Reviewed,
UniProtKB/Swiss-Prot Q9Y5K8 (VATD_HUMAN)
Last modified
November 24, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: V-type proton ATPase subunit D Short name=V-ATPase subunit D Alternative name(s): Vacuolar proton pump subunit D V-ATPase 28 kDa accessory protein | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 247 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system By similarity. |
| 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). |
| Sequence similarities | Belongs to the V-ATPase D subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen ion transport Ion transport Transport |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | proton-transporting two-sector ATPase complex, catalytic domain Inferred from electronic annotation. Source: InterPro vacuolar proton-transporting V-type ATPase complexInferred from direct assay. Source: UniProtKB |
| Molecular function | protein binding Inferred from physical interaction. Source: UniProtKB proton-transporting ATPase activity, rotational mechanismInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Zhao Y., Cao H.Q., Wei Y.J., Jiang Y.X., Zhao X.W., Liu D.Q., Meng X.M., Liu Y.Q., Xu Y.Y., Sheng H., Liu S., Qiao M., Hui R.T., Ding J.F. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart. |
| [2] | "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary. |
| [3] | "cDNA of human vacuolar H-ATPase subunit D (VATD) interacts with Rb." Quan L., Hong W., Shizhou A. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [4] | "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: Placenta. |
| [5] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| AF145316 mRNA. Translation: AAD33953.1. AF100741 mRNA. Translation: AAD40384.1. AF104629 mRNA. Translation: AAG30726.1. BC001411 mRNA. Translation: AAH01411.1. | |
| IPI | IPI00001568. |
| RefSeq | NP_057078.1. |
| UniGene | Hs.272630 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9Y5K8. |
PTM databases | |
| PhosphoSite | Q9Y5K8. |
Proteomic databases | |
| PeptideAtlas | Q9Y5K8. |
| PRIDE | Q9Y5K8. |
Genome annotation databases | |
| Ensembl | ENST00000216442; ENSP00000216442; ENSG00000100554; Homo sapiens. [Genome view] |
| GeneID | 51382. |
| KEGG | hsa:51382. |
| UCSC | uc001xjf.1. human. |
Organism-specific databases | |
| CTD | 51382. |
| GeneCards | GC14M066874. |
| HGNC | HGNC:13527. ATP6V1D. |
| MIM | 609398. gene. |
| PharmGKB | PA25157. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q9Y5K8. |
| HOVERGEN | Q9Y5K8. |
| OMA | FYRLKKV |
Enzyme and pathway databases | |
| BRENDA | 3.6.3.14. 247. |
Gene expression databases | |
| ArrayExpress | Q9Y5K8. |
| Bgee | Q9Y5K8. |
| CleanEx | HS_ATP6V1D. |
| Genevestigator | Q9Y5K8. |
Family and domain databases | |
| InterPro | IPR002699. ATPase_V1/A1-cplx_dsu. [Graphical view] |
| PANTHER | PTHR11671. ATPase_V1/A1_D. 1 hit. |
| Pfam | PF01813. ATP-synt_D. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00309. V_ATPase_subD. 1 hit. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 54891. |
| SOURCE | Search... |
Entry information
| Entry name | VATD_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9Y5K8 Secondary accession number(s): Q9Y688 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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 14 Human chromosome 14: 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 |

Clusters with


