A0A494C142 · A0A494C142_HUMAN
- ProteinBRCA1 associated RING domain 1
- GeneBARD1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids432 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score1/5
Function
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 | |
---|---|---|
Molecular Function | metal ion binding |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A494C142
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,079 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 134 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 247 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 315 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-53 | BARD1 Zinc finger RING-type | ||||
Sequence: TNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMI | ||||||
Compositional bias | 116-131 | Polar residues | ||||
Sequence: AIKKDASAQQDSYEFV | ||||||
Region | 116-156 | Disordered | ||||
Sequence: AIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKK | ||||||
Region | 304-348 | Disordered | ||||
Sequence: NIPLPECSSPPSCKRKVGGTSGRKNSNMSDEFISLSPGTPPSTLS | ||||||
Compositional bias | 322-348 | Polar residues | ||||
Sequence: GTSGRKNSNMSDEFISLSPGTPPSTLS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length432
- Mass (Da)47,758
- Last updated2019-06-05 v1
- Checksum12623C84CEBAF655
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q99728 | BARD1_HUMAN | BARD1 | 777 | ||
C9IYG1 | C9IYG1_HUMAN | BARD1 | 326 | ||
C9J6M1 | C9J6M1_HUMAN | BARD1 | 44 | ||
F6MDI1 | F6MDI1_HUMAN | BARD1 | 307 | ||
F8WCG2 | F8WCG2_HUMAN | BARD1 | 76 | ||
A0A087X0C6 | A0A087X0C6_HUMAN | BARD1 | 63 | ||
A0A087X2H0 | A0A087X2H0_HUMAN | BARD1 | 641 | ||
A0A087WZ19 | A0A087WZ19_HUMAN | BARD1 | 264 |
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: X | ||||||
Compositional bias | 116-131 | Polar residues | ||||
Sequence: AIKKDASAQQDSYEFV | ||||||
Compositional bias | 322-348 | Polar residues | ||||
Sequence: GTSGRKNSNMSDEFISLSPGTPPSTLS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC016708 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |