RNF40

Protein-coding gene in the species Homo sapiens
RNF40
Identifiers
AliasesRNF40, BRE1B, RBP95, STARING, ring finger protein 40
External IDsOMIM: 607700; MGI: 2142048; HomoloGene: 8856; GeneCards: RNF40; OMA:RNF40 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for RNF40
Genomic location for RNF40
Band16p11.2Start30,761,745 bp[1]
End30,776,307 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for RNF40
Genomic location for RNF40
Band7|7 F3Start127,187,939 bp[2]
End127,203,971 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • left testis

  • right testis

  • ganglionic eminence

  • mucosa of transverse colon

  • islet of Langerhans

  • right lobe of thyroid gland

  • granulocyte

  • sural nerve

  • right hemisphere of cerebellum
Top expressed in
  • granulocyte

  • spermatid

  • spermatocyte

  • neural layer of retina

  • zygote

  • ventricular zone

  • lip

  • muscle of thigh

  • dentate gyrus of hippocampal formation granule cell

  • esophagus
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
SpeciesHumanMouse
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 MbChr 7: 127.19 – 127.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000103549 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. ^ a b "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.


  • v
  • t
  • e