VPS4A

Protein-coding gene in the species Homo sapiens
VPS4A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1YXR, 2JQ9, 2K3W

Identifiers
AliasesVPS4A, SKD1, SKD1A, SKD2, VPS4, VPS4-1, vacuolar protein sorting 4 homolog A, CIMDAG
External IDsOMIM: 609982; MGI: 1890520; HomoloGene: 69132; GeneCards: VPS4A; OMA:VPS4A - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for VPS4A
Genomic location for VPS4A
Band16q22.1Start69,311,350 bp[1]
End69,326,939 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for VPS4A
Genomic location for VPS4A
Band8|8 D3Start107,757,854 bp[2]
End107,772,387 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • cerebellar vermis

  • muscle of thigh

  • Skeletal muscle tissue of rectus abdominis

  • parotid gland

  • apex of heart

  • Brodmann area 23

  • middle temporal gyrus

  • right frontal lobe

  • endothelial cell
Top expressed in
  • spermatid

  • spermatocyte

  • seminiferous tubule

  • neural layer of retina

  • dentate gyrus of hippocampal formation granule cell

  • dorsal tegmental nucleus

  • superior colliculus

  • pontine nuclei

  • medial dorsal nucleus

  • primary visual cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • protein domain specific binding
  • microtubule-severing ATPase activity
  • protein C-terminus binding
  • protein binding
  • hydrolase activity
  • ATP binding
  • ATPase activity
  • protein-containing complex binding
Cellular component
  • cytoplasm
  • ESCRT III complex
  • cytosol
  • endosome
  • late endosome
  • centrosome
  • spindle pole
  • vacuolar membrane
  • late endosome membrane
  • Flemming body
  • membrane
  • plasma membrane
  • midbody
  • early endosome
  • perinuclear region of cytoplasm
  • lysosome
  • extracellular exosome
  • nucleus
  • endosome membrane
Biological process
  • late endosomal microautophagy
  • endosomal vesicle fusion
  • viral release from host cell
  • abscission
  • viral budding via host ESCRT complex
  • nucleus organization
  • viral life cycle
  • multivesicular body assembly
  • vacuole organization
  • vesicle uncoating
  • regulation of protein localization
  • cell division
  • intracellular cholesterol transport
  • ESCRT complex disassembly
  • vesicle budding from membrane
  • ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway
  • transport
  • protein transport
  • positive regulation of viral life cycle
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
  • cell cycle
  • negative regulation of cytokinesis
  • septum digestion after cytokinesis
  • mitotic metaphase plate congression
  • positive regulation of exosomal secretion
  • vesicle-mediated transport
  • regulation of protein localization to plasma membrane
  • ESCRT III complex disassembly
  • cytoplasmic microtubule organization
  • endosomal transport
  • macroautophagy
  • positive regulation of viral budding via host ESCRT complex
  • actomyosin contractile ring contraction
  • protein targeting to lysosome
  • nuclear envelope organization
  • nuclear membrane reassembly
  • mitotic cytokinesis checkpoint signaling
  • cytoskeleton-dependent cytokinesis
  • midbody abscission
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

27183

116733

Ensembl

ENSG00000132612

ENSMUSG00000031913

UniProt

Q9UN37

Q8VEJ9

RefSeq (mRNA)

NM_013245

NM_126165

RefSeq (protein)

NP_037377
NP_037377.1

NP_569053

Location (UCSC)Chr 16: 69.31 – 69.33 MbChr 8: 107.76 – 107.77 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.[5][6][7]

Function

The protein encoded by this gene is a member of the AAA protein family (ATPases associated with diverse cellular activities), and is the homolog of the yeast Vps4 protein. In humans, two paralogs of the yeast protein have been identified. They share a high degree of amino acid sequence similarity with each other, and also with yeast Vps4 and mouse proteins. Functional studies indicate that both human paralogs associate with the endosomal compartments, and are involved in intracellular protein trafficking, similar to Vps4 protein in yeast. The gene encoding this paralog has been mapped to chromosome 16; the gene for the other resides on chromosome 18.[7]

Interactions

VPS4A has been shown to interact with CHMP1A.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000132612 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031913 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Bishop N, Woodman P (April 2000). "ATPase-defective Mammalian VPS4 Localizes to Aberrant Endosomes and Impairs Cholesterol Trafficking". Mol Biol Cell. 11 (1): 227–39. doi:10.1091/mbc.11.1.227. PMC 14770. PMID 10637304.
  6. ^ Scheuring S, Röhricht RA, Schöning-Burkhardt B, Beyer A, Müller S, Abts HF, Köhrer K (September 2001). "Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking". J Mol Biol. 312 (3): 469–80. doi:10.1006/jmbi.2001.4917. PMID 11563910.
  7. ^ a b "Entrez Gene: VPS4A vacuolar protein sorting 4 homolog A (S. cerevisiae)".
  8. ^ Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (July 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.

