P54259 · ATN1_HUMAN
- ProteinAtrophin-1
- GeneATN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1190 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional corepressor. Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation (By similarity).
Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats
Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of poly-Gln (polyQ) repeats
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 109-110 | Cleavage; by CASP-3 | ||||
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 | cytoplasm | |
Cellular Component | nuclear matrix | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
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 | central nervous system development | |
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 | response to food | |
Biological Process | spermatogenesis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAtrophin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP54259
- 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 (By similarity).
Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Gln (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles
Colocalizes with MTG8 in discrete nuclear dots. Proteolytic fragment F1 appears to remain in nucleus. Fragment F2 is exported into the cytoplasm. Fragment F2 from mutant sequences with longer poly-Gln (polyQ) tracts are additionally located to the cytoplasmic membrane and to certain organelles
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Dentatorubral-pallidoluysian atrophy (DRPLA)
- Note
- DescriptionAutosomal dominant neurodegenerative disorder characterized by a loss of neurons in the dentate nucleus, rubrum, glogus pallidus and Luys'body. Clinical features are myoclonus epilepsy, dementia, and cerebellar ataxia. Onset of the disease occurs usually in the second decade of life and death in the fourth.
- See alsoMIM:125370
Congenital hypotonia, epilepsy, developmental delay, and digital anomalies (CHEDDA)
- Note
- DescriptionAn autosomal dominant neurodevelopmental syndrome characterized by severe global developmental delay, impaired intellectual development, poor or absent language, significant motor disability with inability to walk, dysmorphic facial features, skeletal anomalies, and variable congenital malformations. Most patients also have seizures and structural brain abnormalities.
- See alsoMIM:618494
Natural variants in CHEDDA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083058 | 1054 | H>N | in CHEDDA | |
VAR_083059 | 1058 | H>Y | in CHEDDA | |
VAR_083060 | 1059-1060 | SH>DL | in CHEDDA; uncertain significance | |
VAR_083061 | 1059-1060 | SH>NL | in CHEDDA; uncertain significance | |
VAR_083062 | 1060 | H>Y | in CHEDDA; the mutation resulted in a perturbation of the structural and functional integrity of the HX repeat; altered zinc-binding properties of the HX repeat | |
VAR_083063 | 1062 | H>D | in CHEDDA | |
VAR_083064 | 1062 | H>R | in CHEDDA | |
VAR_083065 | 1063 | L>R | in CHEDDA |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 109 | Prevents cleavage and suppresses apoptosis. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_030937 | 339 | in dbSNP:rs1058045 | |||
Sequence: M → I | ||||||
Natural variant | VAR_064038 | 484-488 | ||||
Sequence: Missing | ||||||
Mutagenesis | 739 | Abolishes phosphorylation. | ||||
Sequence: S → A | ||||||
Natural variant | VAR_083058 | 1054 | in CHEDDA | |||
Sequence: H → N | ||||||
Natural variant | VAR_083059 | 1058 | in CHEDDA | |||
Sequence: H → Y | ||||||
Natural variant | VAR_083060 | 1059-1060 | in CHEDDA; uncertain significance | |||
Sequence: SH → DL | ||||||
Natural variant | VAR_083061 | 1059-1060 | in CHEDDA; uncertain significance | |||
Sequence: SH → NL | ||||||
Natural variant | VAR_083062 | 1060 | in CHEDDA; the mutation resulted in a perturbation of the structural and functional integrity of the HX repeat; altered zinc-binding properties of the HX repeat | |||
Sequence: H → Y | ||||||
Natural variant | VAR_083063 | 1062 | in CHEDDA | |||
Sequence: H → D | ||||||
Natural variant | VAR_083064 | 1062 | in CHEDDA | |||
Sequence: H → R | ||||||
Natural variant | VAR_083065 | 1063 | in CHEDDA | |||
Sequence: L → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,561 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000064730 | 1-1190 | UniProt | Atrophin-1 | |||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVTTSSATLSTVIATVASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL | |||||||
Modified residue | 34 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 77 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 77 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 79 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 81 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 101 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 103 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 168 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 632 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 632 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 641 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 645 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 653 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 653 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 661 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 661 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 664 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 669 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 669 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 677 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 739 | UniProt | Phosphoserine; by MAPK8 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 739 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 746 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 746 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 748 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 896 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 896 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1115 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Cross-link | 1183 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Phosphorylated in vitro by MAPK8/JNK1 on Ser-739. Mutant ATN1 sequences with expanded poly-Gln (polyQ) traits are more slowly phosphorylated.
