Q8TDN6 · BRX1_HUMAN
- ProteinRibosome biogenesis protein BRX1 homolog
- GeneBRIX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids353 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Required for biogenesis of the 60S ribosomal subunit.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | nucleolus | |
Molecular Function | RNA binding | |
Molecular Function | rRNA binding | |
Biological Process | ribosomal large subunit assembly | |
Biological Process | rRNA processing |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibosome biogenesis protein BRX1 homolog
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8TDN6
- 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 386 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, cross-link, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000120230 | 1-353 | UniProt | Ribosome biogenesis protein BRX1 homolog | |||
Sequence: MAATKRKRRGGFAVQAKKPKRNEIDAEPPAKRHATAEEVEEEERDRIPGPVCKGKWKNKERILIFSSRGINFRTRHLMQDLRMLMPHSKADTKMDRKDKLFVINEVCEMKNCNKCIYFEAKKKQDLYMWLSNSPHGPSAKFLVQNIHTLAELKMTGNCLKGSRPLLSFDPAFDELPHYALLKELLIQIFSTPRYHPKSQPFVDHVFTFTILDNRIWFRNFQIIEEDAALVEIGPRFVLNLIKIFQGSFGGPTLYENPHYQSPNMHRRVIRSITAAKYREKQQVKDVQKLRKKEPKTLLPHDPTADVFVTPAEEKPIEIQWVKPEPKVDLKARKKRIYKRQRKMKQRMDSGKTK | |||||||
Cross-link | 160 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 261 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 276 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 314 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 322 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8TDN6 | EBNA1BP2 Q99848 | 6 | EBI-1052326, EBI-1048111 | |
BINARY | Q8TDN6 | HNRNPU Q00839 | 2 | EBI-1052326, EBI-351126 | |
BINARY | Q8TDN6 | RPL13 P26373 | 3 | EBI-1052326, EBI-356849 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic residues | ||||
Sequence: MAATKRKRRGGFAVQ | ||||||
Region | 1-46 | Disordered | ||||
Sequence: MAATKRKRRGGFAVQAKKPKRNEIDAEPPAKRHATAEEVEEEERDR | ||||||
Compositional bias | 16-46 | Basic and acidic residues | ||||
Sequence: AKKPKRNEIDAEPPAKRHATAEEVEEEERDR | ||||||
Domain | 60-249 | Brix | ||||
Sequence: ERILIFSSRGINFRTRHLMQDLRMLMPHSKADTKMDRKDKLFVINEVCEMKNCNKCIYFEAKKKQDLYMWLSNSPHGPSAKFLVQNIHTLAELKMTGNCLKGSRPLLSFDPAFDELPHYALLKELLIQIFSTPRYHPKSQPFVDHVFTFTILDNRIWFRNFQIIEEDAALVEIGPRFVLNLIKIFQGSFG |
Sequence similarities
Belongs to the BRX1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length353
- Mass (Da)41,401
- Last updated2003-05-09 v2
- ChecksumF05597673A13B7CC
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic residues | ||||
Sequence: MAATKRKRRGGFAVQ | ||||||
Sequence conflict | 11-27 | in Ref. 1; AAL83818 | ||||
Sequence: GFAVQAKKPKRNEIDAE → RLCSSGEEAKKKRNRCG | ||||||
Compositional bias | 16-46 | Basic and acidic residues | ||||
Sequence: AKKPKRNEIDAEPPAKRHATAEEVEEEERDR | ||||||
Sequence conflict | 34 | in Ref. 1; AAL83818 | ||||
Sequence: A → V | ||||||
Sequence conflict | 286 | in Ref. 1; AAL83818 | ||||
Sequence: V → VP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF347667 EMBL· GenBank· DDBJ | AAL83818.1 EMBL· GenBank· DDBJ | mRNA | ||
AY364244 EMBL· GenBank· DDBJ | AAQ76803.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289610 EMBL· GenBank· DDBJ | BAF82299.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471119 EMBL· GenBank· DDBJ | EAW55909.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001546 EMBL· GenBank· DDBJ | AAH01546.2 EMBL· GenBank· DDBJ | mRNA | ||
BC036741 EMBL· GenBank· DDBJ | AAH36741.1 EMBL· GenBank· DDBJ | mRNA |