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Q9UI12

- VATH_HUMAN

UniProt

Q9UI12 - VATH_HUMAN

Protein

V-type proton ATPase subunit H

Gene

ATP6V1H

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. proton-transporting ATPase activity, rotational mechanism Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP hydrolysis coupled proton transport Source: UniProtKB
    3. cellular iron ion homeostasis Source: Reactome
    4. endocytosis Source: UniProtKB
    5. insulin receptor signaling pathway Source: Reactome
    6. interaction with host Source: Reactome
    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

    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:18303. ATP6V1H.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    ArrayExpressiQ9UI12.
    BgeeiQ9UI12.
    CleanExiHS_ATP6V1H.
    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.
    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. Align

    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

    MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI    50
    QRFEMKRSPE EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM 100
    LQENHQRVSI FFDYARCSKN TAWPYFLPML NRQDPFTVHM AARIIAKLAA 150
    WGKELMEGSD LNYYFNWIKT QLSSQKLRGS GVAVETGTVS SSDSSQYVQC 200
    VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ YQMIFSIWLL 250
    AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE 300
    TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS 350
    SFDEYSSELK SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV 400
    SDDPQVLAVA AHDVGEYVRH YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY 450
    NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA ARS 483
    Length:483
    Mass (Da):55,883
    Last modified:May 1, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6153.1. [Q9UI12-1 ]
    CCDS6154.1. [Q9UI12-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.491737.

    3D structure databases

    ProteinModelPortali Q9UI12.
    SMRi Q9UI12. Positions 227-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119635. 29 interactions.
    IntActi Q9UI12. 5 interactions.
    MINTi MINT-5006690.
    STRINGi 9606.ENSP00000352522.

    Protein family/group databases

    TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

    PTM databases

    PhosphoSitei Q9UI12.

    Polymorphism databases

    DMDMi 12643371.

    Proteomic databases

    MaxQBi Q9UI12.
    PaxDbi Q9UI12.
    PRIDEi Q9UI12.

    Protocols and materials databases

    DNASUi 51606.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355221 ; ENSP00000347359 ; ENSG00000047249 . [Q9UI12-2 ]
    ENST00000359530 ; ENSP00000352522 ; ENSG00000047249 . [Q9UI12-1 ]
    ENST00000396774 ; ENSP00000379995 ; ENSG00000047249 . [Q9UI12-1 ]
    GeneIDi 51606.
    KEGGi hsa:51606.
    UCSCi uc003xrk.4. human. [Q9UI12-1 ]
    uc003xrn.4. human. [Q9UI12-2 ]

    Organism-specific databases

    CTDi 51606.
    GeneCardsi GC08M054678.
    HGNCi HGNC:18303. ATP6V1H.
    HPAi CAB009532.
    HPA023421.
    MIMi 608861. gene.
    neXtProti NX_Q9UI12.
    PharmGKBi PA38521.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5231.
    HOGENOMi HOG000007240.
    HOVERGENi HBG000459.
    InParanoidi Q9UI12.
    KOi K02144.
    OMAi DTLQENH.
    OrthoDBi EOG7CCBQQ.
    PhylomeDBi Q9UI12.
    TreeFami TF313488.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00586-MONOMER.
    Reactomei REACT_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

    ChiTaRSi ATP6V1H. human.
    GeneWikii ATP6V1H.
    GenomeRNAii 51606.
    NextBioi 55498.
    PROi Q9UI12.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UI12.
    Bgeei Q9UI12.
    CleanExi HS_ATP6V1H.
    Genevestigatori Q9UI12.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    1.25.40.150. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR004908. ATPase_V1-cplx_hsu.
    IPR011987. ATPase_V1-cplx_hsu_C.
    [Graphical view ]
    PANTHERi PTHR10698. PTHR10698. 1 hit.
    Pfami PF11698. V-ATPase_H_C. 1 hit.
    PF03224. V-ATPase_H_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF032184. ATPase_V1_H. 1 hit.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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(1998) [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(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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 137 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