Q62431 · ARI3A_MOUSE
- ProteinAT-rich interactive domain-containing protein 3A
- GeneArid3a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids601 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway.
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 | cytosol | |
Cellular Component | membrane raft | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | DNA binding | |
Molecular Function | identical protein binding | |
Molecular Function | transcription coregulator activity | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAT-rich interactive domain-containing protein 3A
- Short namesARID domain-containing protein 3A
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ62431
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 268 | Impairs DNA-binding. | ||||
Sequence: P → A | ||||||
Mutagenesis | 299 | Impairs DNA-binding. | ||||
Sequence: W → A | ||||||
Mutagenesis | 317 | Impairs DNA-binding. | ||||
Sequence: F → A | ||||||
Mutagenesis | 330 | Impairs DNA-binding. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 457 | No effect on cellular location. | ||||
Sequence: K → A | ||||||
Mutagenesis | 463 | Abolishes nuclear localization. | ||||
Sequence: P → A | ||||||
Mutagenesis | 466 | Abolishes nuclear localization. | ||||
Sequence: K → A | ||||||
Mutagenesis | 467 | Abolishes nuclear localization. | ||||
Sequence: K → A | ||||||
Mutagenesis | 532 | Abolishes cytosolic localization. | ||||
Sequence: G → A | ||||||
Mutagenesis | 535 | Abolishes cytosolic localization. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 535 | No effect on cellular location. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 537 | Abolishes cytosolic localization. | ||||
Sequence: G → A | ||||||
Mutagenesis | 539 | Abolishes cytosolic localization. | ||||
Sequence: L → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 30 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000200579 | 1-601 | AT-rich interactive domain-containing protein 3A | |||
Sequence: MKLQAVMETLIQRQQRARQELEARQAPPPPPPEPTGVRARTTMTDEDREPENARMHRTQMAALAAMRAAAAGLGHPSSPGGSEDGPPISGDEDTAREGTLSSPALHGSVLEGAGHAEGDRHLMDVGSDDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEEGLGPPESASLGTAGLFTRKAPPAQAFRGDGGPRMLSGPERLGPGPAHPSHMASQMPPPDHGDWTFEEQFKQLYELDADPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECERRGLSSPNELQAAIDSNRREGRRQSFGGSLFAYSPSGAHSMLPSPKLPVTPLGLAASTNGSSITPAPKIKKEEDSAIPITVPGRLPVSLAGHPVVAAQAAAVQAAAAQAAVAAQAAALEQLREKLESTEPPEKKMALVADEQQRLMQRAVQQSFLAMTAQLPMNIRINSQASESRQDSAVSLTSANGSNSISMSVEMNGIVYTGVLFAQPPPPTAPSAPGKGGVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP | ||||||
Modified residue | 78 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 89 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 99 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 102 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 127 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 358 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 367 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 403 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 404 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 457 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 467 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
B-cell specific in the adult. Expressed in B-cell progenitors, down-regulated in the immature B-cell stage, and is up-regulated again at later stages of B-lymphocyte differentiation.
Developmental stage
Expressed in lymphocytes from fetal liver. Expressed in fetal thymus and brain.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-224 | Disordered | ||||
Sequence: MKLQAVMETLIQRQQRARQELEARQAPPPPPPEPTGVRARTTMTDEDREPENARMHRTQMAALAAMRAAAAGLGHPSSPGGSEDGPPISGDEDTAREGTLSSPALHGSVLEGAGHAEGDRHLMDVGSDDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEEGLGPPESASLGTAGLFTRKAPPAQAFRGDGGPRMLSGPERLGPGPAHPSHMASQMPPPD | ||||||
Compositional bias | 40-55 | Basic and acidic residues | ||||
Sequence: RTTMTDEDREPENARM | ||||||
Compositional bias | 113-140 | Basic and acidic residues | ||||
Sequence: AGHAEGDRHLMDVGSDDDDTKSKWEEQE | ||||||
Region | 128-165 | Acidic | ||||
Sequence: DDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEE | ||||||
Compositional bias | 141-168 | Acidic residues | ||||
Sequence: LEELGEEEEEEEEEDDFEEEEEEEEGLG | ||||||
Domain | 243-335 | ARID | ||||
Sequence: DPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWREITKGLNLPTSITSAAFTLRTQYMKYLYPYECERR | ||||||
Domain | 449-546 | REKLES | ||||
Sequence: AALEQLREKLESTEPPEKKMALVADEQQRLMQRAVQQSFLAMTAQLPMNIRINSQASESRQDSAVSLTSANGSNSISMSVEMNGIVYTGVLFAQPPPP | ||||||
Region | 450-493 | Important for nuclear localization | ||||
Sequence: ALEQLREKLESTEPPEKKMALVADEQQRLMQRAVQQSFLAMTAQ | ||||||
Region | 495-518 | Homodimerization | ||||
Sequence: PMNIRINSQASESRQDSAVSLTSA | ||||||
Region | 542-562 | Important for cytoplasmic localization | ||||
Sequence: QPPPPTAPSAPGKGGVSSIGT | ||||||
Region | 545-601 | Disordered | ||||
Sequence: PPTAPSAPGKGGVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP | ||||||
Compositional bias | 556-601 | Polar residues | ||||
Sequence: GVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length601
- Mass (Da)64,173
- Last updated1996-11-01 v1
- Checksum66994C01E1FB68CD
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1A7 | A0A0R4J1A7_MOUSE | Arid3a | 599 | ||
D3YVQ2 | D3YVQ2_MOUSE | Arid3a | 108 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 40-55 | Basic and acidic residues | ||||
Sequence: RTTMTDEDREPENARM | ||||||
Compositional bias | 113-140 | Basic and acidic residues | ||||
Sequence: AGHAEGDRHLMDVGSDDDDTKSKWEEQE | ||||||
Compositional bias | 141-168 | Acidic residues | ||||
Sequence: LEELGEEEEEEEEEDDFEEEEEEEEGLG | ||||||
Sequence conflict | 405-406 | in Ref. 3; AAH50925 | ||||
Sequence: Missing | ||||||
Compositional bias | 556-601 | Polar residues | ||||
Sequence: GVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSLP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U60335 EMBL· GenBank· DDBJ | AAB03416.1 EMBL· GenBank· DDBJ | mRNA | ||
AK141283 EMBL· GenBank· DDBJ | BAE24635.1 EMBL· GenBank· DDBJ | mRNA | ||
AK154956 EMBL· GenBank· DDBJ | BAE32951.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050925 EMBL· GenBank· DDBJ | AAH50925.1 EMBL· GenBank· DDBJ | mRNA |