RNF40

E3 ubiquitin-protein ligase BRE1B is an enzyme that in humans is encoded by the RNF40 gene.[5][6][7][8]

RNF40
Identifiers
Aliases	RNF40, BRE1B, RBP95, STARING, ring finger protein 40
External IDs	OMIM: 607700 MGI: 2142048 HomoloGene: 8856 GeneCards: RNF40
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p11.2 Start 30,761,745 bp[1] End 30,776,307 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 F3 Start 127,588,767 bp[2] End 127,604,799 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • GO:0032403 macromolecular complex binding • ubiquitin conjugating enzyme binding • syntaxin-1 binding • protein homodimerization activity • mRNA 3'-UTR binding • ubiquitin protein ligase binding • GO:0001948 protein binding • ubiquitin-protein transferase activity • transferase activity Cellular component • axon terminus • cytosol • membrane • HULC complex • extrinsic component of membrane • ubiquitin ligase complex • cell nucleus • neuron projection • nucleoplasm • macromolecular complex Biological process • negative regulation of mRNA polyadenylation • histone H2B ubiquitination • positive regulation of proteasomal protein catabolic process • response to peptide hormone • regulation of mitotic cell cycle • positive regulation of protein polyubiquitination • histone monoubiquitination • ubiquitin-dependent protein catabolic process • covalent chromatin modification • positive regulation of histone H2B ubiquitination • protein ubiquitination • chromatin organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9810	233900
Ensembl	ENSG00000103549	ENSMUSG00000030816
UniProt	O75150	Q3U319
RefSeq (mRNA)	NM_001207033 NM_001207034 NM_001286572 NM_014771	NM_172281 NM_001360883
RefSeq (protein)	NP_001193962 NP_001193963 NP_001273501 NP_055586	NP_758485 NP_001347812
Location (UCSC)	Chr 16: 30.76 – 30.78 Mb	Chr 7: 127.59 – 127.6 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[8]

Interactions

RNF40 has been shown to interact with STX1A.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000103549 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030816 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. 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.
8. "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.