VPS4B

VPS4B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1WR0, 1XWI, 2CPT, 2JQH, 2JQK, 4U7Y
Identifiers
Aliases	VPS4B, SKD1, SKD1B, VPS4-2, MIG1, vacuolar protein sorting 4 homolog B
External IDs	OMIM: 609983 MGI: 1100499 HomoloGene: 37976 GeneCards: VPS4B
Gene location (Human)
Chr.	Chromosome 18 (human)[1]
End	63,422,483 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	106,724,458 bp[2]
RNA expression pattern
	Top expressed in
	endothelial cell; ; amniotic fluid; ; secondary oocyte; ; cavity of mouth; ; Achilles tendon; ; palpebral conjunctiva; ; hair follicle; ; pancreatic ductal cell; ; germinal epithelium; ; thymus;
	Top expressed in
	conjunctival fornix; ; ciliary body; ; Paneth cell; ; lacrimal gland; ; hair follicle; ; primitive streak; ; iris; ; medullary collecting duct; ; ureter; ; condyle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; protein homodimerization activity; ATPase activity; protein C-terminus binding; protein binding; identical protein binding; hydrolase activity; ATP binding;
Cellular component	cytoplasm; cytosol; endosome; centrosome; spindle pole; membrane; late endosome membrane; Flemming body; endosome membrane; extracellular exosome; nucleus;
Biological process	late endosomal microautophagy; regulation of centrosome duplication; protein depolymerization; viral budding via host ESCRT complex; viral life cycle; nucleus organization; cholesterol transport; negative regulation of exosomal secretion; multivesicular body assembly; negative regulation of cell death; regulation of mitotic spindle assembly; endosome organization; cell division; positive regulation of centriole elongation; endosomal transport; potassium ion transport; response to lipid; ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; protein transport; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; positive regulation of G2/M transition of mitotic cell cycle; positive regulation of exosomal secretion; septum digestion after cytokinesis; mitotic metaphase plate congression; endosome to lysosome transport via multivesicular body sorting pathway; cell cycle; ESCRT III complex disassembly; macroautophagy; transport; positive regulation of viral process; vacuole organization; midbody abscission;
	Sources:Amigo / QuickGO
Orthologs
	9525
	20479
	ENSG00000119541
	ENSMUSG00000009907
	O75351
	P46467
	NM_004869
	NM_009190
	NP_004860; NP_004860.2
	NP_033216
	Wikidata
View/Edit Human	View/Edit Mouse

Vacuolar protein sorting-associated protein 4B is a protein that in humans is encoded by the VPS4B gene.[5][6]

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 18; the gene for the other (VPS4A) resides on chromosome 16.[6]

References

GRCh38: Ensembl release 89: ENSG00000119541 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000009907 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Scheuring S, Rohricht RA, Schoning-Burkhardt B, Beyer A, Muller S, Abts HF, Kohrer K (Sep 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.
"Entrez Gene: VPS4B vacuolar protein sorting 4 homolog B (S. cerevisiae)".

Périer F, Coulter KL, Liang H, et al. (1994). "Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast". FEBS Lett. 351 (2): 286–90. doi:10.1016/0014-5793(94)00879-5. PMID 8082782. S2CID 31778093.
Mao M, Fu G, Wu JS, et al. (1998). "Identification of genes expressed in human CD34+ hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8175–80. Bibcode:1998PNAS...95.8175M. doi:10.1073/pnas.95.14.8175. PMC 20949. PMID 9653160.
Scheuring S, Bodor O, Röhricht RA, et al. (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.
Bishop N, Woodman P (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.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
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.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Beyer A, Scheuring S, Müller S, et al. (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.
Strack B, Calistri A, Craig S, et al. (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, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. S2CID 16894972.
Fujita H, Umezuki Y, Imamura K, et al. (2005). "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B". J. Cell Sci. 117 (Pt 14): 2997–3009. doi:10.1242/jcs.01170. PMID 15173323.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Katoh K, Suzuki H, Terasawa Y, et al. (2006). "The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B". Biochem. J. 391 (Pt 3): 677–85. doi:10.1042/BJ20050398. PMC 1276969. PMID 16004603.
Takasu H, Jee JG, Ohno A, et al. (2005). "Structural characterization of the MIT domain from human Vps4b". Biochem. Biophys. Res. Commun. 334 (2): 460–5. doi:10.1016/j.bbrc.2005.06.110. PMID 16018968.
Scott A, Chung HY, Gonciarz-Swiatek M, et al. (2005). "Structural and mechanistic studies of VPS4 proteins". EMBO J. 24 (20): 3658–69. doi:10.1038/sj.emboj.7600818. PMC 1276703. PMID 16193069.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Welsch S, Habermann A, Jäger S, et al. (2007). "Ultrastructural analysis of ESCRT proteins suggests a role for endosome-associated tubular-vesicular membranes in ESCRT function". Traffic. 7 (11): 1551–66. doi:10.1111/j.1600-0854.2006.00489.x. PMID 17014699.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000119541 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000009907 - 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.

[pmid11563910-5] Scheuring S, Rohricht RA, Schoning-Burkhardt B, Beyer A, Muller S, Abts HF, Kohrer K (Sep 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.

[entrez-6] "Entrez Gene: VPS4B vacuolar protein sorting 4 homolog B (S. cerevisiae)".

VPS4B

References

Further reading