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O75348 (VATG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATP6V1G1
Synonyms:ATP6G, ATP6G1, ATP6J
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

V-ATPase is an 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).

Tissue specificity

Ubiquitous. Ref.4

Sequence similarities

Belongs to the V-ATPase G subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 118117V-type proton ATPase subunit G 1
PRO_0000192897

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.5

Sequences

Sequence LengthMass (Da)Tools
O75348 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A289C1B96634E34C

FASTA11813,758
        10         20         30         40         50         60 
MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEIEQYRLQ REKEFKAKEA 

        70         80         90        100        110 
AALGSRGSCS TEVEKETQEK MTILQTYFRQ NRDEVLDNLL AFVCDIRPEI HENYRING 

« Hide

References

« Hide 'large scale' references
[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: 9653160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[3]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, MASS SPECTROMETRY.
Tissue: Melanoma.
[4]"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: 12384298] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF038954 mRNA. Translation: AAC39868.1.
BC008452 mRNA. Translation: AAH08452.1.
IPIIPI00025285.
RefSeqNP_004879.1. NM_004888.3.
UniGeneHs.388654.

3D structure databases

ProteinModelPortalO75348.
SMRO75348. Positions 1-59.
ModBaseSearch...

Protein-protein interaction databases

IntActO75348. 4 interactions.
MINTMINT-1377978.
STRINGO75348.

Protein family/group databases

TCDB3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Proteomic databases

PeptideAtlasO75348.
PRIDEO75348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374050; ENSP00000363162; ENSG00000136888.
GeneID9550.
KEGGhsa:9550.
UCSCuc004bjc.1. human.

Organism-specific databases

CTD9550.
GeneCardsGC09P117350.
H-InvDBHIX0008322.
HGNCHGNC:864. ATP6V1G1.
HPACAB004615.
MIM607296. gene.
neXtProtNX_O75348.
PharmGKBPA25163.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG21247.
HOGENOMHBG621942.
HOVERGENHBG057827.
InParanoidO75348.
OMAHGNSAVE.
OrthoDBEOG483D67.
PhylomeDBO75348.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressO75348.
BgeeO75348.
CleanExHS_ATP6V1G1.
GenevestigatorO75348.
GermOnlineENSG00000136888. Homo sapiens.

Family and domain databases

InterProIPR005124. V-ATPase_G.
[Graphical view]
KOK02152.
PANTHERPTHR12713. V-ATPase_G. 1 hit.
PfamPF03179. V-ATPase_G. 1 hit.
[Graphical view]
TIGRFAMsTIGR01147. V_ATP_synt_G. 1 hit.
ProtoNetSearch...

Other

NextBio35807.
SOURCESearch...

Entry information

Entry nameVATG1_HUMAN
AccessionPrimary (citable) accession number: O75348
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families