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Q9UN37

- VPS4A_HUMAN

UniProt

Q9UN37 - VPS4A_HUMAN

Protein

Vacuolar protein sorting-associated protein 4A

Gene

VPS4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission (PubMed:24814515).4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi167 – 1748ATPCurated

    GO - Molecular functioni

    1. ATPase activity, coupled Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. abscission Source: UniProtKB
    2. ATP catabolic process Source: GOC
    3. cytokinesis Source: UniProtKB
    4. cytokinesis checkpoint Source: UniProtKB
    5. endosomal transport Source: UniProtKB
    6. membrane organization Source: Reactome
    7. negative regulation of cytokinesis Source: UniProtKB
    8. protein transport Source: UniProtKB-KW
    9. vesicle-mediated transport Source: UniProtKB
    10. viral life cycle Source: Reactome
    11. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vacuolar protein sorting-associated protein 4A (EC:3.6.4.6)
    Alternative name(s):
    Protein SKD2
    VPS4-1
    Short name:
    hVPS4
    Gene namesi
    Name:VPS4AImported
    Synonyms:VPS4Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:13488. VPS4A.

    Subcellular locationi

    Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane Curated; Peripheral membrane protein Curated. Midbody
    Note: Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody (PubMed:24814515). Localized in two distinct rings on either side of the Fleming body.1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. late endosome membrane Source: UniProtKB-SubCell
    5. midbody Source: UniProtKB
    6. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131V → A or D: Diminishes interaction with IST1. 2 Publications
    Mutagenesisi13 – 131V → D: Abolishes interaction with CHMP6, no effect on interaction with CHMP1A. 2 Publications
    Mutagenesisi13 – 131V → D: Greatly diminishes localization to punctate class E compartments; when associated with Q-173. 2 Publications
    Mutagenesisi64 – 641L → A or D: Abolishes interaction with CHMP1B; diminishes interaction with IST1. 5 Publications
    Mutagenesisi64 – 641L → D: Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with Q-173. 5 Publications
    Mutagenesisi64 – 641L → D: Modestly reduces interaction with CHMP6. 5 Publications
    Mutagenesisi68 – 681E → D: Diminishes interaction with CHMP1B. 1 Publication
    Mutagenesisi173 – 1731K → Q: Defective in ATP-binding. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol sorting. Inhibits HIV-1 release. Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with D-64. Greatly diminishes localization to punctate class E compartments; when associated with D-173. 4 Publications
    Mutagenesisi201 – 2022WL → AA: Strongly impairs HIV-1 release.
    Mutagenesisi203 – 2031G → A: Impairs HIV-1 release. 1 Publication
    Mutagenesisi228 – 2281E → Q: Defective in ATP-hydrolysis. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol and protein sorting. Inhibits HIV-1 release. Increases binding to CHMP1. 5 Publications

    Organism-specific databases

    PharmGKBiPA38362.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 437436Vacuolar protein sorting-associated protein 4APRO_0000084765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei8 – 81N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UN37.
    PaxDbiQ9UN37.
    PRIDEiQ9UN37.

    PTM databases

    PhosphoSiteiQ9UN37.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9UN37.
    BgeeiQ9UN37.
    CleanExiHS_VPS4A.
    GenevestigatoriQ9UN37.

    Organism-specific databases

    HPAiCAB018751.

    Interactioni

    Subunit structurei

    Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner By similarity. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP6. Interacts with VPS4B; the interaction suggests a heteromeric assembly with VPS4B. Interacts with SPAST. Interacts with IST1. Interacts with ZFYVE19/ANCHR; leading to retain it at midbody.By similarity12 Publications

    Protein-protein interaction databases

    BioGridi118059. 18 interactions.
    DIPiDIP-44585N.
    IntActiQ9UN37. 6 interactions.
    STRINGi9606.ENSP00000254950.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 2117
    Helixi25 – 4521
    Helixi50 – 7627

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YXRNMR-A1-77[»]
    2JQ9NMR-A1-84[»]
    2K3WNMR-A1-84[»]
    ProteinModelPortaliQ9UN37.
    SMRiQ9UN37. Positions 1-101, 116-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UN37.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8079MITAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8483Interaction with CHMP1BAdd
    BLAST

    Domaini

    The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2).

