Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P56480

- ATPB_MOUSE

UniProt

P56480 - ATPB_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Catalytic activityi

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi206 – 2138ATPBy 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

    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.

    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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4646MitochondrionBy similarityAdd
    BLAST
    Chaini47 – 529483ATP synthase subunit beta, mitochondrialPRO_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.2 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → V in AAB86421. (PubMed:10657236)Curated
    Sequence conflicti43 – 431A → V in BAE35088. (PubMed:16141072)Curated
    Sequence conflicti76 – 761D → G in BAE40961. (PubMed:16141072)Curated
    Sequence conflicti92 – 921D → E in AAB86421. (PubMed:10657236)Curated
    Sequence conflicti134 – 1341I → V in BAE31497. (PubMed:16141072)Curated
    Sequence conflicti239 – 2391R → K in AAB86421. (PubMed:10657236)Curated
    Sequence conflicti271 – 2711Q → R in BAE38888. (PubMed:16141072)Curated
    Sequence conflicti271 – 2711Q → R in BAE39301. (PubMed:16141072)Curated
    Sequence conflicti279 – 2802RA → PT in AAB86421. (PubMed:10657236)Curated
    Sequence conflicti288 – 2881T → A in BAE31497. (PubMed:16141072)Curated
    Sequence conflicti288 – 2881T → A in BAE31630. (PubMed:16141072)Curated
    Sequence conflicti375 – 3751T → N in BAE30095. (PubMed:16141072)Curated
    Sequence conflicti383 – 3831T → S in BAB22802. (PubMed:16141072)Curated
    Sequence conflicti433 – 4342SL → FF in AAB86421. (PubMed:10657236)Curated
    Sequence conflicti466 – 4661Q → H in BAB22802. (PubMed:16141072)Curated
    Sequence conflicti469 – 4691Q → R in BAE39797. (PubMed:16141072)Curated
    Sequence conflicti518 – 5181A → V in BAE35331. (PubMed:16141072)Curated

    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

    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: October 1, 2014
    This is version 144 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