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O75964

- ATP5L_HUMAN

UniProt

O75964 - ATP5L_HUMAN

Protein

ATP synthase subunit g, mitochondrial

Gene

ATP5L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane.

    GO - Molecular functioni

    1. hydrogen ion transmembrane transporter activity Source: InterPro
    2. transmembrane transporter activity Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular metabolic process Source: Reactome
    3. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
    4. respiratory electron transport chain Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    ATP synthesis, Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_6759. Formation of ATP by chemiosmotic coupling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP synthase subunit g, mitochondrial
    Short name:
    ATPase subunit g
    Gene namesi
    Name:ATP5L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14247. ATP5L.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
    4. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
    5. mitochondrion Source: LIFEdb

    Keywords - Cellular componenti

    CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25143.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 103102ATP synthase subunit g, mitochondrialPRO_0000071691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei11 – 111N6-acetyllysineBy similarity
    Modified residuei24 – 241N6-acetyllysine1 Publication
    Modified residuei35 – 351N6-acetyllysineBy similarity
    Modified residuei54 – 541N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO75964.
    PaxDbiO75964.
    PeptideAtlasiO75964.
    PRIDEiO75964.

    PTM databases

    PhosphoSiteiO75964.

    Expressioni

    Gene expression databases

    ArrayExpressiO75964.
    BgeeiO75964.
    CleanExiHS_ATP5L.
    GenevestigatoriO75964.

    Organism-specific databases

    HPAiHPA044629.

    Interactioni

    Subunit structurei

    F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115876. 10 interactions.
    IntActiO75964. 6 interactions.
    MINTiMINT-3002124.
    STRINGi9606.ENSP00000300688.

    Structurei

    3D structure databases

    ProteinModelPortaliO75964.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATPase g subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG323765.
    HOGENOMiHOG000007506.
    HOVERGENiHBG050614.
    InParanoidiO75964.
    KOiK02140.
    OMAiFVGECIG.
    PhylomeDBiO75964.
    TreeFamiTF313978.

    Family and domain databases

    InterProiIPR016702. ATP-Synthase_su_G_mt_met.
    IPR006808. ATPase_F0-cplx_gsu_mt.
    [Graphical view]
    PfamiPF04718. ATP-synt_G. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017835. ATP-synth_g_mitoch_animal. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O75964-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQFVRNLVE KTPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPRAI    50
    QSLKKIVNSA QTGSFKQLTV KEAVLNGLVA TEVLMWFYVG EIIGKRGIIG 100
    YDV 103
    Length:103
    Mass (Da):11,428
    Last modified:April 26, 2005 - v3
    Checksum:i03D484BCF836E6C2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → G in AAC61597. 1 PublicationCurated
    Sequence conflicti48 – 481R → K in AAC61597. 1 PublicationCurated
    Sequence conflicti57 – 571V → A in AAH15128. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092124 mRNA. Translation: AAC61597.1.
    AF087846 mRNA. Translation: AAP97159.1.
    AF070655 mRNA. Translation: AAD20961.1.
    AL050277 mRNA. Translation: CAB43378.1.
    CR533494 mRNA. Translation: CAG38525.1.
    CR542211 mRNA. Translation: CAG47007.1.
    AK289568 mRNA. Translation: BAF82257.1.
    CH471065 Genomic DNA. Translation: EAW67376.1.
    BC015128 mRNA. Translation: AAH15128.1.
    BC070165 mRNA. Translation: AAH70165.1.
    CCDSiCCDS8397.1.
    PIRiT08727.
    RefSeqiNP_006467.4. NM_006476.4.
    UniGeneiHs.486360.

    Genome annotation databases

    EnsembliENST00000300688; ENSP00000300688; ENSG00000167283.
    GeneIDi10632.
    KEGGihsa:10632.
    UCSCiuc001psx.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092124 mRNA. Translation: AAC61597.1 .
    AF087846 mRNA. Translation: AAP97159.1 .
    AF070655 mRNA. Translation: AAD20961.1 .
    AL050277 mRNA. Translation: CAB43378.1 .
    CR533494 mRNA. Translation: CAG38525.1 .
    CR542211 mRNA. Translation: CAG47007.1 .
    AK289568 mRNA. Translation: BAF82257.1 .
    CH471065 Genomic DNA. Translation: EAW67376.1 .
    BC015128 mRNA. Translation: AAH15128.1 .
    BC070165 mRNA. Translation: AAH70165.1 .
    CCDSi CCDS8397.1.
    PIRi T08727.
    RefSeqi NP_006467.4. NM_006476.4.
    UniGenei Hs.486360.

    3D structure databases

    ProteinModelPortali O75964.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115876. 10 interactions.
    IntActi O75964. 6 interactions.
    MINTi MINT-3002124.
    STRINGi 9606.ENSP00000300688.

    PTM databases

    PhosphoSitei O75964.

    Proteomic databases

    MaxQBi O75964.
    PaxDbi O75964.
    PeptideAtlasi O75964.
    PRIDEi O75964.

    Protocols and materials databases

    DNASUi 10632.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300688 ; ENSP00000300688 ; ENSG00000167283 .
    GeneIDi 10632.
    KEGGi hsa:10632.
    UCSCi uc001psx.3. human.

    Organism-specific databases

    CTDi 10632.
    GeneCardsi GC11P118271.
    HGNCi HGNC:14247. ATP5L.
    HPAi HPA044629.
    neXtProti NX_O75964.
    PharmGKBi PA25143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323765.
    HOGENOMi HOG000007506.
    HOVERGENi HBG050614.
    InParanoidi O75964.
    KOi K02140.
    OMAi FVGECIG.
    PhylomeDBi O75964.
    TreeFami TF313978.

    Enzyme and pathway databases

    Reactomei REACT_6759. Formation of ATP by chemiosmotic coupling.

    Miscellaneous databases

    GeneWikii ATP5L.
    GenomeRNAii 10632.
    NextBioi 40403.
    PROi O75964.

    Gene expression databases

    ArrayExpressi O75964.
    Bgeei O75964.
    CleanExi HS_ATP5L.
    Genevestigatori O75964.

    Family and domain databases

    InterProi IPR016702. ATP-Synthase_su_G_mt_met.
    IPR006808. ATPase_F0-cplx_gsu_mt.
    [Graphical view ]
    Pfami PF04718. ATP-synt_G. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017835. ATP-synth_g_mitoch_animal. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal assignment of F1F0-type ATP synthase subunit g from human infant thymus."
      Kang Y.J., Hwang M.Y., Lee M.Y., Lee H.C., Sohn U.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thymus.
    2. "Cloning and characterization of a novel human cDNA homologous to Bos taurus F1Fo-ATP synthase complex Fo membrane domain g subunit mRNA."
      Zhang M., Yu L., Zhou Y., Hu P.R., Xin Y.R., Zhao S.Y.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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].
      Tissue: Cerebellum.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "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-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATP5L_HUMAN
    AccessioniPrimary (citable) accession number: O75964
    Secondary accession number(s): A8K0K3, Q96BV6, Q9UBZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 126 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3