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Q9Y487

- VPP2_HUMAN

UniProt

Q9Y487 - VPP2_HUMAN

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Protein
V-type proton ATPase 116 kDa subunit a isoform 2
Gene
ATP6V0A2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH.2 Publications

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro
  2. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. immune response Source: ProtInc
  4. insulin receptor signaling pathway Source: Reactome
  5. interaction with host Source: Reactome
  6. phagosome maturation Source: Reactome
  7. transferrin transport Source: Reactome
  8. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:G66-33375-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 116 kDa subunit a isoform 2
Short name:
V-ATPase 116 kDa isoform a2
Alternative name(s):
Lysosomal H(+)-transporting ATPase V0 subunit a2
TJ6
Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:18481. ATP6V0A2.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Endosome membrane
Note: In kidney proximal tubules, also detected in subapical vesicles By similarity.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 393393Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei394 – 41219Helical; Reviewed prediction
Add
BLAST
Topological domaini413 – 4142Vacuolar Reviewed prediction
Transmembranei415 – 43117Helical; Reviewed prediction
Add
BLAST
Topological domaini432 – 44514Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei446 – 47530Helical; Reviewed prediction
Add
BLAST
Topological domaini476 – 54974Vacuolar Reviewed prediction
Add
BLAST
Transmembranei550 – 56920Helical; Reviewed prediction
Add
BLAST
Topological domaini570 – 58718Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei588 – 60821Helical; Reviewed prediction
Add
BLAST
Topological domaini609 – 65143Vacuolar Reviewed prediction
Add
BLAST
Transmembranei652 – 67120Helical; Reviewed prediction
Add
BLAST
Topological domaini672 – 73968Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei740 – 76425Helical; Reviewed prediction
Add
BLAST
Topological domaini765 – 78521Vacuolar Reviewed prediction
Add
BLAST
Transmembranei786 – 82439Helical; Reviewed prediction
Add
BLAST
Topological domaini825 – 85632Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. cytoplasm Source: HPA
  3. endosome membrane Source: Reactome
  4. integral component of membrane Source: UniProtKB-KW
  5. lysosomal membrane Source: UniProtKB
  6. phagocytic vesicle membrane Source: Reactome
  7. plasma membrane Source: HPA
  8. vacuolar proton-transporting V-type ATPase, V0 domain Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Cutis laxa, autosomal recessive, 2A (ARCL2A) [MIM:219200]: A disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, a general connective tissue weakness, and varying degrees of growth and developmental delay and neurological abnormalities. Some affected individuals develop seizures and mental deterioration later in life, whereas the skin phenotype tends to become milder with age. At the molecular level, an abnormal glycosylation of serum proteins is observed in many cases.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Wrinkly skin syndrome (WSS) [MIM:278250]: A rare autosomal recessive disorder characterized by wrinkling of the skin of the dorsum of the hands and feet, an increased number of palmar and plantar creases, wrinkled abdominal skin, multiple musculoskeletal abnormalities, microcephaly, growth failure and developmental delay.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

MIMi219200. phenotype.
278250. phenotype.
Orphaneti357074. Autosomal recessive cutis laxa type 2, classic type.
2834. Wrinkly skin syndrome.
PharmGKBiPA38549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 856856V-type proton ATPase 116 kDa subunit a isoform 2
PRO_0000119216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei700 – 7001Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y487.
PaxDbiQ9Y487.
PRIDEiQ9Y487.

PTM databases

PhosphoSiteiQ9Y487.

Expressioni

Gene expression databases

ArrayExpressiQ9Y487.
BgeeiQ9Y487.
CleanExiHS_ATP6V0A2.
GenevestigatoriQ9Y487.

Organism-specific databases

HPAiHPA044279.

Interactioni

Subunit structurei

The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''. Directly interacts with PSCD2 through its N-terminal cytosolic tail in an intra-endosomal acidification-dependent manner. Disruption of this interaction results in the inhibition of endocytosis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CYTH2Q994182EBI-988630,EBI-448974

Protein-protein interaction databases

BioGridi117089. 9 interactions.
IntActiQ9Y487. 2 interactions.
STRINGi9606.ENSP00000332247.

Structurei

3D structure databases

ProteinModelPortaliQ9Y487.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1269.
HOGENOMiHOG000037059.
HOVERGENiHBG014606.
InParanoidiQ9Y487.
KOiK02154.
OMAiEIMRMFF.
OrthoDBiEOG74FF04.
PhylomeDBiQ9Y487.
TreeFamiTF300346.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y487-1 [UniParc]FASTAAdd to Basket

