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RFFL
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Y02
Identifiers
Aliases	RFFL, CARP-2, CARP2, FRING, RIFIFYLIN, RNF189, RNF34L, ring finger and FYVE-like domain containing E3 ubiquitin protein ligase, ring finger and FYVE like domain containing E3 ubiquitin protein ligase
External IDs	OMIM: 609735; MGI: 1914588; HomoloGene: 12116; GeneCards: RFFL; OMA:RFFL - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q12 Start 35,005,990 bp End 35,089,319 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 C Start 82,693,275 bp End 82,762,036 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve secondary oocyte pancreatic epithelial cell buccal mucosa cell corpus callosum mucosa of ileum spinal cord amniotic fluid subthalamic nucleus C1 segment Top expressed in granulocyte olfactory epithelium zygote secondary oocyte lacrimal gland seminiferous tubule spermatid blood epithelium of stomach primary oocyte More reference expression data BioGPS n/a
Gene ontology Molecular function p53 binding metal ion binding protease binding protein binding protein kinase binding ubiquitin protein ligase binding ubiquitin protein ligase activity transferase activity Cellular component cytoplasm cytosol endosome membrane plasma membrane Golgi membrane tumor necrosis factor receptor superfamily complex recycling endosome membrane lysosome endosome membrane nucleoplasm Biological process regulation of TOR signaling ubiquitin-dependent protein catabolic process negative regulation of tumor necrosis factor-mediated signaling pathway protein K48-linked ubiquitination negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis negative regulation of extrinsic apoptotic signaling pathway via death domain receptors protein ubiquitination negative regulation of signal transduction by p53 class mediator regulation of fibroblast migration proteasome-mediated ubiquitin-dependent protein catabolic process apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 117584 67338 Ensembl ENSG00000092871 ENSMUSG00000020696 UniProt Q8WZ73 Q6ZQM0 RefSeq (mRNA) NM_001017368 NM_057178 NM_001007465 NM_001164569 NM_001164570 NM_001164571 NM_026097 RefSeq (protein) NP_001017368 NP_001007466 NP_001158041 NP_001158042 NP_001158043 NP_080373 Location (UCSC) Chr 17: 35.01 – 35.09 Mb Chr 11: 82.69 – 82.76 Mb PubMed search
Wikidata
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E3 ubiquitin-protein ligase RFFL (Ring Finger And FYVE Like Domain Containing E3 Ubiquitin) is a ubiquitin ligase enzyme that in humans is encoded by the RFFL gene. RFFL associates with endosomes. RFFL is known to affect cardiac repolarization, Cystic fibrosis transmembrane conductance regulator (CFTR) ubiquitination, and mitochondrial clearance by affecting Parkin/PRKN recruitment.

Interactors

• ATXN3
• MDM2
• OPTN
• Parkin
• RAB10
• RNF34
• STUB1
• VCP

See also

• FYVE domain
• RING finger domain

References

1. ^ GRCh38: Ensembl release 89: ENSG00000092871 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020696 – 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. Coumailleau F, Das V, Alcover A, Raposo G, Vandormael-Pournin S, Le Bras S, et al. (October 2004). "Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment". Molecular Biology of the Cell. 15 (10): 4444–4456. doi:10.1091/mbc.E04-04-0274. PMC 519139. PMID 15229288.
6. "Entrez Gene: RFFL ring finger and FYVE-like domain containing 1".
7. ^ Ravindran R, Velikkakath AK, Narendradev ND, Chandrasekharan A, Santhoshkumar TR, Srinivasula SM (December 2022). "Endosomal-associated RFFL facilitates mitochondrial clearance by enhancing PRKN/parkin recruitment to mitochondria". Autophagy. 18 (12): 2851–2864. doi:10.1080/15548627.2022.2052460. PMC 9673925. PMID 35373701.
8. Kabakov AY, Roder K, Bronk P, Turan NN, Dhakal S, Zhong M, et al. (March 2024). "E3 ubiquitin ligase rififylin has yin and yang effects on rabbit cardiac transient outward potassium currents (I_to) and corresponding channel proteins". The Journal of Biological Chemistry. 300 (3): 105759. doi:10.1016/j.jbc.2024.105759. PMC 10945274. PMID 38367666.
9. Okiyoneda T, Veit G, Sakai R, Aki M, Fujihara T, Higashi M, et al. (March 2018). "Chaperone-Independent Peripheral Quality Control of CFTR by RFFL E3 Ligase". Developmental Cell. 44 (6): 694–708.e7. doi:10.1016/j.devcel.2018.02.001. PMC 6447300. PMID 29503157.

Further reading

• Tibbetts MD, Shiozaki EN, Gu L, McDonald ER, El-Deiry WS, Shi Y (December 2004). "Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2". Structure. 12 (12): 2257–2263. doi:10.1016/j.str.2004.10.007. PMID 15576038.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• McDonald ER, El-Deiry WS (April 2004). "Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth". Proceedings of the National Academy of Sciences of the United States of America. 101 (16): 6170–6175. Bibcode:2004PNAS..101.6170M. doi:10.1073/pnas.0307459101. PMC 395941. PMID 15069192.

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