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Q8N8Y2

- VA0D2_HUMAN

UniProt

Q8N8Y2 - VA0D2_HUMAN

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Protein

V-type proton ATPase subunit d 2

Gene
ATP6V0D2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Subunit of the integral membrane V0 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. May play a role in coupling of proton transport and ATP hydrolysis By similarity.

GO - Molecular functioni

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

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. insulin receptor signaling pathway Source: Reactome
  4. interaction with host Source: Reactome
  5. phagosome maturation Source: Reactome
  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:HS07458-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit d 2
Short name:
V-ATPase subunit d 2
Alternative name(s):
Vacuolar proton pump subunit d 2
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:18266. ATP6V0D2.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. early endosome Source: Ensembl
  3. endosome membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. membrane Source: UniProtKB
  6. phagocytic vesicle membrane Source: Reactome
  7. proton-transporting V-type ATPase, V0 domain Source: InterPro
  8. vacuolar proton-transporting V-type ATPase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38516.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350V-type proton ATPase subunit d 2PRO_0000285657Add
BLAST

Proteomic databases

MaxQBiQ8N8Y2.
PaxDbiQ8N8Y2.
PRIDEiQ8N8Y2.

PTM databases

PhosphoSiteiQ8N8Y2.

Expressioni

Tissue specificityi

Kidney, osteoclast and lung.1 Publication

Gene expression databases

ArrayExpressiQ8N8Y2.
BgeeiQ8N8Y2.
CleanExiHS_ATP6V0D2.
GenevestigatoriQ8N8Y2.

Organism-specific databases

HPAiHPA055327.
HPA058496.

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

BioGridi128858. 5 interactions.
IntActiQ8N8Y2. 4 interactions.
STRINGi9606.ENSP00000285393.

Structurei

3D structure databases

ProteinModelPortaliQ8N8Y2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1527.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ8N8Y2.
KOiK02146.
OMAiFFTYMTC.
PhylomeDBiQ8N8Y2.
TreeFamiTF300857.

Family and domain databases

InterProiIPR002843. ATPase_V0-cplx_csu/dsu.
IPR016727. ATPase_V0-cplx_dsu.
[Graphical view]
PANTHERiPTHR11028. PTHR11028. 1 hit.
PfamiPF01992. vATP-synt_AC39. 1 hit.
[Graphical view]
PIRSFiPIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAMiSSF103486. SSF103486. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8N8Y2-1 [UniParc]FASTAAdd to Basket

« Hide

MLEGAELYFN VDHGYLEGLV RGCKASLLTQ QDYINLVQCE TLEDLKIHLQ    50
TTDYGNFLAN HTNPLTVSKI DTEMRKRLCG EFEYFRNHSL EPLSTFLTYM 100
TCSYMIDNVI LLMNGALQKK SVKEILGKCH PLGRFTEMEA VNIAETPSDL 150
FNAILIETPL APFFQDCMSE NALDELNIEL LRNKLYKSYL EAFYKFCKNH 200
GDVTAEVMCP ILEFEADRRA FIITLNSFGT ELSKEDRETL YPTFGKLYPE 250
GLRLLAQAED FDQMKNVADH YGVYKPLFEA VGGSGGKTLE DVFYEREVQM 300
NVLAFNRQFH YGVFYAYVKL KEQEIRNIVW IAECISQRHR TKINSYIPIL 350
Length:350
Mass (Da):40,426
Last modified:October 1, 2002 - v1
Checksum:i07658C37F2A10CB7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721G → R.
Corresponds to variant rs10094744 [ dbSNP | Ensembl ].
VAR_032039
Natural varianti295 – 2951E → K.
Corresponds to variant rs4263741 [ dbSNP | Ensembl ].
VAR_032040

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY079172 mRNA. Translation: AAL87000.1.
AK096027 mRNA. Translation: BAC04679.1.
BC065207 mRNA. Translation: AAH65207.1.
CCDSiCCDS6241.1.
RefSeqiNP_689778.1. NM_152565.1.
UniGeneiHs.436360.

Genome annotation databases

EnsembliENST00000285393; ENSP00000285393; ENSG00000147614.
GeneIDi245972.
KEGGihsa:245972.
UCSCiuc003ydp.1. human.

Polymorphism databases

DMDMi74729555.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY079172 mRNA. Translation: AAL87000.1 .
AK096027 mRNA. Translation: BAC04679.1 .
BC065207 mRNA. Translation: AAH65207.1 .
CCDSi CCDS6241.1.
RefSeqi NP_689778.1. NM_152565.1.
UniGenei Hs.436360.

3D structure databases

ProteinModelPortali Q8N8Y2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128858. 5 interactions.
IntActi Q8N8Y2. 4 interactions.
STRINGi 9606.ENSP00000285393.

PTM databases

PhosphoSitei Q8N8Y2.

Polymorphism databases

DMDMi 74729555.

Proteomic databases

MaxQBi Q8N8Y2.
PaxDbi Q8N8Y2.
PRIDEi Q8N8Y2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285393 ; ENSP00000285393 ; ENSG00000147614 .
GeneIDi 245972.
KEGGi hsa:245972.
UCSCi uc003ydp.1. human.

Organism-specific databases

CTDi 245972.
GeneCardsi GC08P086999.
HGNCi HGNC:18266. ATP6V0D2.
HPAi HPA055327.
HPA058496.
neXtProti NX_Q8N8Y2.
PharmGKBi PA38516.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1527.
HOGENOMi HOG000199065.
HOVERGENi HBG018065.
InParanoidi Q8N8Y2.
KOi K02146.
OMAi FFTYMTC.
PhylomeDBi Q8N8Y2.
TreeFami TF300857.

Enzyme and pathway databases

BioCyci MetaCyc:HS07458-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

GenomeRNAii 245972.
NextBioi 91831.
PROi Q8N8Y2.

Gene expression databases

ArrayExpressi Q8N8Y2.
Bgeei Q8N8Y2.
CleanExi HS_ATP6V0D2.
Genevestigatori Q8N8Y2.

Family and domain databases

InterProi IPR002843. ATPase_V0-cplx_csu/dsu.
IPR016727. ATPase_V0-cplx_dsu.
[Graphical view ]
PANTHERi PTHR11028. PTHR11028. 1 hit.
Pfami PF01992. vATP-synt_AC39. 1 hit.
[Graphical view ]
PIRSFi PIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAMi SSF103486. SSF103486. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "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: Kidney.
  3. "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: Colon.

Entry informationi

Entry nameiVA0D2_HUMAN
AccessioniPrimary (citable) accession number: Q8N8Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 92 of the entry and version 1 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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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