« Hide

MGSLFRSETM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK    50
FVGEVKRCEE LERILVYLVQ EINRADIPLP EGEASPPAPP LKQVLEMQEQ 100
LQKLEVELRE VTKNKEKLRK NLLELIEYTH MLRVTKTFVK RNVEFEPTYE 150
EFPSLESDSL LDYSCMQRLG AKLGFVSGLI NQGKVEAFEK MLWRVCKGYT 200
IVSYAELDES LEDPETGEVI KWYVFLISFW GEQIGHKVKK ICDCYHCHVY 250
PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVYSRVI 300
QVKKMKAIYH MLNMCSFDVT NKCLIAEVWC PEADLQDLRR ALEEGSRESG 350
ATIPSFMNII PTKETPPTRI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT 400
IITFPFLFAV MFGDFGHGFV MFLFALLLVL NENHPRLNQS QEIMRMFFNG 450
RYILLLMGLF SVYTGLIYND CFSKSVNLFG SGWNVSAMYS SSHPPAEHKK 500
MVLWNDSVVR HNSILQLDPS IPGVFRGPYP LGIDPIWNLA TNRLTFLNSF 550
KMKMSVILGI IHMTFGVILG IFNHLHFRKK FNIYLVSIPE LLFMLCIFGY 600
LIFMIFYKWL VFSAETSRVA PSILIEFINM FLFPASKTSG LYTGQEYVQR 650
VLLVVTALSV PVLFLGKPLF LLWLHNGRSC FGVNRSGYTL IRKDSEEEVS 700
LLGSQDIEEG NHQVEDGCRE MACEEFNFGE ILMTQVIHSI EYCLGCISNT 750
ASYLRLWALS LAHAQLSDVL WAMLMRVGLR VDTTYGVLLL LPVIALFAVL 800
TIFILLIMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF SFSLLSSKFN 850
NDDSVA 856
Length:856
Mass (Da):98,082
Last modified:March 18, 2008 - v2
Checksum:i6C38B36FA33A92BA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti685 – 6851R → Q.
Corresponds to variant rs7969410 [ dbSNP | Ensembl ].
VAR_042730
Natural varianti813 – 8131A → V.
Corresponds to variant rs17883456 [ dbSNP | Ensembl ].
VAR_042731

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti428 – 4281L → W in AAD04632. 1 Publication
Sequence conflicti669 – 6691L → P in BAF82080. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF112972 mRNA. Translation: AAD04632.1.
AK289391 mRNA. Translation: BAF82080.1.
CH471054 Genomic DNA. Translation: EAW98434.1.
BC068531 mRNA. Translation: AAH68531.1.
CCDSiCCDS9254.1.
RefSeqiNP_036595.2. NM_012463.3.
UniGeneiHs.25786.

Genome annotation databases

EnsembliENST00000330342; ENSP00000332247; ENSG00000185344.
GeneIDi23545.
KEGGihsa:23545.
UCSCiuc001ufr.3. human.

Polymorphism databases

DMDMi172046607.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF112972 mRNA. Translation: AAD04632.1 .
AK289391 mRNA. Translation: BAF82080.1 .
CH471054 Genomic DNA. Translation: EAW98434.1 .
BC068531 mRNA. Translation: AAH68531.1 .
CCDSi CCDS9254.1.
RefSeqi NP_036595.2. NM_012463.3.
UniGenei Hs.25786.

3D structure databases

ProteinModelPortali Q9Y487.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117089. 9 interactions.
IntActi Q9Y487. 2 interactions.
STRINGi 9606.ENSP00000332247.

PTM databases

PhosphoSitei Q9Y487.

Polymorphism databases

DMDMi 172046607.

Proteomic databases

MaxQBi Q9Y487.
PaxDbi Q9Y487.
PRIDEi Q9Y487.

Protocols and materials databases

DNASUi 23545.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330342 ; ENSP00000332247 ; ENSG00000185344 .
GeneIDi 23545.
KEGGi hsa:23545.
UCSCi uc001ufr.3. human.

Organism-specific databases

CTDi 23545.
GeneCardsi GC12P124196.
GeneReviewsi ATP6V0A2.
H-InvDB HIX0011113.
HGNCi HGNC:18481. ATP6V0A2.
HPAi HPA044279.
MIMi 219200. phenotype.
278250. phenotype.
611716. gene.
neXtProti NX_Q9Y487.
Orphaneti 357074. Autosomal recessive cutis laxa type 2, classic type.
2834. Wrinkly skin syndrome.
PharmGKBi PA38549.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1269.
HOGENOMi HOG000037059.
HOVERGENi HBG014606.
InParanoidi Q9Y487.
KOi K02154.
OMAi EIMRMFF.
OrthoDBi EOG74FF04.
PhylomeDBi Q9Y487.
TreeFami TF300346.

Enzyme and pathway databases

BioCyci MetaCyc:G66-33375-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSi ATP6V0A2. human.
GeneWikii ATP6V0A2.
GenomeRNAii 23545.
NextBioi 46076.
PROi Q9Y487.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y487.
Bgeei Q9Y487.
CleanExi HS_ATP6V0A2.
Genevestigatori Q9Y487.

Family and domain databases

InterProi IPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view ]
PANTHERi PTHR11629. PTHR11629. 1 hit.
Pfami PF01496. V_ATPase_I. 1 hit.
[Graphical view ]
PIRSFi PIRSF001293. ATP6V0A1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human TJ6 homolog."
    Babichev Y., Isakov N.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Astrocyte.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway."
    Hurtado-Lorenzo A., Skinner M., El Annan J., Futai M., Sun-Wada G.-H., Bourgoin S., Casanova J., Wildeman A., Bechoua S., Ausiello D.A., Brown D., Marshansky V.
    Nat. Cell Biol. 8:124-136(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PSCD2.
  6. "The N-terminal domain of the a2 isoform of vacuolar ATPase can regulate interleukin-1beta production from mononuclear cells in co-culture with JEG-3 choriocarcinoma cells."
    Ntrivalas E., Gilman-Sachs A., Kwak-Kim J., Beaman K.
    Am. J. Reprod. Immunol. 57:201-209(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: INVOLVEMENT IN ARCL2A, INVOLVEMENT IN WSS, FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVPP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y487
Secondary accession number(s): A8K026, Q6NUM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 18, 2008
Last modified: September 3, 2014
This is version 125 of the entry and version 2 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

Caution

The N-terminal peptide may increase IL1B secretion by peripheral blood monocytes; however as this region is probably in the cytosol, the in vivo relevance of this observation needs to be confirmed.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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