RFFL

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
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q12 Start 35,005,990 bp [1] End 35,089,319 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11|11 C Start 82,693,275 bp [2] End 82,762,036 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve secondary oocyte pancreatic epithelial cell corpus callosum spinal cord amniotic fluid subthalamic nucleus medulla oblongata internal globus pallidus bone marrow cells Top expressed in olfactory epithelium secondary oocyte lacrimal gland seminiferous tubule spermatid blood Epithelium of stomach medial ganglionic eminence ascending aorta morula 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

E3 ubiquitin-protein ligase rififylin is an enzyme that in humans is encoded by the RFFL gene. ^{[5] [6]}

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, Baldacci P, Dautry-Varsat A, Babinet C, Cohen-Tannoudji M (Sep 2004). "Over-Expression of Rififylin, a New RING Finger and FYVE-like Domain-containing Protein, Inhibits Recycling from the Endocytic Recycling Compartment". Mol Biol Cell. 15 (10): 4444–56. doi:10.1091/mbc.E04-04-0274. PMC   519139 . PMID   15229288.
6. "Entrez Gene: RFFL ring finger and FYVE-like domain containing 1".

Further reading

• Tibbetts MD, Shiozaki EN, Gu L, et al. (2005). "Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2". Structure. 12 (12): 2257–63. doi: 10.1016/j.str.2004.10.007 . PMID   15576038.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . PMID   15302935.
• McDonald ER, El-Deiry WS (2004). "Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 6170–5. Bibcode:2004PNAS..101.6170M. doi: 10.1073/pnas.0307459101 . PMC   395941 . PMID   15069192.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.