Q6PCT2 · FXL19_HUMAN
- ProteinF-box/LRR-repeat protein 19
- GeneFBXL19
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids694 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that plays a role in different processes including cell migration, cell proliferation or cytoskeletal reorganization (PubMed:24684802, PubMed:29522376).
Mediates RHOA ubiquitination and degradation in a ERK2-dependent manner (PubMed:23871831).
Induces RAC1 and RAC3 degradation by the proteasome system and thereby regulates TGFB1-induced E-cadherin down-regulation and cell migration (PubMed:23512198, PubMed:24684802).
Mediates also ubiquitination and degradation of IL-33-induced receptor IL1RL1 and subsequently blocks IL-33-mediated apoptosis (By similarity).
Within the nucleus, binds to DNA containing unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides (PubMed:29276034).
Recruits CDK-mediator to chromatin and targets CDK8 to promoters of silent developmental genes leading to induction of these genes during cell differentiation. In addition, plays a critical role in the recruitment of RNF20 to histone H2B leading to H2B mono-ubiquitination (By similarity).
Mediates RHOA ubiquitination and degradation in a ERK2-dependent manner (PubMed:23871831).
Induces RAC1 and RAC3 degradation by the proteasome system and thereby regulates TGFB1-induced E-cadherin down-regulation and cell migration (PubMed:23512198, PubMed:24684802).
Mediates also ubiquitination and degradation of IL-33-induced receptor IL1RL1 and subsequently blocks IL-33-mediated apoptosis (By similarity).
Within the nucleus, binds to DNA containing unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides (PubMed:29276034).
Recruits CDK-mediator to chromatin and targets CDK8 to promoters of silent developmental genes leading to induction of these genes during cell differentiation. In addition, plays a critical role in the recruitment of RNF20 to histone H2B leading to H2B mono-ubiquitination (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 42 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 45 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 50 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 72 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 77 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 88 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 91 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 114 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 117 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 122 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 125 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 145 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 148 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | SCF ubiquitin ligase complex | |
Molecular Function | histone demethylase activity | |
Molecular Function | transcription coregulator activity | |
Molecular Function | ubiquitin-like ligase-substrate adaptor activity | |
Molecular Function | unmethylated CpG binding | |
Molecular Function | zinc ion binding | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameF-box/LRR-repeat protein 19
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PCT2
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 673 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000119868 | 1-694 | UniProt | F-box/LRR-repeat protein 19 | |||
Sequence: MGMKVPGKGESGPSALLTPPMSSSSRGPGAGARRRRTRCRRCRACVRTECGDCHFCRDMKKFGGPGRMKQSCLLRQCTAPVLPHTAVCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRCTQEGRTSKDSGEGPGRRRADNGEEGASLGSGWKLTEEPPLPPPPPRRKGPLPAGPPPEDVPGPPKRKEREAGNEPPTPRKKVKGGRERHLKKVGGDACLLRGSDPGGPGLLPPRVLNPSQAFSSCHPGLPPENWEKPKPPLASAEGPAVPSPSPQREKLERFKRMCQLLERVPDTSSSSSDSDSDSDSSGTSLSEDEAPGEARNGRRPARGSSGEKENRGGRRAVRPGSGGPLLSWPLGPAPPPRPPQLERHVVRPPPRSPEPDTLPLAAGSDHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRMDLSRRKSLTPPMLSGVVRRQPRALDLSWTGVSKKQLMWLLNRLQGLQELVLSGCSWLSVSALGSAPLPALRLLDLRWIEDVKDSQLRELLLPPPDTKPGQTESRGRLQGVAELRLAGLELTDASLRLLLRHAPQLSALDLSHCAHVGDPSVHLLTAPTSPLRETLVHLNLAGCHRLTDHCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 299 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 413 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Acetylated by CREBBP; leading to ubiquitination and subsequent proteasomal degradation.
