FBXO6

From Wikipedia, the free encyclopedia

F-box protein 6

Identifiers

FBXO6; FBG2; FBS2; FBX6; Fbx6b

External IDs

OMIM: 605647 MGI: 1354743 HomoloGene: 9274

Gene ontology
Molecular Function:	• glycoprotein binding • ubiquitin-protein ligase activity • carbohydrate binding
Biological Process:	• proteolysis • ubiquitin cycle • glycoprotein catabolic process • protein catabolic process • ER-associated protein catabolic process

Orthologs

Human

Mouse

Refseq

NM_018438 (mRNA)
NP_060908 (protein)

NM_015797 (mRNA)
NP_056612 (protein)

Location

Chr 1: 11.65 - 11.66 Mb

Chr 4: 146.99 - 147 Mb

Pubmed search

[1]

[2]

F-box protein 6, also known as FBXO6, is a human gene.^[1]

This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class, and its C-terminal region is highly similar to that of rat NFB42 (neural F Box 42 kDa) which may be involved in the control of the cell cycle.^[1]

[edit] References

^ ^a ^b Entrez Gene: FBXO6 F-box protein 6.

[edit] Further reading

Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. doi:10.1038/nature04727. PMID 16710414.
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. PMID 15489334.
Yoshida Y, Tokunaga F, Chiba T, et al. (2003). "Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains.". J. Biol. Chem. 278 (44): 43877-84. doi:10.1074/jbc.M304157200. PMID 12939278.
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. PMID 12477932.
Ilyin GP, Sérandour AL, Pigeon C, et al. (2003). "A new subfamily of structurally related human F-box proteins.". Gene 296 (1-2): 11-20. PMID 12383498.
Ilyin GP, Rialland M, Pigeon C, Guguen-Guillouzo C (2001). "cDNA cloning and expression analysis of new members of the mammalian F-box protein family.". Genomics 67 (1): 40-7. doi:10.1006/geno.2000.6211. PMID 10945468.
Winston JT, Koepp DM, Zhu C, et al. (1999). "A family of mammalian F-box proteins.". Curr. Biol. 9 (20): 1180-2. doi:10.1016/S0960-9822(00)80021-4. PMID 10531037.
Cenciarelli C, Chiaur DS, Guardavaccaro D, et al. (1999). "Identification of a family of human F-box proteins.". Curr. Biol. 9 (20): 1177-9. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.