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Q03265

- ATPA_MOUSE

UniProt

Q03265 - ATPA_MOUSE

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Protein
ATP synthase subunit alpha, mitochondrial
Gene
Atp5a1
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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei413 – 4131Required for activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2198ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. ATP synthesis coupled proton transport Source: InterPro
  3. lipid metabolic process Source: MGI
  4. negative regulation of endothelial cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:Atp5a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:88115. Atp5a1.

Subcellular locationi

Mitochondrion inner membrane By similarity. Cell membrane; Peripheral membrane protein; Extracellular side By similarity
Note: Colocalizes with HRG on the cell surface of T-cells By similarity.UniRule annotation

GO - Cellular componenti

  1. COP9 signalosome Source: Ensembl
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  4. mitochondrion Source: MGI
  5. plasma membrane Source: UniProtKB-SubCell
  6. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Mitochondrion By similarity
Add
BLAST
Chaini44 – 553510ATP synthase subunit alpha, mitochondrialUniRule annotation
PRO_0000002425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Pyrrolidone carboxylic acid By similarity
Modified residuei76 – 761Phosphoserine1 Publication
Glycosylationi76 – 761O-linked (GlcNAc) By similarity
Modified residuei123 – 1231N6-acetyllysine1 Publication
Modified residuei126 – 1261N6-acetyllysine1 Publication
Modified residuei132 – 1321N6-acetyllysine1 Publication
Modified residuei161 – 1611N6-acetyllysine; alternate1 Publication
Modified residuei161 – 1611N6-succinyllysine; alternate1 Publication
Modified residuei166 – 1661Phosphoserine By similarity
Modified residuei167 – 1671N6-acetyllysine; alternate1 Publication
Modified residuei167 – 1671N6-succinyllysine; alternate1 Publication
Modified residuei230 – 2301N6-acetyllysine; alternate1 Publication
Modified residuei230 – 2301N6-succinyllysine; alternate1 Publication
Modified residuei239 – 2391N6-acetyllysine; alternate1 Publication
Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
Modified residuei240 – 2401N6-acetyllysine1 Publication
Modified residuei261 – 2611N6-acetyllysine; alternate1 Publication
Modified residuei261 – 2611N6-succinyllysine; alternate1 Publication
Modified residuei305 – 3051N6-acetyllysine; alternate1 Publication
Modified residuei305 – 3051N6-succinyllysine; alternate1 Publication
Modified residuei427 – 4271N6-acetyllysine; alternate1 Publication
Modified residuei427 – 4271N6-succinyllysine; alternate1 Publication
Modified residuei434 – 4341N6-acetyllysine1 Publication
Modified residuei498 – 4981N6-acetyllysine; alternate2 Publications
Modified residuei498 – 4981N6-succinyllysine; alternate1 Publication
Modified residuei506 – 5061N6-acetyllysine; alternate1 Publication
Modified residuei506 – 5061N6-succinyllysine; alternate1 Publication
Modified residuei531 – 5311N6-acetyllysine; alternate2 Publications
Modified residuei531 – 5311N6-succinyllysine; alternate1 Publication
Modified residuei539 – 5391N6-acetyllysine; alternate2 Publications
Modified residuei539 – 5391N6-succinyllysine; alternate1 Publication
Modified residuei541 – 5411N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.UniRule annotation
Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity.UniRule annotation

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiQ03265.
PaxDbiQ03265.
PRIDEiQ03265.

2D gel databases

REPRODUCTION-2DPAGEIPI00130280.
Q03265.
SWISS-2DPAGEQ03265.
UCD-2DPAGEQ03265.

PTM databases

PhosphoSiteiQ03265.

Expressioni

Gene expression databases

BgeeiQ03265.
GenevestigatoriQ03265.

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. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin. 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 BLOC1S1. 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.

Protein-protein interaction databases

BioGridi198253. 13 interactions.
IntActiQ03265. 18 interactions.
MINTiMINT-1859704.

