O35126 · ATN1_MOUSE
- ProteinAtrophin-1
- GeneAtn1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1175 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity).
Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation
Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation
Miscellaneous
A mouse model of DRPLA with 129 CAG repeats (Q129) exhibits severe neurological defects similar to those of juvenile-onset DRPLA patients including age-dependent and region-specific presynaptic dysfunction in the globus pallidus and cerebellum. Progressive shrinkage of distal dendrites of Purkinje cells and decreased currents through alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid and gamma-aminobutyrate type A receptors in CA1 neurons is observed. There is progressive brain atrophy.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 109-110 | Cleavage | ||||
Sequence: DG |
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 | anchoring junction | |
Cellular Component | cell leading edge | |
Cellular Component | cytoplasm | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | JUN kinase binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | transcription coactivator activity | |
Molecular Function | transcription corepressor activity | |
Biological Process | cell killing | |
Biological Process | cell migration | |
Biological Process | determination of adult lifespan | |
Biological Process | maintenance of cell polarity | |
Biological Process | male gonad development | |
Biological Process | multicellular organism growth | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | neuron apoptotic process | |
Biological Process | post-embryonic development | |
Biological Process | regulation of neuron differentiation | |
Biological Process | response to food | |
Biological Process | spermatogenesis |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAtrophin-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO35126
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000356253 | 1-1175 | Atrophin-1 | |||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL | ||||||
Modified residue | 34 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 77 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 79 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 101 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 103 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 107 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 617 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 626 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 638 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 646 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 654 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 724 | Phosphoserine; by MAPK8 | ||||
Sequence: S | ||||||
Modified residue | 731 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 733 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 881 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1100 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Cross-link | 1168 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Phosphorylated in vitro by MAPK8/JNK1 on Ser-724.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Most abundant in the brain.
Induction
In vascular smooth muscle, induced by angiotensin II, FGF; PGF and IL1B.
Developmental stage
Expressed as early as 5 days and thereafter shows little variation throughout 17 days.
Gene expression databases
Interaction
Subunit
Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the interaction enhances transcriptional repression of MTG8. Interacts with PQBP1 (By similarity).
Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts with FAT1 (via a C-terminal domain)
Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts with FAT1 (via a C-terminal domain)
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-31 | Basic and acidic residues | ||||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRG | ||||||
Region | 1-595 | Disordered | ||||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTS | ||||||
Motif | 16-32 | Nuclear localization signal | ||||
Sequence: RKKEAPGPREELRSRGR | ||||||
Compositional bias | 48-95 | Basic and acidic residues | ||||
Sequence: EKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQE | ||||||
Compositional bias | 109-127 | Basic and acidic residues | ||||
Sequence: DGRSINDDGSSDPRDIDQD | ||||||
Compositional bias | 128-154 | Polar residues | ||||
Sequence: NRSTSPSIYSPGSVENDSDSSSGLSQG | ||||||
Compositional bias | 156-218 | Pro residues | ||||
Sequence: ARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHP | ||||||
