RNF40

Ring finger protein 40, E3 ubiquitin protein ligase
Identifiers
Symbols	RNF40 ; BRE1B; RBP95; STARING
External IDs	OMIM: 607700 MGI: 2142048 HomoloGene: 8856 GeneCards: RNF40 Gene
EC number	6.3.2.-
Gene ontology Molecular function • mRNA 3'-UTR binding • ubiquitin-protein transferase activity • protein binding • zinc ion binding • ligase activity • syntaxin-1 binding • ubiquitin conjugating enzyme binding • ubiquitin protein ligase binding • protein complex binding • protein homodimerization activity Cellular component • ubiquitin ligase complex • nucleus • nucleoplasm • cytosol • membrane • extrinsic component of membrane • HULC complex • neuron projection • axon terminus Biological process • ubiquitin-dependent protein catabolic process • regulation of mitotic cell cycle • histone monoubiquitination • histone H2B ubiquitination • response to peptide hormone • negative regulation of mRNA polyadenylation • positive regulation of proteasomal protein catabolic process • positive regulation of protein polyubiquitination • positive regulation of histone H2B ubiquitination Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9810	233900
Ensembl	ENSG00000103549	ENSMUSG00000030816
UniProt	O75150	Q3U319
RefSeq (mRNA)	NM_001207033	NM_172281
RefSeq (protein)	NP_001193962	NP_758485
Location (UCSC)	Chr 16: 30.76 – 30.78 Mb	Chr 7: 127.59 – 127.6 Mb
PubMed search

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

1. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "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. doi:10.1093/dnares/5.3.169. PMID 9734811.
2. Wen H, Ao S (Sep 2000). "RBP95, a novel leucine zipper protein, binds to the retinoblastoma protein". Biochem. Biophys. Res. Commun. 275 (1): 141–8. doi:10.1006/bbrc.2000.3242. PMID 10944455.
3. Chin LS, Vavalle JP, Li L (Sep 2002). "Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation". J. Biol. Chem. 277 (38): 35071–9. doi:10.1074/jbc.M203300200. PMID 12121982.
4. "Entrez Gene: RNF40 ring finger protein 40".

Further reading

• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T (2005). "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. doi:10.1093/dnares/12.2.117. PMID 16303743.
• Zhu B, Zheng Y, Pham AD, Mandal SS, Erdjument-Bromage H, Tempst P, Reinberg D (2005). "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation". Mol. Cell 20 (4): 601–11. doi:10.1016/j.molcel.2005.09.025. PMID 16307923.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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.