Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UI12 (VATH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase subunit H

Short name=V-ATPase subunit H
Alternative name(s):
Nef-binding protein 1
Short name=NBP1
Protein VMA13 homolog
V-ATPase 50/57 kDa subunits
Vacuolar proton pump subunit H
Vacuolar proton pump subunit SFD
Gene names
Name:ATP6V1H
ORF Names:CGI-11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. 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. Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes.

Subunit structure

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). Interacts with HIV-1 Nef protein and AP2M1. Ref.2 Ref.8

Tissue specificity

Widely expressed. Ref.2

Sequence similarities

Belongs to the V-ATPase H subunit family.

Ontologies

Keywords
   Biological processHost-virus interaction
Hydrogen ion transport
Ion transport
Transport
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Non-traceable author statement PubMed 9442887. Source: GOC

ATP hydrolysis coupled proton transport

Non-traceable author statement PubMed 9442887. Source: UniProtKB

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

endocytosis

Inferred from direct assay Ref.8. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interaction with host

Traceable author statement. Source: Reactome

phagosome maturation

Traceable author statement. Source: Reactome

regulation of catalytic activity

Non-traceable author statement PubMed 9442887. Source: GOC

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

vacuolar acidification

Non-traceable author statement PubMed 9442887. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

vacuolar proton-transporting V-type ATPase, V1 domain

Non-traceable author statement PubMed 9442887. Source: UniProtKB

   Molecular_functionenzyme regulator activity

Non-traceable author statement PubMed 9442887. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11179428Ref.8Ref.2. Source: UniProtKB

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: 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.
Isoform 2 (identifier: Q9UI12-2)

The sequence of this isoform differs from the canonical sequence as follows:
     176-193: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483V-type proton ATPase subunit H
PRO_0000124193

Amino acid modifications

Modified residue4831Phosphoserine Ref.9

Natural variations

Alternative sequence176 – 19318Missing in isoform 2.
VSP_012274

Experimental info

Sequence conflict1291M → I in AAD27720. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EAE0457C538AC906

FASTA48355,883
        10         20         30         40         50         60 
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE 

        70         80         90        100        110        120 
EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM LQENHQRVSI FFDYARCSKN 

       130        140        150        160        170        180 
TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS 

       190        200        210        220        230        240 
GVAVETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ 

       250        260        270        280        290        300 
YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE 

       310        320        330        340        350        360 
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK 

       370        380        390        400        410        420 
SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH 

       430        440        450        460        470        480 
YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA 


ARS 

« Hide

Isoform 2 [UniParc].

Checksum: 710D9FAE82982B7A
Show »

FASTA46554,151

References

« Hide 'large scale' references
[1]Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. expand/collapse author list , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart.
[2]"Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4."
Lu X., Yu H., Liu S.-H., Brodsky F.M., Peterlin B.M.
Immunity 8:647-656(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH HIV-1 NEF.
Tissue: B-cell.
[3]"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. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus.
[4]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Mammary gland.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Eye and Lymphoma.
[8]"Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery."
Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T., Peterlin B.M.
J. Biol. Chem. 277:28521-28529(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 NEF AND AP2M1.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF113222 mRNA. Translation: AAG39293.1.
AF298777 mRNA. Translation: AAG22809.1.
AF112204 mRNA. Translation: AAF17192.1.
AF132945 mRNA. Translation: AAD27720.1.
AK022345 mRNA. Translation: BAG51072.1.
CH471068 Genomic DNA. Translation: EAW86727.1.
BC025275 mRNA. Translation: AAH25275.1.
CCDSCCDS6153.1. [Q9UI12-1]
CCDS6154.1. [Q9UI12-2]
RefSeqNP_057025.2. NM_015941.3. [Q9UI12-1]
NP_998784.1. NM_213619.2. [Q9UI12-2]
NP_998785.1. NM_213620.2. [Q9UI12-1]
XP_006716518.1. XM_006716455.1. [Q9UI12-2]
UniGeneHs.491737.

3D structure databases

ProteinModelPortalQ9UI12.
SMRQ9UI12. Positions 227-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119635. 29 interactions.
IntActQ9UI12. 5 interactions.
MINTMINT-5006690.
STRING9606.ENSP00000352522.

Protein family/group databases

TCDB3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteQ9UI12.

Polymorphism databases

DMDM12643371.

Proteomic databases

MaxQBQ9UI12.
PaxDbQ9UI12.
PRIDEQ9UI12.

Protocols and materials databases

DNASU51606.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355221; ENSP00000347359; ENSG00000047249. [Q9UI12-2]
ENST00000359530; ENSP00000352522; ENSG00000047249. [Q9UI12-1]
ENST00000396774; ENSP00000379995; ENSG00000047249. [Q9UI12-1]
GeneID51606.
KEGGhsa:51606.
UCSCuc003xrk.4. human. [Q9UI12-1]
uc003xrn.4. human. [Q9UI12-2]

Organism-specific databases

CTD51606.
GeneCardsGC08M054678.
HGNCHGNC:18303. ATP6V1H.
HPACAB009532.
HPA023421.
MIM608861. gene.
neXtProtNX_Q9UI12.
PharmGKBPA38521.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5231.
HOGENOMHOG000007240.
HOVERGENHBG000459.
InParanoidQ9UI12.
KOK02144.
OMADTLQENH.
OrthoDBEOG7CCBQQ.
PhylomeDBQ9UI12.
TreeFamTF313488.

Enzyme and pathway databases

BioCycMetaCyc:HS00586-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9UI12.
BgeeQ9UI12.
CleanExHS_ATP6V1H.
GenevestigatorQ9UI12.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERPTHR10698. PTHR10698. 1 hit.
PfamPF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view]
PIRSFPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATP6V1H. human.
GeneWikiATP6V1H.
GenomeRNAi51606.
NextBio55498.
PROQ9UI12.
SOURCESearch...

Entry information

Entry nameVATH_HUMAN
AccessionPrimary (citable) accession number: Q9UI12
Secondary accession number(s): B3KMR0 expand/collapse secondary AC list , Q6PK44, Q9H3E3, Q9Y300
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 135 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM