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]
End	35,089,319 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	82,871,210 bp[2]
Gene ontology
Molecular function	• p53 binding; • metal ion binding; • protease binding; • GO:0001948 protein binding; • protein kinase binding; • ubiquitin protein ligase binding; • GO:1904264, GO:1904822 ubiquitin protein ligase activity; • transferase activity;
Cellular component	• cytoplasm; • cytosol; • endosome; • membrane; • cell 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
	117584
	67338
	ENSG00000092871
	ENSMUSG00000020696
	Q8WZ73
	Q6ZQM0
	NM_001017368; NM_057178
	NM_001007465; NM_001164569; NM_001164570; NM_001164571; NM_026097
	NP_001017368
	NP_001007466; NP_001158041; NP_001158042; NP_001158043; NP_080373
	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

GRCh38: Ensembl release 89: ENSG00000092871 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000020696 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"Entrez Gene: RFFL ring finger and FYVE-like domain containing 1".

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. 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. 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000092871 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid15229288-5] 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.

[entrez-6] "Entrez Gene: RFFL ring finger and FYVE-like domain containing 1".

RFFL

References

Further reading