Q9UI12 · VATH_HUMAN
- ProteinV-type proton ATPase subunit H
- GeneATP6V1H
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids483 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity).
Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (PubMed:12032142).
V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity).
Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (PubMed:12032142).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | clathrin-coated vesicle membrane | |
Cellular Component | cytosol | |
Cellular Component | endosome membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | extrinsic component of synaptic vesicle membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | lysosomal membrane | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | proton-transporting V-type ATPase complex | |
Cellular Component | vacuolar proton-transporting V-type ATPase, V1 domain | |
Molecular Function | enzyme regulator activity | |
Molecular Function | proton-transporting ATPase activity, rotational mechanism | |
Biological Process | endocytosis | |
Biological Process | endosomal lumen acidification | |
Biological Process | Golgi lumen acidification | |
Biological Process | intracellular pH reduction | |
Biological Process | lysosomal lumen acidification | |
Biological Process | proton transmembrane transport | |
Biological Process | regulation of macroautophagy | |
Biological Process | synaptic vesicle lumen acidification | |
Biological Process | vacuolar acidification |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameV-type proton ATPase subunit H
- Short namesV-ATPase subunit H
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UI12
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle, clathrin-coated vesicle membrane ; Peripheral membrane protein
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 577 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000124193 | 1-483 | UniProt | V-type proton ATPase subunit H | |||
Sequence: MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRSPEEKQEMLQTEGSQCAKTFINLMTHICKEQTVQYILTMVDDMLQENHQRVSIFFDYARCSKNTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTVSSSDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 483 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
V-ATPase is a heteromultimeric enzyme made up of two complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex (PubMed:33065002).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (PubMed:33065002).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002).
Interacts with AP2M1 (PubMed:12032142).
Interacts with TM9SF4 in colon cancer cells (PubMed:25659576).
The V1 complex consists of three catalytic AB heterodimers that form a heterohexamer, three peripheral stalks each consisting of EG heterodimers, one central rotor including subunits D and F, and the regulatory subunits C and H (PubMed:33065002).
The proton translocation complex V0 consists of the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002).
Interacts with AP2M1 (PubMed:12032142).
Interacts with TM9SF4 in colon cancer cells (PubMed:25659576).
(Microbial infection) Interacts with HIV-1 Nef protein.
(Microbial infection) Interacts with M.tuberculosis PtpA, which blocks V-ATPase trafficking and phagosome acidification.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UI12 | BOD1 Q96IK1-2 | 3 | EBI-724719, EBI-18924329 | |
BINARY | Q9UI12 | CDKN2B P42772 | 3 | EBI-724719, EBI-711280 | |
BINARY | Q9UI12 | FLACC1 Q96Q35-2 | 3 | EBI-724719, EBI-11533409 | |
BINARY | Q9UI12 | HTT P42858 | 3 | EBI-724719, EBI-466029 | |
BINARY | Q9UI12 | PPP1R12C Q9BZL4 | 3 | EBI-724719, EBI-721802 | |
BINARY | Q9UI12 | SNPH O15079 | 3 | EBI-724719, EBI-4401902 | |
BINARY | Q9UI12 | SPATA2 Q9UM82 | 3 | EBI-724719, EBI-744066 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9UI12-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length483
- Mass (Da)55,883
- Last updated2000-05-01 v1
- ChecksumEAE0457C538AC906
Q9UI12-2
- Name2
- Differences from canonical
- 176-193: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 129 | in Ref. 4; AAD27720 | ||||
Sequence: M → I | ||||||
Alternative sequence | VSP_012274 | 176-193 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF113222 EMBL· GenBank· DDBJ | AAG39293.1 EMBL· GenBank· DDBJ | mRNA | ||
AF298777 EMBL· GenBank· DDBJ | AAG22809.1 EMBL· GenBank· DDBJ | mRNA | ||
AF112204 EMBL· GenBank· DDBJ | AAF17192.1 EMBL· GenBank· DDBJ | mRNA | ||
AF132945 EMBL· GenBank· DDBJ | AAD27720.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022345 EMBL· GenBank· DDBJ | BAG51072.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471068 EMBL· GenBank· DDBJ | EAW86727.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC025275 EMBL· GenBank· DDBJ | AAH25275.1 EMBL· GenBank· DDBJ | mRNA |