Further reading

  • Scheuring S, Bodor O, Röhricht RA, Müller S, Beyer A, Köhrer K (1999). "Cloning, characterisation, and functional expression of the Mus musculus SKD1 gene in yeast demonstrates that the mouse SKD1 and the yeast VPS4 genes are orthologues and involved in intracellular protein trafficking". Gene. 234 (1): 149–59. doi:10.1016/S0378-1119(99)00163-8. PMID 10393249.
  • Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
  • Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J. Cell Sci. 114 (Pt 13): 2395–404. doi:10.1242/jcs.114.13.2395. PMID 11559748.
  • Tanaka H, Fujita H, Katoh H, Mori K, Negishi M (2002). "Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2". Biochem. J. 365 (Pt 2): 349–53. doi:10.1042/BJ20020062. PMC 1222680. PMID 11931639.
  • Nara A, Mizushima N, Yamamoto A, Kabeya Y, Ohsumi Y, Yoshimori T (2002). "SKD1 AAA ATPase-dependent endosomal transport is involved in autolysosome formation". Cell Struct. Funct. 27 (1): 29–37. doi:10.1247/csf.27.29. PMID 11937716.
  • Chagnon P, Michaud J, Mitchell G, Mercier J, Marion JF, Drouin E, Rasquin-Weber A, Hudson TJ, Richter A (2003). "A Missense Mutation (R565W) in Cirhin (FLJ14728) in North American Indian Childhood Cirrhosis". Am. J. Hum. Genet. 71 (6): 1443–9. doi:10.1086/344580. PMC 378590. PMID 12417987.
  • Beyer A, Scheuring S, Müller S, Mincheva A, Lichter P, Köhrer K (2003). "Comparative sequence and expression analyses of four mammalian VPS4 genes". Gene. 305 (1): 47–59. doi:10.1016/S0378-1119(02)01205-2. PMID 12594041.
  • Katoh K, Shibata H, Suzuki H, Nara A, Ishidoh K, Kominami E, Yoshimori T, Maki M (2003). "The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting". J. Biol. Chem. 278 (40): 39104–13. doi:10.1074/jbc.M301604200. PMID 12860994.
  • Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi:10.1016/S0092-8674(03)00653-6. PMID 14505569. S2CID 10733770.
  • von Schwedler UK, Stuchell M, Müller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Kräusslich HG, Kaplan J, Morham SG, Sundquist WI (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. S2CID 16894972.
  • Sachse M, Strous GJ, Klumperman J (2004). "ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles". J. Cell Sci. 117 (Pt 9): 1699–708. doi:10.1242/jcs.00998. PMID 15075231.
  • Lin Y, Kimpler LA, Naismith TV, Lauer JM, Hanson PI (2005). "Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1". J. Biol. Chem. 280 (13): 12799–809. doi:10.1074/jbc.M413968200. PMID 15632132.
  • Scott A, Gaspar J, Stuchell-Brereton MD, Alam SL, Skalicky JJ, Sundquist WI (2005). "Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A". Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13813–8. Bibcode:2005PNAS..10213813S. doi:10.1073/pnas.0502165102. PMC 1236530. PMID 16174732.
  • Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
  • Chen VY, Posada MM, Blazer LL, Zhao T, Rosania GR (2007). "The role of the VPS4A-exosome pathway in the intrinsic egress route of a DNA-binding anticancer drug". Pharm. Res. 23 (8): 1687–95. doi:10.1007/s11095-006-9043-0. PMID 16841193. S2CID 2777033.
  • Lambert C, Döring T, Prange R (2007). "Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and γ2-Adaptin". J. Virol. 81 (17): 9050–60. doi:10.1128/JVI.00479-07. PMC 1951427. PMID 17553870.
  • v
  • t
  • e
  • 1yxr: NMR Structure of VPS4A MIT Domain
    1yxr: NMR Structure of VPS4A MIT Domain


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