Structurei

3D structure databases

ProteinModelPortaliQ03265.
SMRiQ03265. Positions 56-552.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiQ03265.
KOiK02132.
OMAiTPYPVED.
OrthoDBiEOG773XFP.
PhylomeDBiQ03265.
TreeFamiTF300321.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
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]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 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.

Q03265-1 [UniParc]FASTAAdd to Basket

« Hide

MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE    50
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 100
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV 150
VDALGNAIDG KGPIGSKTRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 200
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 250
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 300
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 350
RAAKMNDSFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 400
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 450
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 500
PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL KEIVTNFLAG 550
FEP 553
Length:553
Mass (Da):59,753
Last modified:October 1, 1993 - v1
Checksum:iCF35B4FBA7ED431D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → T in BAE37632. 1 Publication
Sequence conflicti63 – 631D → Y in BAE34114. 1 Publication
Sequence conflicti119 – 1191F → L in BAE34114. 1 Publication
Sequence conflicti126 – 1261K → N in BAE34114. 1 Publication
Sequence conflicti315 – 3151S → Y in BAE34114. 1 Publication
Sequence conflicti321 – 3211Y → C in BAE40868. 1 Publication
Sequence conflicti422 – 45635Missing in BAE27439. 1 Publication
Add
BLAST
Sequence conflicti486 – 4861A → T in BAE40158. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01062 mRNA. Translation: AAA37271.1.
AK043976 mRNA. Translation: BAC31722.1.
AK076572 mRNA. Translation: BAC36399.1.
AK146797 mRNA. Translation: BAE27439.1.
AK150426 mRNA. Translation: BAE29549.1.
AK150843 mRNA. Translation: BAE29901.1.
AK151004 mRNA. Translation: BAE30027.1.
AK151128 mRNA. Translation: BAE30136.1.
AK151224 mRNA. Translation: BAE30216.1.
AK151920 mRNA. Translation: BAE30798.1.
AK152054 mRNA. Translation: BAE30910.1.
AK152890 mRNA. Translation: BAE31573.1.
AK157529 mRNA. Translation: BAE34114.1.
AK159540 mRNA. Translation: BAE35167.1.
AK159491 mRNA. Translation: BAE35125.1.
AK159758 mRNA. Translation: BAE35349.1.
AK160043 mRNA. Translation: BAE35585.1.
AK164110 mRNA. Translation: BAE37632.1.
AK164193 mRNA. Translation: BAE37675.1.
AK166709 mRNA. Translation: BAE38962.1.
AK166812 mRNA. Translation: BAE39039.1.
AK167159 mRNA. Translation: BAE39300.1.
AK167863 mRNA. Translation: BAE39881.1.
AK168198 mRNA. Translation: BAE40158.1.
AK168617 mRNA. Translation: BAE40482.1.
AK168879 mRNA. Translation: BAE40697.1.
AK168890 mRNA. Translation: BAE40707.1.
AK168932 mRNA. Translation: BAE40744.1.
AK169080 mRNA. Translation: BAE40864.1.
AK169084 mRNA. Translation: BAE40868.1.
AK169105 mRNA. Translation: BAE40887.1.
AK169142 mRNA. Translation: BAE40921.1.
AK169300 mRNA. Translation: BAE41056.1.
AK169308 mRNA. Translation: BAE41063.1.
AK169414 mRNA. Translation: BAE41160.1.
BC014854 mRNA. Translation: AAH14854.1.
CCDSiCCDS29358.1.
PIRiJC1473.
RefSeqiNP_031531.1. NM_007505.2.
UniGeneiMm.276137.

