Q9UK97 · FBX9_HUMAN
- ProteinF-box only protein 9
- GeneFBXO9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids447 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins and plays a role in several biological processes such as cell cycle, cell proliferation, or maintenance of chromosome stability (PubMed:23263282, PubMed:34480022).
Ubiquitinates mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is the activated due to the relief of feedback inhibition by mTORC1 (PubMed:23263282).
Plays a role in maintaining epithelial cell survival by regulating the turn-over of chromatin modulator PRMT4 through ubiquitination and degradation by the proteasomal pathway (PubMed:34480022).
Regulates also PPARgamma stability by facilitating PPARgamma/PPARG ubiquitination and thereby plays a role in adipocyte differentiation (By similarity).
Ubiquitinates mTORC1-bound TTI1 and TELO2 when they are phosphorylated by CK2 following growth factor deprivation, leading to their degradation. In contrast, does not mediate ubiquitination of TTI1 and TELO2 when they are part of the mTORC2 complex. As a consequence, mTORC1 is inactivated to restrain cell growth and protein translation, while mTORC2 is the activated due to the relief of feedback inhibition by mTORC1 (PubMed:23263282).
Plays a role in maintaining epithelial cell survival by regulating the turn-over of chromatin modulator PRMT4 through ubiquitination and degradation by the proteasomal pathway (PubMed:34480022).
Regulates also PPARgamma stability by facilitating PPARgamma/PPARG ubiquitination and thereby plays a role in adipocyte differentiation (By similarity).
Miscellaneous
Overexpressed in multiple myeloma leading to constitutive activation of the PI3K/mTORC2/Akt pathway to promote survival.
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | SCF ubiquitin ligase complex | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | fat cell differentiation | |
Biological Process | innate immune response | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of TOR signaling | |
Biological Process | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameF-box only protein 9
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UK97
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 426 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000119886 | 1-447 | UniProt | F-box only protein 9 | |||
Sequence: MPDIIWVFPPQAEAEEDCHSDTVRADDDEENESPAETDLQAQLQMFRAQWMFELAPGVSSSNLENRPCRAARGSLQKTSADTKGKQEQAKEEKARELFLKAVEEEQNGALYEAIKFYRRAMQLVPDIEFKITYTRSPDGDGVGNSYIEDNDDDSKMADLLSYFQQQLTFQESVLKLCQPELESSQIHISVLPMEVLMYIFRWVVSSDLDLRSLEQLSLVCRGFYICARDPEIWRLACLKVWGRSCIKLVPYTSWREMFLERPRVRFDGVYISKTTYIRQGEQSLDGFYRAWHQVEYYRYIRFFPDGHVMMLTTPEEPQSIVPRLRTRNTRTDAILLGHYRLSQDTDNQTKVFAVITKKKEEKPLDYKYRYFRRVPVQEADQSFHVGLQLCSSGHQRFNKLIWIHHSCHITYKSTGETAVSAFEIDKMYTPLFFARVRSYTAFSERPL | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 111 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 136 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Interacts with TTI1 and TELO2; when TTI1 and TELO2 are phosphorylated by CK2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UK97 | EEF2 P13639 | 2 | EBI-2869927, EBI-352560 | |
BINARY | Q9UK97 | SKP1 P63208 | 5 | EBI-2869927, EBI-307486 | |
BINARY | Q9UK97 | TELO2 Q9Y4R8 | 5 | EBI-2869927, EBI-1043674 | |
BINARY | Q9UK97 | TTI1 O43156 | 5 | EBI-2869927, EBI-1055680 | |
BINARY | Q9UK97-2 | SKP1 P63208 | 3 | EBI-11023199, EBI-307486 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 9-36 | Disordered | ||||
Sequence: PPQAEAEEDCHSDTVRADDDEENESPAE | ||||||
Repeat | 94-127 | TPR | ||||
Sequence: ARELFLKAVEEEQNGALYEAIKFYRRAMQLVPDI | ||||||
Domain | 185-236 | F-box | ||||
Sequence: QIHISVLPMEVLMYIFRWVVSSDLDLRSLEQLSLVCRGFYICARDPEIWRLA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9UK97-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length447
- Mass (Da)52,329
- Last updated2000-05-01 v1
- Checksum2A88163DAB898D69
Q9UK97-2
- Name2
- Differences from canonical
- 1-11: MPDIIWVFPPQ → M
Q9UK97-3
- Name3
- Differences from canonical
- 1-44: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF176704 EMBL· GenBank· DDBJ | AAF03704.1 EMBL· GenBank· DDBJ | mRNA | ||
AY858798 EMBL· GenBank· DDBJ | AAW51115.1 EMBL· GenBank· DDBJ | mRNA | ||
AL137520 EMBL· GenBank· DDBJ | CAB70786.2 EMBL· GenBank· DDBJ | mRNA | ||
AK021559 EMBL· GenBank· DDBJ | BAG51038.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209833 EMBL· GenBank· DDBJ | BAD93070.1 EMBL· GenBank· DDBJ | mRNA | ||
AL031178 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC000650 EMBL· GenBank· DDBJ | AAH00650.2 EMBL· GenBank· DDBJ | mRNA | ||
AF174597 EMBL· GenBank· DDBJ | AAF04518.1 EMBL· GenBank· DDBJ | mRNA |