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O75348

- VATG1_HUMAN

UniProt

O75348 - VATG1_HUMAN

Protein

V-type proton ATPase subunit G 1

Gene

ATP6V1G1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

    GO - Molecular functioni

    1. ATPase binding Source: UniProtKB
    2. hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances Source: InterPro

    GO - Biological processi

    1. cellular iron ion homeostasis Source: Reactome
    2. insulin receptor signaling pathway Source: Reactome
    3. interaction with host Source: Reactome
    4. phagosome maturation Source: Reactome
    5. proton transport Source: UniProtKB-KW
    6. transferrin transport Source: Reactome
    7. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Hydrogen ion transport, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06241-MONOMER.
    ReactomeiREACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Protein family/group databases

    TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    V-type proton ATPase subunit G 1
    Short name:
    V-ATPase subunit G 1
    Alternative name(s):
    V-ATPase 13 kDa subunit 1
    Vacuolar proton pump subunit G 1
    Vacuolar proton pump subunit M16
    Gene namesi
    Name:ATP6V1G1
    Synonyms:ATP6G, ATP6G1, ATP6J
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:864. ATP6V1G1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. lysosomal membrane Source: UniProtKB
    4. plasma membrane Source: UniProtKB
    5. vacuolar proton-transporting V-type ATPase complex Source: InterPro

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25163.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 118117V-type proton ATPase subunit G 1PRO_0000192897Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO75348.
    PaxDbiO75348.
    PeptideAtlasiO75348.
    PRIDEiO75348.

    PTM databases

    PhosphoSiteiO75348.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiO75348.
    CleanExiHS_ATP6V1G1.
    GenevestigatoriO75348.

    Organism-specific databases

    HPAiCAB004615.

    Interactioni

    Subunit structurei

    V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d).

    Protein-protein interaction databases

    BioGridi114922. 8 interactions.
    IntActiO75348. 5 interactions.
    MINTiMINT-5001706.
    STRINGi9606.ENSP00000363162.

    Structurei

    3D structure databases

    ProteinModelPortaliO75348.
    SMRiO75348. Positions 3-81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the V-ATPase G subunit family.Curated

    Phylogenomic databases

    eggNOGiNOG272364.
    HOGENOMiHOG000186416.
    HOVERGENiHBG057827.
    InParanoidiO75348.
    KOiK02152.
    OMAiKFEAEHT.
    OrthoDBiEOG7MWH0X.
    PhylomeDBiO75348.
    TreeFamiTF313777.

    Family and domain databases

    InterProiIPR005124. V-ATPase_G.
    [Graphical view]
    PANTHERiPTHR12713. PTHR12713. 1 hit.
    TIGRFAMsiTIGR01147. V_ATP_synt_G. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O75348-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEIEQYRLQ    50
    REKEFKAKEA AALGSRGSCS TEVEKETQEK MTILQTYFRQ NRDEVLDNLL 100
    AFVCDIRPEI HENYRING 118
    Length:118
    Mass (Da):13,758
    Last modified:January 23, 2007 - v3
    Checksum:iA289C1B96634E34C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038954 mRNA. Translation: AAC39868.1.
    CR456971 mRNA. Translation: CAG33252.1.
    CR542237 mRNA. Translation: CAG47033.1.
    AL160275 Genomic DNA. Translation: CAH73481.1.
    CH471090 Genomic DNA. Translation: EAW87424.1.
    BC008452 mRNA. Translation: AAH08452.1.
    CCDSiCCDS6807.1.
    RefSeqiNP_004879.1. NM_004888.3.
    UniGeneiHs.388654.

    Genome annotation databases

    EnsembliENST00000374050; ENSP00000363162; ENSG00000136888.
    GeneIDi9550.
    KEGGihsa:9550.
    UCSCiuc004bjc.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF038954 mRNA. Translation: AAC39868.1 .
    CR456971 mRNA. Translation: CAG33252.1 .
    CR542237 mRNA. Translation: CAG47033.1 .
    AL160275 Genomic DNA. Translation: CAH73481.1 .
    CH471090 Genomic DNA. Translation: EAW87424.1 .
    BC008452 mRNA. Translation: AAH08452.1 .
    CCDSi CCDS6807.1.
    RefSeqi NP_004879.1. NM_004888.3.
    UniGenei Hs.388654.

    3D structure databases

    ProteinModelPortali O75348.
    SMRi O75348. Positions 3-81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114922. 8 interactions.
    IntActi O75348. 5 interactions.
    MINTi MINT-5001706.
    STRINGi 9606.ENSP00000363162.

    Protein family/group databases

    TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    PTM databases

    PhosphoSitei O75348.

    Proteomic databases

    MaxQBi O75348.
    PaxDbi O75348.
    PeptideAtlasi O75348.
    PRIDEi O75348.

    Protocols and materials databases

    DNASUi 9550.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374050 ; ENSP00000363162 ; ENSG00000136888 .
    GeneIDi 9550.
    KEGGi hsa:9550.
    UCSCi uc004bjc.3. human.

    Organism-specific databases

    CTDi 9550.
    GeneCardsi GC09P117350.
    HGNCi HGNC:864. ATP6V1G1.
    HPAi CAB004615.
    MIMi 607296. gene.
    neXtProti NX_O75348.
    PharmGKBi PA25163.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272364.
    HOGENOMi HOG000186416.
    HOVERGENi HBG057827.
    InParanoidi O75348.
    KOi K02152.
    OMAi KFEAEHT.
    OrthoDBi EOG7MWH0X.
    PhylomeDBi O75348.
    TreeFami TF313777.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06241-MONOMER.
    Reactomei REACT_1109. Insulin receptor recycling.
    REACT_121256. Phagosomal maturation (early endosomal stage).
    REACT_25283. Transferrin endocytosis and recycling.

    Miscellaneous databases

    ChiTaRSi ATP6V1G1. human.
    GeneWikii ATP6V1G1.
    GenomeRNAii 9550.
    NextBioi 35807.
    PROi O75348.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75348.
    CleanExi HS_ATP6V1G1.
    Genevestigatori O75348.

    Family and domain databases

    InterProi IPR005124. V-ATPase_G.
    [Graphical view ]
    PANTHERi PTHR12713. PTHR12713. 1 hit.
    TIGRFAMsi TIGR01147. V_ATP_synt_G. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Skeletal muscle.
    6. Kanor S., Bienvenut W.V., Quadroni M.
      Submitted (DEC-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-16; 38-48 AND 81-89, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Melanoma.
    7. "Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis."
      Smith A.N., Borthwick K.J., Karet F.E.
      Gene 297:169-177(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVATG1_HUMAN
    AccessioniPrimary (citable) accession number: O75348
    Secondary accession number(s): Q6IB33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3