Biology:RNF40
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
E3 ubiquitin-protein ligase BRE1B is an enzyme that in humans is encoded by the RNF40 gene.[1][2][3][4]
Function
The protein encoded by this gene contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the rat counterpart suggested that this protein may function as an E3 ubiquitin-protein ligase, and facilitate the ubiquitination and degradation of syntaxin 1, which is an essential component of the neurotransmitter release machinery.[4]
Interactions
RNF40 has been shown to interact with STX1A.[3]
References
- ↑ "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169–76. Dec 1998. doi:10.1093/dnares/5.3.169. PMID 9734811.
- ↑ "RBP95, a novel leucine zipper protein, binds to the retinoblastoma protein". Biochem. Biophys. Res. Commun. 275 (1): 141–8. Sep 2000. doi:10.1006/bbrc.2000.3242. PMID 10944455.
- ↑ 3.0 3.1 "Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation". J. Biol. Chem. 277 (38): 35071–9. Sep 2002. doi:10.1074/jbc.M203300200. PMID 12121982.
- ↑ 4.0 4.1 "Entrez Gene: RNF40 ring finger protein 40". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9810.
Further reading
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. 2005. doi:10.1093/dnares/12.2.117. PMID 16303743.
- "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation". Mol. Cell 20 (4): 601–11. 2005. doi:10.1016/j.molcel.2005.09.025. PMID 16307923.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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