Genome annotation databases

EnsembliENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneIDi11946.
KEGGimmu:11946.
UCSCiuc008fru.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01062 mRNA. Translation: AAA37271.1 .
AK043976 mRNA. Translation: BAC31722.1 .
AK076572 mRNA. Translation: BAC36399.1 .
AK146797 mRNA. Translation: BAE27439.1 .
AK150426 mRNA. Translation: BAE29549.1 .
AK150843 mRNA. Translation: BAE29901.1 .
AK151004 mRNA. Translation: BAE30027.1 .
AK151128 mRNA. Translation: BAE30136.1 .
AK151224 mRNA. Translation: BAE30216.1 .
AK151920 mRNA. Translation: BAE30798.1 .
AK152054 mRNA. Translation: BAE30910.1 .
AK152890 mRNA. Translation: BAE31573.1 .
AK157529 mRNA. Translation: BAE34114.1 .
AK159540 mRNA. Translation: BAE35167.1 .
AK159491 mRNA. Translation: BAE35125.1 .
AK159758 mRNA. Translation: BAE35349.1 .
AK160043 mRNA. Translation: BAE35585.1 .
AK164110 mRNA. Translation: BAE37632.1 .
AK164193 mRNA. Translation: BAE37675.1 .
AK166709 mRNA. Translation: BAE38962.1 .
AK166812 mRNA. Translation: BAE39039.1 .
AK167159 mRNA. Translation: BAE39300.1 .
AK167863 mRNA. Translation: BAE39881.1 .
AK168198 mRNA. Translation: BAE40158.1 .
AK168617 mRNA. Translation: BAE40482.1 .
AK168879 mRNA. Translation: BAE40697.1 .
AK168890 mRNA. Translation: BAE40707.1 .
AK168932 mRNA. Translation: BAE40744.1 .
AK169080 mRNA. Translation: BAE40864.1 .
AK169084 mRNA. Translation: BAE40868.1 .
AK169105 mRNA. Translation: BAE40887.1 .
AK169142 mRNA. Translation: BAE40921.1 .
AK169300 mRNA. Translation: BAE41056.1 .
AK169308 mRNA. Translation: BAE41063.1 .
AK169414 mRNA. Translation: BAE41160.1 .
BC014854 mRNA. Translation: AAH14854.1 .
CCDSi CCDS29358.1.
PIRi JC1473.
RefSeqi NP_031531.1. NM_007505.2.
UniGenei Mm.276137.

3D structure databases

ProteinModelPortali Q03265.
SMRi Q03265. Positions 56-552.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198253. 13 interactions.
IntActi Q03265. 18 interactions.
MINTi MINT-1859704.

PTM databases

PhosphoSitei Q03265.

2D gel databases

REPRODUCTION-2DPAGE IPI00130280.
Q03265.
SWISS-2DPAGE Q03265.
UCD-2DPAGE Q03265.

Proteomic databases

MaxQBi Q03265.
PaxDbi Q03265.
PRIDEi Q03265.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000026495 ; ENSMUSP00000026495 ; ENSMUSG00000025428 .
GeneIDi 11946.
KEGGi mmu:11946.
UCSCi uc008fru.1. mouse.

Organism-specific databases

CTDi 498.
MGIi MGI:88115. Atp5a1.

Phylogenomic databases

eggNOGi COG0056.
GeneTreei ENSGT00550000074846.
HOVERGENi HBG001536.
InParanoidi Q03265.
KOi K02132.
OMAi TPYPVED.
OrthoDBi EOG773XFP.
PhylomeDBi Q03265.
TreeFami TF300321.

Miscellaneous databases

ChiTaRSi ATP5A1. mouse.
NextBioi 280057.
PROi Q03265.
SOURCEi Search...

Gene expression databases

Bgeei Q03265.
Genevestigatori Q03265.

Family and domain databases

Gene3Di 2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01346. ATP_synth_alpha_bact.
InterProi IPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
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 ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00962. atpA. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression analysis of the alpha subunit of mouse ATP synthase."
    Yotov W.V., St Arnaud R.
    Biochem. Biophys. Res. Commun. 191:142-148(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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, C57BL/6J and NOD.
    Tissue: Heart, Hippocampus, Liver, Spinal cord and Spleen.
  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].
    Tissue: Eye.
  4. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
    Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
    Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "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-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATPA_MOUSE
AccessioniPrimary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0
, Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 149 of the entry and version 1 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

Similar proteinsi