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Sequence Analysis
    Contains 1 MIT domain.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG0464.
    HOGENOMiHOG000225146.
    HOVERGENiHBG057074.
    InParanoidiQ9UN37.
    KOiK12196.
    OMAiARTQMFR.
    OrthoDBiEOG74BJS2.
    PhylomeDBiQ9UN37.
    TreeFamiTF105012.

    Family and domain databases

    Gene3Di1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view]
    SUPFAMiSSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UN37-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTSTLQKAI DLVTKATEED KAKNYEEALR LYQHAVEYFL HAIKYEAHSD    50
    KAKESIRAKC VQYLDRAEKL KDYLRSKEKH GKKPVKENQS EGKGSDSDSE 100
    GDNPEKKKLQ EQLMGAVVME KPNIRWNDVA GLEGAKEALK EAVILPIKFP 150
    HLFTGKRTPW RGILLFGPPG TGKSYLAKAV ATEANNSTFF SVSSSDLMSK 200
    WLGESEKLVK NLFELARQHK PSIIFIDEVD SLCGSRNENE SEAARRIKTE 250
    FLVQMQGVGN NNDGTLVLGA TNIPWVLDSA IRRRFEKRIY IPLPEEAARA 300
    QMFRLHLGST PHNLTDANIH ELARKTEGYS GADISIIVRD SLMQPVRKVQ 350
    SATHFKKVCG PSRTNPSMMI DDLLTPCSPG DPGAMEMTWM DVPGDKLLEP 400
    VVCMSDMLRS LATTRPTVNA DDLLKVKKFS EDFGQES 437
    Length:437
    Mass (Da):48,898
    Last modified:May 1, 2000 - v1
    Checksum:iC3CC556FB84F105C
    GO

    Sequence cautioni

    The sequence AAL75948.1 differs from that shown. Reason: Frameshift at positions 123, 133, 157 and 163.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791K → E in AAL75948. 1 PublicationCurated
    Sequence conflicti79 – 791K → E in AAF17203. (PubMed:10931946)Curated
    Sequence conflicti185 – 1851N → T in AAL75948. 1 PublicationCurated
    Sequence conflicti284 – 2841R → K in AAD42971. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255952 mRNA. Translation: AAK52408.1.
    AF282903 Genomic DNA. Translation: AAG01470.1.
    AF132747 mRNA. Translation: AAL75948.1. Frameshift.
    AF159063 mRNA. Translation: AAD49227.1.
    AF112215 mRNA. Translation: AAF17203.1.
    AK315026 mRNA. Translation: BAG37514.1.
    CH471092 Genomic DNA. Translation: EAW83263.1.
    BC047932 mRNA. Translation: AAH47932.1.
    AF155740 mRNA. Translation: AAD42971.1.
    CCDSiCCDS45517.1.
    RefSeqiNP_037377.1. NM_013245.2.
    UniGeneiHs.128420.

    Genome annotation databases

    EnsembliENST00000254950; ENSP00000254950; ENSG00000132612.
    GeneIDi27183.
    KEGGihsa:27183.
    UCSCiuc002eww.3. human.

    Polymorphism databases

    DMDMi62511240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF255952 mRNA. Translation: AAK52408.1 .
    AF282903 Genomic DNA. Translation: AAG01470.1 .
    AF132747 mRNA. Translation: AAL75948.1 . Frameshift.
    AF159063 mRNA. Translation: AAD49227.1 .
    AF112215 mRNA. Translation: AAF17203.1 .
    AK315026 mRNA. Translation: BAG37514.1 .
    CH471092 Genomic DNA. Translation: EAW83263.1 .
    BC047932 mRNA. Translation: AAH47932.1 .
    AF155740 mRNA. Translation: AAD42971.1 .
    CCDSi CCDS45517.1.
    RefSeqi NP_037377.1. NM_013245.2.
    UniGenei Hs.128420.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YXR NMR - A 1-77 [» ]
    2JQ9 NMR - A 1-84 [» ]
    2K3W NMR - A 1-84 [» ]
    ProteinModelPortali Q9UN37.
    SMRi Q9UN37. Positions 1-101, 116-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118059. 18 interactions.
    DIPi DIP-44585N.
    IntActi Q9UN37. 6 interactions.
    STRINGi 9606.ENSP00000254950.