Compositional bias | 274-313 | Pro residues | ||||
Sequence: PAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLN | ||||||
Compositional bias | 349-370 | Pro residues | ||||
Sequence: EKGPTLAPSPHPLPPASSSAPG | ||||||
Compositional bias | 372-404 | Polar residues | ||||
Sequence: PMRYPYSSSSSSAAASSSSSSSSASQYPASQAL | ||||||
Compositional bias | 413-435 | Polar residues | ||||
Sequence: PPTSMSVSNQPPKYTQPSLPSQA | ||||||
Compositional bias | 457-492 | Polar residues | ||||
Sequence: HPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGN | ||||||
Region | 503-553 | Involved in binding BAIAP2 | ||||
Sequence: HPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPP | ||||||
Compositional bias | 543-582 | Polar residues | ||||
Sequence: SYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGA | ||||||
Region | 608-752 | Disordered | ||||
Sequence: SSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFN | ||||||
Compositional bias | 668-703 | Pro residues | ||||
Sequence: GTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTG | ||||||
Compositional bias | 720-739 | Pro residues | ||||
Sequence: EPPESPVPPARSPSPPPKVV | ||||||
Region | 770-847 | Disordered | ||||
Sequence: VPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPP | ||||||
Compositional bias | 776-828 | Basic and acidic residues | ||||
Sequence: KLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQ | ||||||
Region | 864-879 | Required for interaction with FAT1 | ||||
Sequence: DTPALRTLSEYARPHV | ||||||
Region | 913-932 | Disordered | ||||
Sequence: PAAREREREARERDLRDRLK | ||||||
Motif | 1018-1026 | Nuclear export signal | ||||
Sequence: ALGNDPLAR |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,175
- Mass (Da)123,724
- Last updated1998-01-01 v1
- Checksum8BEFFAB75DDC0F36
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YYE6 | D3YYE6_MOUSE | Atn1 | 183 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-31 | Basic and acidic residues | ||||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRG | ||||||
Compositional bias | 48-95 | Basic and acidic residues | ||||
Sequence: EKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQE | ||||||
Compositional bias | 109-127 | Basic and acidic residues | ||||
Sequence: DGRSINDDGSSDPRDIDQD | ||||||
Compositional bias | 128-154 | Polar residues | ||||
Sequence: NRSTSPSIYSPGSVENDSDSSSGLSQG | ||||||
Compositional bias | 156-218 | Pro residues | ||||
Sequence: ARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHP | ||||||
Compositional bias | 274-313 | Pro residues | ||||
Sequence: PAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLN | ||||||
Compositional bias | 349-370 | Pro residues | ||||
Sequence: EKGPTLAPSPHPLPPASSSAPG | ||||||
Compositional bias | 372-404 | Polar residues | ||||
Sequence: PMRYPYSSSSSSAAASSSSSSSSASQYPASQAL | ||||||
Compositional bias | 413-435 | Polar residues | ||||
Sequence: PPTSMSVSNQPPKYTQPSLPSQA | ||||||
Sequence conflict | 452 | in Ref. 1; BAA13450 | ||||
Sequence: A → G | ||||||
Compositional bias | 457-492 | Polar residues | ||||
Sequence: HPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGN | ||||||
Sequence conflict | 495 | in Ref. 1; BAA13450 | ||||
Sequence: P → A | ||||||
Sequence conflict | 532 | in Ref. 1; BAA13450 | ||||
Sequence: P → A | ||||||
Compositional bias | 543-582 | Polar residues | ||||
Sequence: SYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGA | ||||||
Compositional bias | 668-703 | Pro residues | ||||
Sequence: GTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTG | ||||||
Sequence conflict | 691 | in Ref. 1; BAA13450 | ||||
Sequence: S → L | ||||||
Compositional bias | 720-739 | Pro residues | ||||
Sequence: EPPESPVPPARSPSPPPKVV | ||||||
Sequence conflict | 734 | in Ref. 1; BAA13450 | ||||
Sequence: P → A | ||||||
Sequence conflict | 766 | in Ref. 1; BAA13450 | ||||
Sequence: D → T | ||||||
Compositional bias | 776-828 | Basic and acidic residues | ||||
Sequence: KLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQ | ||||||
Sequence conflict | 926 | in Ref. 1; BAA13450 | ||||
Sequence: D → N |
Polymorphism
The poly-Gln region of Atn1 is polymorphic (3 to 8 repeats).
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D87744 EMBL· GenBank· DDBJ | BAA13450.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002397 EMBL· GenBank· DDBJ | AAC36003.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466523 EMBL· GenBank· DDBJ | EDK99754.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466523 EMBL· GenBank· DDBJ | EDK99755.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC050920 EMBL· GenBank· DDBJ | AAH50920.2 EMBL· GenBank· DDBJ | mRNA | ||
BC053051 EMBL· GenBank· DDBJ | AAH53051.1 EMBL· GenBank· DDBJ | mRNA |