ZFYVE20
Protein-coding gene in the species Homo sapiens
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Aliases | RBSN, Rabenosyn-5, ZFYVE20, rabenosyn, RAB effector | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 609511; MGI: 1925537; HomoloGene: 41477; GeneCards: RBSN; OMA:RBSN - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Rabenosyn-5 is a protein that in humans is encoded by the ZFYVE20 gene.[5][6]
Interactions
ZFYVE20 has been shown to interact with RAB5A.[5]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000131381 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000014550 – 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.
- ^ a b 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.
- ^ "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. S2CID 14294292.
- 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. Bibcode:2005Natur.436..415E. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 6596498.
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PDB gallery
- 1yzm: Structure of Rabenosyn (458-503), Rab4 binding domain
- 1z0j: Structure of GTP-Bound Rab22Q64L GTPase in complex with the minimal Rab binding domain of Rabenosyn-5
- 1z0k: Structure of GTP-Bound Rab4Q67L GTPase in complex with the central Rab binding domain of Rabenosyn-5
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