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Q03265

- ATPA_MOUSE

UniProt

Q03265 - ATPA_MOUSE

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
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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.By similarity

    Sites

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

    Regions

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

    GO - Molecular functioni

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

    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

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

    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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionBy similarityAdd
    BLAST
    Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002425Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441Pyrrolidone carboxylic acidBy 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 – 1661PhosphoserineBy 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.2 Publications
    Acetylated on lysine residues. BLOC1S1 is required for acetylation By similarity.By similarity

    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.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ03265.
    SMRiQ03265. Positions 56-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    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

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    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31S → T in BAE37632. (PubMed:16141072)Curated
    Sequence conflicti63 – 631D → Y in BAE34114. (PubMed:16141072)Curated
    Sequence conflicti119 – 1191F → L in BAE34114. (PubMed:16141072)Curated
    Sequence conflicti126 – 1261K → N in BAE34114. (PubMed:16141072)Curated
    Sequence conflicti315 – 3151S → Y in BAE34114. (PubMed:16141072)Curated
    Sequence conflicti321 – 3211Y → C in BAE40868. (PubMed:16141072)Curated
    Sequence conflicti422 – 45635Missing in BAE27439. (PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti486 – 4861A → T in BAE40158. (PubMed:16141072)Curated

    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

    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: October 1, 2014
    This is version 150 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