ZFYVE20

RBSN
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1YZM, 1Z0J, 1Z0K
Identifiers
Aliases	RBSN, Rabenosyn-5, ZFYVE20, rabenosyn, RAB effector
External IDs	MGI: 1925537 HomoloGene: 41477 GeneCards: RBSN
Gene ontology Molecular function • zinc ion binding • metal ion binding • Rab GTPase binding • protein binding Cellular component • endosome • early endosome membrane • intracellular membrane-bounded organelle • membrane • cytoplasmic side of endosome membrane • plasma membrane • endosome membrane • extracellular exosome • cytosol Biological process • endosomal vesicle fusion • Golgi to vacuole transport • endocytosis • vacuole inheritance • Golgi to endosome transport • blood coagulation • endosomal transport • transport • protein transport • regulation of Golgi organization • Golgi to lysosome transport • early endosome to Golgi transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	64145	78287
Ensembl	ENSG00000131381	ENSMUSG00000014550
UniProt	Q9H1K0	Q80Y56
RefSeq (mRNA)	NM_001302378 NM_022340	NM_030081
RefSeq (protein)	NP_001289307.1 NP_071735.2	NP_084357.2
Location (UCSC)	Chr 3: 15.07 – 15.1 Mb	Chr 6: 92.19 – 92.21 Mb
PubMed search	[1]	[2]
Wikidata

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View/Edit Mouse

Rabenosyn-5 is a protein that in humans is encoded by the ZFYVE20 gene.^[3][4]

Interactions

ZFYVE20 has been shown to interact with RAB5A.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, Hoflack B, Zerial M (Nov 2000). "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain". J Cell Biol. 151 (3): 601–12. doi:10.1083/jcb.151.3.601. PMC 2185588. PMID 11062261.
4. "Entrez Gene: ZFYVE20 zinc finger, FYVE domain containing 20".

Further reading

• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• Eathiraj S, Pan X, Ritacco C, Lambright DG (2005). "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.". Nature. 436 (7049): 415–9. doi:10.1038/nature03798. PMC 1360218. PMID 16034420.
• 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.
• Naslavsky N, Boehm M, Backlund PS, Caplan S (2005). "Rabenosyn-5 and EHD1 interact and sequentially regulate protein recycling to the plasma membrane.". Mol. Biol. Cell. 15 (5): 2410–22. doi:10.1091/mbc.E03-10-0733. PMC 404033. PMID 15020713.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• de Renzis S, Sönnichsen B, Zerial M (2002). "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes.". Nat. Cell Biol. 4 (2): 124–33. doi:10.1038/ncb744. PMID 11788822.