    PTM databases

    PhosphoSitei Q9UN37.

    Polymorphism databases

    DMDMi 62511240.

    Proteomic databases

    MaxQBi Q9UN37.
    PaxDbi Q9UN37.
    PRIDEi Q9UN37.

    Protocols and materials databases

    DNASUi 27183.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254950 ; ENSP00000254950 ; ENSG00000132612 .
    GeneIDi 27183.
    KEGGi hsa:27183.
    UCSCi uc002eww.3. human.

    Organism-specific databases

    CTDi 27183.
    GeneCardsi GC16P069335.
    HGNCi HGNC:13488. VPS4A.
    HPAi CAB018751.
    MIMi 609982. gene.
    neXtProti NX_Q9UN37.
    PharmGKBi PA38362.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0464.
    HOGENOMi HOG000225146.
    HOVERGENi HBG057074.
    InParanoidi Q9UN37.
    KOi K12196.
    OMAi ARTQMFR.
    OrthoDBi EOG74BJS2.
    PhylomeDBi Q9UN37.
    TreeFami TF105012.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    ChiTaRSi VPS4A. human.
    EvolutionaryTracei Q9UN37.
    GeneWikii VPS4A.
    GenomeRNAii 27183.
    NextBioi 50017.
    PROi Q9UN37.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UN37.
    Bgeei Q9UN37.
    CleanExi HS_VPS4A.
    Genevestigatori Q9UN37.

    Family and domain databases

    Gene3Di 1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking."
      Scheuring S., Roehricht R.A., Schoening-Burkhardt B., Beyer A., Mueller S., Abts H.F., Koehrer K.
      J. Mol. Biol. 312:469-480(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VPS4B, MUTAGENESIS OF GLU-228.
      Tissue: Keratinocyte.
    2. "Comparative sequence and expression analyses of four mammalian VPS4 genes."
      Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K.
      Gene 305:47-59(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of a new human cDNA homologous to Homo sapiens SKD1 protein."
      Ding J.B., Yu L., Zhao S.Y.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Isolation of a homolog of SKD1."
      Patejunas G.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: HypothalamusImported.
    6. "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: Kidney.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
    9. "ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking."
      Bishop N., Woodman P.
      Mol. Biol. Cell 11:227-239(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-437, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-173 AND GLU-228.
      Tissue: BrainImported.
    10. Cited for: FUNCTION IN VIRUS RELEASE, MUTAGENESIS OF LYS-173 AND GLU-228.
    11. "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
      Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
      J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP1A, MUTAGENESIS OF GLU-228.
    12. Cited for: INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP4A; CHMP4B; CHMP4C AND CHMP6.
    13. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP2B AND CHMP3.
    14. Erratum
      Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
      Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
    15. "ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles."
      Sachse M., Strous G.J., Klumperman J.
      J. Cell Sci. 117:1699-1708(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLU-228.
    16. Cited for: MUTAGENESIS OF 201-TRP-LEU-202 AND GLY-203.
    17. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
      Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
      EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    18. "Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
      Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
      Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPAST.
    19. Cited for: INTERACTION WITH IST1, MUTAGENESIS OF LEU-64.
    20. "Biochemical analyses of human IST1 and its function in cytokinesis."
      Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
      Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IST1, MUTAGENESIS OF VAL-13 AND LEU-64.
    21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
      Kuang Z., Seo E.J., Leis J.
      J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHMP1B; CHMP2A; CHMP3; CHMP4B AND CHMP6.
    24. "ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
      Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
      Nat. Cell Biol. 16:550-560(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE19.
    25. Cited for: STRUCTURE BY NMR OF 1-77, INTERACTION WITH CHMP1B, MUTAGENESIS OF LEU-64 AND GLU-68.
    26. Cited for: STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP1A, INTERACTION WITH CHMP2B, MUTAGENESIS OF LEU-64 AND LYS-173.
    27. "Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding."
      Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J., Sundquist W.I.
      Dev. Cell 15:62-73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP6, INTERACTION WITH CHMP1A, MUTAGENESIS OF VAL-13; LEU-64 AND LYS-173.

    Entry informationi

    Entry nameiVPS4A_HUMAN
    AccessioniPrimary (citable) accession number: Q9UN37
    Secondary accession number(s): B2RCB7
    , Q8TF07, Q9UI03, Q9Y582
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 131 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3