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Protein

V-type proton ATPase subunit H

Gene

ATP6V1H

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

Functioni

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.By similarity

GO - Molecular functioni

  1. enzyme regulator activity Source: UniProtKB
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: UniProtKB
  2. cellular iron ion homeostasis Source: Reactome
  3. endocytosis Source: UniProtKB
  4. insulin receptor signaling pathway Source: Reactome
  5. interaction with host Source: Reactome
  6. metabolic process Source: GOC
  7. phagosome maturation Source: Reactome
  8. regulation of catalytic activity Source: GOC
  9. regulation of defense response to virus by virus Source: Reactome
  10. transferrin transport Source: Reactome
  11. transmembrane transport Source: Reactome
  12. vacuolar acidification Source: UniProtKB
  13. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS00586-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ATP6V1H
ORF Names:CGI-11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:18303. ATP6V1H.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. lysosomal membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
  5. vacuolar proton-transporting V-type ATPase, V1 domain Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38521.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483V-type proton ATPase subunit HPRO_0000124193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei483 – 4831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UI12.
PaxDbiQ9UI12.
PRIDEiQ9UI12.

PTM databases

PhosphoSiteiQ9UI12.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9UI12.
CleanExiHS_ATP6V1H.
ExpressionAtlasiQ9UI12. baseline and differential.
GenevestigatoriQ9UI12.

Organism-specific databases

HPAiCAB009532.
HPA023421.

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

Protein-protein interaction databases

BioGridi119635. 29 interactions.
IntActiQ9UI12. 5 interactions.
MINTiMINT-5006690.
STRINGi9606.ENSP00000352522.

Structurei

3D structure databases

ProteinModelPortaliQ9UI12.
SMRiQ9UI12. Positions 227-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase H subunit family.Curated

Phylogenomic databases

eggNOGiCOG5231.
GeneTreeiENSGT00390000003289.
HOGENOMiHOG000007240.
HOVERGENiHBG000459.
InParanoidiQ9UI12.
KOiK02144.
OMAiDTLQENH.
OrthoDBiEOG7CCBQQ.
PhylomeDBiQ9UI12.
TreeFamiTF313488.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UI12-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI
60 70 80 90 100
QRFEMKRSPE EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM
110 120 130 140 150
LQENHQRVSI FFDYARCSKN TAWPYFLPML NRQDPFTVHM AARIIAKLAA
160 170 180 190 200
WGKELMEGSD LNYYFNWIKT QLSSQKLRGS GVAVETGTVS SSDSSQYVQC
210 220 230 240 250
VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ YQMIFSIWLL
260 270 280 290 300
AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE
310 320 330 340 350
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS
360 370 380 390 400
SFDEYSSELK SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV
410 420 430 440 450
SDDPQVLAVA AHDVGEYVRH YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY
460 470 480
NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA ARS
Length:483
Mass (Da):55,883
Last modified:April 30, 2000 - v1
Checksum:iEAE0457C538AC906
GO
Isoform 2 (identifier: Q9UI12-2) [UniParc]FASTAAdd to basket

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

Show »
Length:465
Mass (Da):54,151
Checksum:i710D9FAE82982B7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291M → I in AAD27720 (PubMed:10810093).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei176 – 19318Missing in isoform 2. 1 PublicationVSP_012274Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6153.1. [Q9UI12-1]
CCDS6154.1. [Q9UI12-2]
RefSeqiNP_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]
UniGeneiHs.491737.

Genome annotation databases

EnsembliENST00000355221; ENSP00000347359; ENSG00000047249. [Q9UI12-2]
ENST00000359530; ENSP00000352522; ENSG00000047249. [Q9UI12-1]
ENST00000396774; ENSP00000379995; ENSG00000047249. [Q9UI12-1]
GeneIDi51606.
KEGGihsa:51606.
UCSCiuc003xrk.4. human. [Q9UI12-1]
uc003xrn.4. human. [Q9UI12-2]

Polymorphism databases

DMDMi12643371.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6153.1. [Q9UI12-1]
CCDS6154.1. [Q9UI12-2]
RefSeqiNP_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]
UniGeneiHs.491737.

3D structure databases

ProteinModelPortaliQ9UI12.
SMRiQ9UI12. Positions 227-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119635. 29 interactions.
IntActiQ9UI12. 5 interactions.
MINTiMINT-5006690.
STRINGi9606.ENSP00000352522.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiQ9UI12.

Polymorphism databases

DMDMi12643371.

Proteomic databases

MaxQBiQ9UI12.
PaxDbiQ9UI12.
PRIDEiQ9UI12.

Protocols and materials databases

DNASUi51606.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355221; ENSP00000347359; ENSG00000047249. [Q9UI12-2]
ENST00000359530; ENSP00000352522; ENSG00000047249. [Q9UI12-1]
ENST00000396774; ENSP00000379995; ENSG00000047249. [Q9UI12-1]
GeneIDi51606.
KEGGihsa:51606.
UCSCiuc003xrk.4. human. [Q9UI12-1]
uc003xrn.4. human. [Q9UI12-2]

Organism-specific databases

CTDi51606.
GeneCardsiGC08M054678.
HGNCiHGNC:18303. ATP6V1H.
HPAiCAB009532.
HPA023421.
MIMi608861. gene.
neXtProtiNX_Q9UI12.
PharmGKBiPA38521.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5231.
GeneTreeiENSGT00390000003289.
HOGENOMiHOG000007240.
HOVERGENiHBG000459.
InParanoidiQ9UI12.
KOiK02144.
OMAiDTLQENH.
OrthoDBiEOG7CCBQQ.
PhylomeDBiQ9UI12.
TreeFamiTF313488.

Enzyme and pathway databases

BioCyciMetaCyc:HS00586-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSiATP6V1H. human.
GeneWikiiATP6V1H.
GenomeRNAii51606.
NextBioi55498.
PROiQ9UI12.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UI12.
CleanExiHS_ATP6V1H.
ExpressionAtlasiQ9UI12. baseline and differential.
GenevestigatoriQ9UI12.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
1.25.40.150. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR004908. ATPase_V1-cplx_hsu.
IPR011987. ATPase_V1-cplx_hsu_C.
[Graphical view]
PANTHERiPTHR10698. PTHR10698. 1 hit.
PfamiPF11698. V-ATPase_H_C. 1 hit.
PF03224. V-ATPase_H_N. 1 hit.
[Graphical view]
PIRSFiPIRSF032184. ATPase_V1_H. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH HIV-1 NEF.
    Tissue: B-cell.
  3. 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(1999) [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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  6. 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(2003) [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(2001) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVATH_HUMAN
AccessioniPrimary (citable) accession number: Q9UI12
Secondary accession number(s): B3KMR0
, Q6PK44, Q9H3E3, Q9Y300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2001
Last sequence update: April 30, 2000
Last modified: March 3, 2015
This is version 141 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.