Ubiquitinated; leading to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Directly interacts with SKP1 and CUL1. Interacts with RNF20.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q6PCT2 | Il1rl1 P14719 | 3 | EBI-6664563, EBI-525078 | |
BINARY | Q6PCT2-2 | ABI1 Q8IZP0-5 | 3 | EBI-11959077, EBI-11743294 | |
BINARY | Q6PCT2-2 | ABI2 Q9NYB9-2 | 3 | EBI-11959077, EBI-11096309 | |
BINARY | Q6PCT2-2 | DGAT2L6 Q6ZPD8 | 3 | EBI-11959077, EBI-12831978 | |
BINARY | Q6PCT2-2 | EFHC2 Q5JST6 | 3 | EBI-11959077, EBI-2349927 | |
BINARY | Q6PCT2-2 | NCK2 O43639 | 3 | EBI-11959077, EBI-713635 | |
BINARY | Q6PCT2-2 | PSME3 P61289 | 3 | EBI-11959077, EBI-355546 | |
BINARY | Q6PCT2-2 | RPRM Q9NS64 | 3 | EBI-11959077, EBI-1052363 | |
BINARY | Q6PCT2-2 | SORBS3 O60504 | 3 | EBI-11959077, EBI-741237 | |
BINARY | Q6PCT2-2 | TMEM239 Q8WW34-2 | 3 | EBI-11959077, EBI-11528917 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger, compositional bias, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MGMKVPGKGESGPSALLTPPMSSSSRGPGAGA | ||||||
Zinc finger | 32-78 | CXXC-type | ||||
Sequence: ARRRRTRCRRCRACVRTECGDCHFCRDMKKFGGPGRMKQSCLLRQCT | ||||||
Zinc finger | 85-151 | PHD-type | ||||
Sequence: TAVCLLCGEAGKEDTVEGEEEKFGLSLMECTICNEIVHPGCLKMGKAEGVINAEIPNCWECPRCTQE | ||||||
Compositional bias | 150-171 | Basic and acidic residues | ||||
Sequence: QEGRTSKDSGEGPGRRRADNGE | ||||||
Region | 150-420 | Disordered | ||||
Sequence: QEGRTSKDSGEGPGRRRADNGEEGASLGSGWKLTEEPPLPPPPPRRKGPLPAGPPPEDVPGPPKRKEREAGNEPPTPRKKVKGGRERHLKKVGGDACLLRGSDPGGPGLLPPRVLNPSQAFSSCHPGLPPENWEKPKPPLASAEGPAVPSPSPQREKLERFKRMCQLLERVPDTSSSSSDSDSDSDSSGTSLSEDEAPGEARNGRRPARGSSGEKENRGGRRAVRPGSGGPLLSWPLGPAPPPRPPQLERHVVRPPPRSPEPDTLPLAAGS | ||||||
Compositional bias | 184-208 | Pro residues | ||||
Sequence: EEPPLPPPPPRRKGPLPAGPPPEDV | ||||||
Compositional bias | 209-229 | Basic and acidic residues | ||||
Sequence: PGPPKRKEREAGNEPPTPRKK | ||||||
Compositional bias | 280-295 | Pro residues | ||||
Sequence: ENWEKPKPPLASAEGP | ||||||
Compositional bias | 319-343 | Polar residues | ||||
Sequence: RVPDTSSSSSDSDSDSDSSGTSLSE | ||||||
Compositional bias | 347-371 | Basic and acidic residues | ||||
Sequence: PGEARNGRRPARGSSGEKENRGGRR | ||||||
Compositional bias | 384-412 | Pro residues | ||||
Sequence: WPLGPAPPPRPPQLERHVVRPPPRSPEPD | ||||||
Domain | 418-464 | F-box | ||||
Sequence: AGSDHPLPRAAWLRVFQHLGPRELCICMRVCRTWSRWCYDKRLWPRM | ||||||
Repeat | 492-517 | LRR 1 | ||||
Sequence: WTGVSKKQLMWLLNRLQGLQELVLSG | ||||||
Repeat | 518-541 | LRR 2 | ||||
Sequence: CSWLSVSALGSAPLPALRLLDLRW | ||||||
Repeat | 581-606 | LRR 3 | ||||
Sequence: GLELTDASLRLLLRHAPQLSALDLSH | ||||||
Repeat | 607-636 | LRR 4 | ||||
Sequence: CAHVGDPSVHLLTAPTSPLRETLVHLNLAG | ||||||
Repeat | 637-661 | LRR 5 | ||||
Sequence: CHRLTDHCLPLFRRCPRLRRLDLRS | ||||||
Repeat | 662-694 | LRR 6 | ||||
Sequence: CRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS |
Domain
The CXXC zinc finger mediates binding to DNA containing unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6PCT2-1
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
- Length694
- Mass (Da)75,707
- Last updated2011-02-08 v3
- Checksum8D8A3BC4C86AD396
Q6PCT2-2
- Name2
- Differences from canonical
- 241-283: Missing
Q6PCT2-3
- Name3
- Differences from canonical
- 643-694: HCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS → PAGLGPWAPGLYNTVCYKTQNLP
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 150-171 | Basic and acidic residues | ||||
Sequence: QEGRTSKDSGEGPGRRRADNGE | ||||||
Compositional bias | 184-208 | Pro residues | ||||
Sequence: EEPPLPPPPPRRKGPLPAGPPPEDV | ||||||
Compositional bias | 209-229 | Basic and acidic residues | ||||
Sequence: PGPPKRKEREAGNEPPTPRKK | ||||||
Alternative sequence | VSP_013015 | 241-283 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 280-295 | Pro residues | ||||
Sequence: ENWEKPKPPLASAEGP | ||||||
Compositional bias | 319-343 | Polar residues | ||||
Sequence: RVPDTSSSSSDSDSDSDSSGTSLSE | ||||||
Compositional bias | 347-371 | Basic and acidic residues | ||||
Sequence: PGEARNGRRPARGSSGEKENRGGRR | ||||||
Compositional bias | 384-412 | Pro residues | ||||
Sequence: WPLGPAPPPRPPQLERHVVRPPPRSPEPD | ||||||
Alternative sequence | VSP_040503 | 643-694 | in isoform 3 | |||
Sequence: HCLPLFRRCPRLRRLDLRSCRQLSPEACARLAAAGPPGPFRCPEEKLLLKDS → PAGLGPWAPGLYNTVCYKTQNLP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC135048 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC059173 EMBL· GenBank· DDBJ | AAH59173.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK098777 EMBL· GenBank· DDBJ | BAC05410.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL137589 EMBL· GenBank· DDBJ | CAB70830.1 EMBL· GenBank· DDBJ | mRNA |