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O75348

- VATG1_HUMAN

UniProt

O75348 - VATG1_HUMAN

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Protein

V-type proton ATPase subunit G 1

Gene
ATP6V1G1, ATP6G, ATP6G1, ATP6J
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
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
Complete GO annotation...

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.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 132 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

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