VPS53

VPS53
Identifiers
AliasesVPS53, HCCS1, PCH2E, hVps53L, pp13624, GARP complex subunit
External IDsMGI: 1915549 HomoloGene: 6264 GeneCards: VPS53
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17p13.3Start508,668 bp[1]
End721,717 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

55275

68299

Ensembl

ENSG00000283883
ENSG00000141252

ENSMUSG00000017288

UniProt

Q5VIR6

Q8CCB4

RefSeq (mRNA)

NM_001128159
NM_018289

NM_026664
NM_001364738

RefSeq (protein)

NP_001121631
NP_060759

NP_080940
NP_001351667

Location (UCSC)Chr 17: 0.51 – 0.72 MbChr 11: 76.05 – 76.18 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vacuolar protein sorting 53 homolog (S. cerevisiae) is a protein that in humans is encoded by the VPS53 gene.[5]

Function

This gene encodes a protein with sequence similarity to the yeast Vps53p protein. Vps53p is involved in retrograde vesicle trafficking in late Golgi. [provided by RefSeq, Jul 2008].

Mutations in VPS53 cause cerebello-cerebral atrophy type 2 .[6]

References

  1. 1 2 3 ENSG00000141252 GRCh38: Ensembl release 89: ENSG00000283883, ENSG00000141252 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000017288 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ "Entrez Gene: Vacuolar protein sorting 53 homolog (S. cerevisiae)".
  6. ↑ Feinstein M, Flusser H, Lerman-Sagie T, Ben-Zeev B, Lev D, Agamy O, Cohen I, Kadir R, Sivan S, Leshinsky-Silver E, Markus B, Birk OS (May 2014). "VPS53 mutations cause progressive cerebello-cerebral atrophy type 2 (PCCA2)". Journal of Medical Genetics. 51 (5): 303–8. doi:10.1136/jmedgenet-2013-101823. PMID 24577744.

Further reading

  • Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH (April 2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". American Journal of Human Genetics. 72 (4): 918–30. doi:10.1086/374320. PMC 1180354. PMID 12621583.
  • Pérez-Victoria FJ, Schindler C, Magadán JG, Mardones GA, Delevoye C, Romao M, Raposo G, Bonifacino JS (October 2010). "Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex". Molecular Biology of the Cell. 21 (19): 3386–95. doi:10.1091/mbc.E10-05-0392. PMC 2947474. PMID 20685960.
  • Zhu JD, Fei Q, Wang P, Lan F, Mao DQ, Zhang HY, Yao XB (September 2006). "Transcription of the putative tumor suppressor gene HCCS1 requires binding of ETS-2 to its consensus near the transcription start site". Cell Research. 16 (9): 780–96. doi:10.1038/sj.cr.7310092. PMID 16953216.
  • Pérez-Victoria FJ, Bonifacino JS (October 2009). "Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network". Molecular and Cellular Biology. 29 (19): 5251–63. doi:10.1128/MCB.00495-09. PMC 2747979. PMID 19620288.
  • Ko JK, Choi KH, Pan Z, Lin P, Weisleder N, Kim CW, Ma J (August 2007). "The tail-anchoring domain of Bfl1 and HCCS1 targets mitochondrial membrane permeability to induce apoptosis". Journal of Cell Science. 120 (Pt 16): 2912–23. doi:10.1242/jcs.006197. PMID 17666431.
  • Liewen H, Meinhold-Heerlein I, Oliveira V, Schwarzenbacher R, Luo G, Wadle A, Jung M, Pfreundschuh M, Stenner-Liewen F (May 2005). "Characterization of the human GARP (Golgi associated retrograde protein) complex". Experimental Cell Research. 306 (1): 24–34. doi:10.1016/j.yexcr.2005.01.022. PMID 15878329.
  • Zhao X, He M, Wan D, Ye Y, He Y, Han L, Guo M, Huang Y, Qin W, Wang MW, Chong W, Chen J, Zhang L, Yang N, Xu B, Wu M, Zuo L, Gu J (February 2003). "The minimum LOH region defined on chromosome 17p13.3 in human hepatocellular carcinoma with gene content analysis". Cancer Letters. 190 (2): 221–32. doi:10.1016/s0304-3835(02)00622-5. PMID 12565177.
  • Pérez-Victoria FJ, Mardones GA, Bonifacino JS (June 2008). "Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of cathepsin D to lysosomes". Molecular Biology of the Cell. 19 (6): 2350–62. doi:10.1091/mbc.E07-11-1189. PMC 2397299. PMID 18367545.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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