FBXO7

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
4L9C, 4L9H

Identifiers

Aliases

FBXO7, FBX, FBX07, FBX7, PARK15, PKPS, F-box protein 7

External IDs

MGI: 1917004 HomoloGene: 8136 GeneCards: FBXO7

Gene ontology
Molecular function	• protein binding • protein kinase binding • ubiquitin-protein transferase activity
Cellular component	• cytoplasm • ubiquitin ligase complex • protein complex • cytosol • mitochondrion • nucleus
Biological process	• negative regulation of G1/S transition of mitotic cell cycle • protein targeting to mitochondrion • negative regulation of lymphocyte differentiation • mitophagy • regulation of protein stability • protein ubiquitination • ubiquitin-dependent protein catabolic process • negative regulation of cyclin-dependent protein serine/threonine kinase activity • positive regulation of mitophagy • regulation of locomotion
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


25793


69754

Ensembl


ENSG00000100225


ENSMUSG00000001786

UniProt


Q9Y3I1


Q3U7U3

RefSeq (mRNA)


NM_001033024 NM_001257990 NM_012179


NM_153195 NM_001310745

RefSeq (protein)


NP_001028196.1 NP_001244919.1 NP_036311.3


NP_694875.2

Location (UCSC)

Chr 22: 32.47 – 32.5 Mb

Chr 10: 86.02 – 86.05 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

F-box only protein 7 is a protein that in humans is encoded by the FBXO7 gene.^[3]^[4]^[5]^[6]

Function

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 it may play a role in regulation of hematopoiesis. Alternatively spliced transcript variants of this gene have been identified with the full-length natures of only some variants being determined.^[6]

Interactions

FBXO7 has been shown to interact with SKP1A^[7] and CUL1.^[3]^[8]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (December 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.
↑ Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW (December 1999). "A family of mammalian F-box proteins". Curr Biol. 9 (20): 1180–2. doi:10.1016/S0960-9822(00)80021-4. PMID 10531037.
↑ Di Fonzo A, Dekker MC, Montagna P, Baruzzi A, Yonova EH, Correia Guedes L, Szczerbinska A, Zhao T, Dubbel-Hulsman LO, Wouters CH, de Graaff E, Oyen WJ, Simons EJ, Breedveld GJ, Oostra BA, Horstink MW, Bonifati V (January 2009). "FBXO7 mutations cause autosomal recessive, early-onset parkinsonian-pyramidal syndrome". Neurology. 72 (3): 240–5. doi:10.1212/01.wnl.0000338144.10967.2b. PMID 19038853.
1 2 "Entrez Gene: FBXO7 F-box protein 7".
↑ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (October 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.
↑ Kirk R, Laman H, Knowles PP, Murray-Rust J, Lomonosov M, Meziane el K, McDonald NQ (August 2008). "Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor". J. Biol. Chem. 283 (32): 22325–35. doi:10.1074/jbc.M709900200. PMID 18495667.

Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (1999). "The DNA sequence of human chromosome 22.". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Dias Neto E, Correa RG, Verjovski-Almeida S, Briones MR, Nagai MA, da Silva W, Zago MA, Bordin S, Costa FF, Goldman GH, Carvalho AF, Matsukuma A, Baia GS, Simpson DH, Brunstein A, de Oliveira PS, Bucher P, Jongeneel CV, O'Hare MJ, Soares F, Brentani RR, Reis LF, de Souza SJ, Simpson AJ (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
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.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Tsou AP, Yang CW, Huang CY, Yu RC, Lee YC, Chang CW, Chen BR, Chung YF, Fann MJ, Chi CW, Chiu JH, Chou CK (2003). "Identification of a novel cell cycle regulated gene, HURP, overexpressed in human hepatocellular carcinoma.". Oncogene. 22 (2): 298–307. doi:10.1038/sj.onc.1206129. PMID 12527899.
Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I (2003). "Reevaluating human gene annotation: a second-generation analysis of chromosome 22.". Genome Res. 13 (1): 27–36. doi:10.1101/gr.695703. PMC 430954. PMID 12529303.
Hsu JM, Lee YC, Yu CT, Huang CY (2004). "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.". J. Biol. Chem. 279 (31): 32592–602. doi:10.1074/jbc.M404950200. PMID 15145941.
Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
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. doi:10.1038/nature04209. PMID 16189514.
Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
Chang YF, Cheng CM, Chang LK, Jong YJ, Yuo CY (2006). "The F-box protein Fbxo7 interacts with human inhibitor of apoptosis protein cIAP1 and promotes cIAP1 ubiquitination.". Biochem. Biophys. Res. Commun. 342 (4): 1022–6. doi:10.1016/j.bbrc.2006.02.061. PMID 16510124.
Liu Y, Hedvat CV, Mao S, Zhu XH, Yao J, Nguyen H, Koff A, Nimer SD (2006). "The ETS protein MEF is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2.". Mol. Cell. Biol. 26 (8): 3114–23. doi:10.1128/MCB.26.8.3114-3123.2006. PMC 1446966. PMID 16581786.

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FBXO7

Function

Interactions

References

Further reading