVERGENiHBG004307.
InParanoidiP56480.
KOiK02133.
OMAiKYLSQPF.
OrthoDBiEOG73V6K6.
PhylomeDBiP56480.
TreeFamiTF105640.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. 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]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56480-1 [UniParc]FASTAAdd to Basket

« Hide

MLSLVGRVAS ASASGALRGL SPSAALPQAQ LLLRAAPAGV HPARDYAAQA    50
SAAPKAGTAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RDSRLVLEVA 100
QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE 150
PIDERGPIKT KQFAPIHAEA PEFIEMSVEQ EILVTGIKVV DLLAPYAKGG 200
KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM 250
IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD 300
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK 350
KGSITSVQAI YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP 400
LDSTSRIMDP NIVGNEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED 450
KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD 500
HLPEQAFYMV GPIEEAVAKA DKLAEEHGS 529
Length:529
Mass (Da):56,300
Last modified:May 2, 2002 - v2
Checksum:iF3E1100C390A78A7
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → V in AAB86421. 1 Publication
Sequence conflicti43 – 431A → V in BAE35088. 1 Publication
Sequence conflicti76 – 761D → G in BAE40961. 1 Publication
Sequence conflicti92 – 921D → E in AAB86421. 1 Publication
Sequence conflicti134 – 1341I → V in BAE31497. 1 Publication
Sequence conflicti239 – 2391R → K in AAB86421. 1 Publication
Sequence conflicti271 – 2711Q → R in BAE38888. 1 Publication
Sequence conflicti271 – 2711Q → R in BAE39301. 1 Publication
Sequence conflicti279 – 2802RA → PT in AAB86421. 1 Publication
Sequence conflicti288 – 2881T → A in BAE31497. 1 Publication
Sequence conflicti288 – 2881T → A in BAE31630. 1 Publication
Sequence conflicti375 – 3751T → N in BAE30095. 1 Publication
Sequence conflicti383 – 3831T → S in BAB22802. 1 Publication
Sequence conflicti433 – 4342SL → FF in AAB86421. 1 Publication
Sequence conflicti466 – 4661Q → H in BAB22802. 1 Publication
Sequence conflicti469 – 4691Q → R in BAE39797. 1 Publication
Sequence conflicti518 – 5181A → V in BAE35331. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24259.1.
RefSeqiNP_058054.2. NM_016774.3.
UniGeneiMm.238973.

Genome annotation databases

EnsembliENSMUST00000026459; ENSMUSP00000026459; ENSMUSG00000025393.
GeneIDi11947.
KEGGimmu:11947.
UCSCiuc007hle.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24259.1.
RefSeqi NP_058054.2. NM_016774.3.
UniGenei Mm.238973.

3D structure databases

ProteinModelPortali P56480.
SMRi P56480. Positions 51-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198254. 6 interactions.
IntActi P56480. 32 interactions.
MINTi MINT-4996869.

PTM databases

PhosphoSitei P56480.

2D gel databases

COMPLUYEAST-2DPAGE P56480.
REPRODUCTION-2DPAGE IPI00468481.
P56480.
SWISS-2DPAGE P56480.
UCD-2DPAGE P56480.

Proteomic databases

MaxQBi P56480.
PaxDbi P56480.
PRIDEi P56480.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026459 ; ENSMUSP00000026459 ; ENSMUSG00000025393 .
GeneIDi 11947.
KEGGi mmu:11947.
UCSCi uc007hle.1. mouse.

Organism-specific databases

CTDi 506.
MGIi MGI:107801. Atp5b.

Phylogenomic databases

eggNOGi COG0055.
GeneTreei ENSGT00550000074800.
HOVERGENi HBG004307.
InParanoidi P56480.
KOi K02133.
OMAi KYLSQPF.
OrthoDBi EOG73V6K6.
PhylomeDBi P56480.
TreeFami TF105640.

Enzyme and pathway databases

Reactomei REACT_199101. Mitochondrial protein import.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSi ATP5B. mouse.
NextBioi 280061.
PROi P56480.
SOURCEi Search...

Gene expression databases

Bgeei P56480.
Genevestigatori P56480.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01347. ATP_synth_beta_bact.
InterProi IPR003593. 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 ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01039. atpD. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiATPB_MOUSE
AccessioniPrimary (citable) accession number: P56480
Secondary accession number(s): Q0QEP4
, Q3TFD7, Q3TIP9, Q3TK44, Q3TWD5, Q3TX28, Q3U6U4, Q3U774, Q3UB69, Q3UF69, Q8CI65, Q8VEJ5, Q9CTI7, Q9CWX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 2, 2002
Last modified: September 3, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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