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P06576

- ATPB_HUMAN

UniProt

P06576 - ATPB_HUMAN

Protein

ATP synthase subunit beta, mitochondrial

Gene

ATP5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 3 (01 Apr 1990)
      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.

    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. MHC class I protein binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. proton-transporting ATPase activity, rotational mechanism Source: UniProtKB
    5. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro
    6. transmembrane transporter activity Source: UniProtKB
    7. transporter activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. ATP biosynthetic process Source: UniProtKB
    3. ATP catabolic process Source: GOC
    4. ATP hydrolysis coupled proton transport Source: InterPro
    5. cellular metabolic process Source: Reactome
    6. generation of precursor metabolites and energy Source: UniProtKB
    7. lipid metabolic process Source: Ensembl
    8. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    9. negative regulation of cell adhesion involved in substrate-bound cell migration Source: Ensembl
    10. osteoblast differentiation Source: UniProt
    11. proton transport Source: UniProtKB
    12. regulation of intracellular pH Source: UniProtKB
    13. respiratory electron transport chain Source: Reactome
    14. small molecule metabolic process Source: Reactome

    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_118595. Mitochondrial protein import.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_6759. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
    Gene namesi
    Name:ATP5B
    Synonyms:ATPMB, ATPSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:830. ATP5B.

    Subcellular locationi

    Mitochondrion. Mitochondrion inner membrane
    Note: Peripheral membrane protein.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. mitochondrial matrix Source: UniProtKB
    5. mitochondrial membrane Source: UniProtKB
    6. mitochondrial nucleoid Source: BHF-UCL
    7. mitochondrial proton-transporting ATP synthase, catalytic core Source: UniProtKB
    8. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    9. mitochondrion Source: UniProtKB
    10. nucleus Source: UniProt
    11. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25122.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4747Mitochondrion1 PublicationAdd
    BLAST
    Chaini48 – 529482ATP synthase subunit beta, mitochondrialPRO_0000002443Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP06576.
    PaxDbiP06576.
    PRIDEiP06576.

    2D gel databases

    DOSAC-COBS-2DPAGEP06576.
    OGPiP06576.
    REPRODUCTION-2DPAGEIPI00303476.
    P06576.
    SWISS-2DPAGEP06576.
    UCD-2DPAGEP06576.

    PTM databases

    PhosphoSiteiP06576.

    Expressioni

    Gene expression databases

    ArrayExpressiP06576.
    BgeeiP06576.
    CleanExiHS_ATP5B.
    GenevestigatoriP06576.

    Organism-specific databases

    HPAiCAB017527.
    HPA001520.
    HPA001528.

    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 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHAZP631042EBI-356231,EBI-347088

    Protein-protein interaction databases

    BioGridi106994. 83 interactions.
    IntActiP06576. 38 interactions.
    MINTiMINT-5004016.
    STRINGi9606.ENSP00000262030.

    Structurei

    3D structure databases

    ProteinModelPortaliP06576.
    SMRiP06576. Positions 60-525.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase alpha/beta chains family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0055.
    HOGENOMiHOG000009605.
    HOVERGENiHBG004307.
    InParanoidiP06576.
    KOiK02133.
    OMAiVSEILVT.
    OrthoDBiEOG73V6K6.
    PhylomeDBiP06576.
    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]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

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

    P06576-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGFVGRVAA APASGALRRL TPSASLPPAQ LLLRAAPTAV HPVRDYAAQT    50
    SPSPKAGAAT GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA 100
    QHLGESTVRT IAMDGTEGLV RGQKVLDSGA PIKIPVGPET LGRIMNVIGE 150
    PIDERGPIKT KQFAPIHAEA PEFMEMSVEQ 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 NIVGSEHYDV ARGVQKILQD YKSLQDIIAI LGMDELSEED 450
    KLTVSRARKI QRFLSQPFQV AEVFTGHMGK LVPLKETIKG FQQILAGEYD 500
    HLPEQAFYMV GPIEEAVAKA DKLAEEHSS 529
    Length:529
    Mass (Da):56,560
    Last modified:April 1, 1990 - v3
    Checksum:i960C616A2252B91A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti274 – 2741E → Q.2 Publications
    Corresponds to variant rs1042001 [ dbSNP | Ensembl ].
    VAR_048371

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in BAA00016. (PubMed:2870059)Curated
    Sequence conflicti1 – 66MLGFVG → MTSLWGKGTGCKLFKF in CAA27246. (PubMed:2870059)Curated
    Sequence conflicti36 – 405APTAV → VRRRF in AAA51808. (PubMed:2900241)Curated
    Sequence conflicti36 – 405APTAV → VRRRS in BAA00016. (PubMed:2870059)Curated
    Sequence conflicti36 – 405APTAV → VRRRS in CAA27246. (PubMed:2870059)Curated
    Sequence conflicti130 – 1323API → DQL in AAA51808. (PubMed:2900241)Curated
    Sequence conflicti378 – 3781H → D in AAA51808. (PubMed:2900241)Curated
    Sequence conflicti435 – 4351Q → H in AAA51808. (PubMed:2900241)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27132 Genomic DNA. Translation: AAA51809.1.
    M19483, M19482 Genomic DNA. Translation: AAA51808.1.
    X03559 mRNA. Translation: CAA27246.1.
    D00022 mRNA. Translation: BAA00016.1.
    AK291085 mRNA. Translation: BAF83774.1.
    CH471054 Genomic DNA. Translation: EAW96952.1.
    BC016512 mRNA. Translation: AAH16512.1.
    X05606 mRNA. Translation: CAA29095.1.
    CCDSiCCDS8924.1.
    PIRiA33370.
    RefSeqiNP_001677.2. NM_001686.3.
    UniGeneiHs.406510.

