RNF40

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 127,187,939 bp [2] End 127,203,971 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence islet of Langerhans right lobe of thyroid gland sural nerve left lobe of thyroid gland left uterine tube monocyte canal of the cervix anterior pituitary Left adrenal gland Top expressed in spermatid spermatocyte lip esophagus thymus seminiferous tubule superior frontal gyrus yolk sac triceps brachii muscle temporal muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding protein-containing complex binding ubiquitin conjugating enzyme binding syntaxin-1 binding protein homodimerization activity mRNA 3'-UTR binding ubiquitin protein ligase binding protein binding ubiquitin-protein transferase activity transferase activity Cellular component axon terminus cytosol membrane HULC complex extrinsic component of membrane ubiquitin ligase complex nucleus neuron projection nucleoplasm protein-containing 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 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_194352 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: 127.19 – 127.2 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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. S2CID   7827573.