    Genome annotation databases

    EnsembliENST00000262030; ENSP00000262030; ENSG00000110955.
    GeneIDi506.
    KEGGihsa:506.
    UCSCiuc001slr.3. human.

    Polymorphism databases

    DMDMi114549.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27132 Genomic DNA. Translation: AAA51809.1 .
    M19483 , M19482 Genomic DNA. Translation: AAA51808.1 .
    X03559 mRNA. Translation: CAA27246.1 .
    D00022 mRNA. Translation: BAA00016.1 .
    AK291085 mRNA. Translation: BAF83774.1 .
    CH471054 Genomic DNA. Translation: EAW96952.1 .
    BC016512 mRNA. Translation: AAH16512.1 .
    X05606 mRNA. Translation: CAA29095.1 .
    CCDSi CCDS8924.1.
    PIRi A33370.
    RefSeqi NP_001677.2. NM_001686.3.
    UniGenei Hs.406510.

    3D structure databases

    ProteinModelPortali P06576.
    SMRi P06576. Positions 60-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106994. 83 interactions.
    IntActi P06576. 38 interactions.
    MINTi MINT-5004016.
    STRINGi 9606.ENSP00000262030.

    Chemistry

    ChEMBLi CHEMBL2062350.

    PTM databases

    PhosphoSitei P06576.

    Polymorphism databases

    DMDMi 114549.

    2D gel databases

    DOSAC-COBS-2DPAGE P06576.
    OGPi P06576.
    REPRODUCTION-2DPAGE IPI00303476.
    P06576.
    SWISS-2DPAGE P06576.
    UCD-2DPAGE P06576.

    Proteomic databases

    MaxQBi P06576.
    PaxDbi P06576.
    PRIDEi P06576.

    Protocols and materials databases

    DNASUi 506.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262030 ; ENSP00000262030 ; ENSG00000110955 .
    GeneIDi 506.
    KEGGi hsa:506.
    UCSCi uc001slr.3. human.

    Organism-specific databases

    CTDi 506.
    GeneCardsi GC12M057031.
    HGNCi HGNC:830. ATP5B.
    HPAi CAB017527.
    HPA001520.
    HPA001528.
    MIMi 102910. gene.
    neXtProti NX_P06576.
    PharmGKBi PA25122.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0055.
    HOGENOMi HOG000009605.
    HOVERGENi HBG004307.
    InParanoidi P06576.
    KOi K02133.
    OMAi VSEILVT.
    OrthoDBi EOG73V6K6.
    PhylomeDBi P06576.
    TreeFami TF105640.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    ChiTaRSi ATP5B. human.
    GeneWikii ATP5B.
    GenomeRNAii 506.
    NextBioi 2109.
    PROi P06576.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06576.
    Bgeei P06576.
    CleanExi HS_ATP5B.
    Genevestigatori P06576.

    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. "The human ATP synthase beta subunit gene: sequence analysis, chromosome assignment, and differential expression."
      Neckelmann N., Warner C.K., Chung A., Kudoh J., Minoshima S., Fukuyama R., Maekawa M., Shimizu Y., Shimizu N., Liu J.D., Wallace D.C.
      Genomics 5:829-843(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit."
      Ohta S., Tomura H., Matsuda K., Kagawa Y.
      J. Biol. Chem. 263:11257-11262(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-274.
    3. "Human F1-ATPase: molecular cloning of cDNA for the beta subunit."
      Ohta S., Kagawa Y.
      J. Biochem. 99:135-141(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-274.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Placenta.
    7. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 48-63.
      Tissue: Leukemic T-cell.
    8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 189-198; 202-239; 242-259; 265-279; 282-345; 388-422; 433-456 AND 490-519, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Sequence analysis of cDNAs for the human and bovine ATP synthase beta subunit: mitochondrial DNA genes sustain seventeen times more mutations."
      Wallace D.C., Ye J., Neckelmann S.N., Singh G., Webster K.A., Greenberg B.D.
      Curr. Genet. 12:81-90(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-529.
    10. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 95-109; 282-294 AND 311-324.
      Tissue: Adipocyte.
    11. Bienvenut W.V.
      Submitted (MAR-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 95-121; 125-155; 162-188; 202-239; 242-259; 265-279; 282-345; 407-422 AND 463-480, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-198 AND LYS-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATPB_HUMAN
    AccessioniPrimary (citable) accession number: P06576
    Secondary accession number(s): A8K4X0, Q14283
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 178 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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