Proteolytically cleaved, probably in the nucleus, to produce two C-terminal fragments of 140 kDa (F1) and 125 kDa (F2) each containing poly-Gln (polyQ) tracts. F2 is produced by cleavage by caspases and is exported into the cytoplasm. In vitro, cleavage increases with an increase in the number of polyQ tracts. C-terminal proteolytic products appear to be the cause of cell toxicity. In vitro cleavage at Asp-109.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed in various tissues including heart, lung, kidney, ovary, testis, prostate, placenta, skeletal Low levels in the liver, thymus and leukocytes. In the adult brain, broadly expressed in amygdala, caudate nucleus, corpus callosum, hippocampus, hypothalamus, substantia nigra, subthalamic nucleus, and thalamus. High levels in fetal tissues, especially brain.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts (via its N-terminus) with FAT1 (via a C-terminal domain) (By similarity).
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
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
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P54259 | EFEMP1 Q12805 | 3 | EBI-945980, EBI-536772 | |
BINARY | P54259 | EFEMP2 O95967 | 3 | EBI-945980, EBI-743414 | |
BINARY | P54259 | PLEKHA5 Q9HAU0 | 2 | EBI-945980, EBI-945934 | |
BINARY | P54259 | PSME3 P61289 | 3 | EBI-945980, EBI-355546 | |
BINARY | P54259 | RBFOX1 Q9NWB1 | 2 | EBI-945980, EBI-945906 | |
BINARY | P54259 | RERE Q9P2R6 | 3 | EBI-945980, EBI-948076 | |
BINARY | P54259 | TRIP6 Q15654 | 2 | EBI-945980, EBI-742327 | |
BINARY | P54259 | WDR5 P61964 | 6 | EBI-945980, EBI-540834 |
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 | 1-608 | Disordered | ||||
Sequence: MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQELPRPQSPSDLDSLDGRSLNDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPQPPDSTPRQPEASFEPHPSVTPTGYHAPMEPPTSRMFQAPPGAPPPHPQLYPGGTGGVLSGPPMGPKGGGAASSVGGPNGGKQHPPPTTPISVSSSGASGAPPTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLNNASASPPGLGAQPLPGHLPSPHAMGQGMGGLPPGPEKGPTLAPSPHSLPPASSSAPAPPMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQALPSYPHSFPPPTSLSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANSNAHPGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNSGPPPPGAFPHPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSPSQGPQGAPYPFPPVPTVT | ||||||
Motif | 16-32 | Nuclear localization signal | ||||
Sequence: RKKEAPGPREELRSRGR | ||||||
Compositional bias | 48-95 | Basic and acidic residues | ||||
Sequence: EKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQE | ||||||
Compositional bias | 109-127 | Basic and acidic residues | ||||
Sequence: DGRSLNDDGSSDPRDIDQD | ||||||
Compositional bias | 128-154 | Polar residues | ||||
Sequence: NRSTSPSIYSPGSVENDSDSSSGLSQG | ||||||
Compositional bias | 156-178 | Pro residues | ||||
Sequence: ARPYHPPPLFPPSPQPPDSTPRQ | ||||||
Compositional bias | 203-220 | Pro residues | ||||
Sequence: SRMFQAPPGAPPPHPQLY | ||||||
Compositional bias | 255-271 | Polar residues | ||||
Sequence: PPTTPISVSSSGASGAP | ||||||
Compositional bias | 272-311 | Pro residues | ||||
Sequence: PTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLN | ||||||
Compositional bias | 347-368 | Pro residues | ||||
Sequence: EKGPTLAPSPHSLPPASSSAPA | ||||||
Compositional bias | 370-404 | Polar residues | ||||
Sequence: PMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQA | ||||||
Compositional bias | 414-436 | Polar residues | ||||
Sequence: PPTSLSVSNQPPKYTQPSLPSQA | ||||||
Compositional bias | 459-507 | Polar residues | ||||
Sequence: PGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNS | ||||||
Region | 517-567 | Involved in binding BAIAP2 | ||||
Sequence: HPLEGGSSHHAHPYAMSPSLGSLRPYPPGPAHLPPPHSQVSYSQAGPNGPP | ||||||
Compositional bias | 553-590 | Polar residues | ||||
Sequence: HSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSP | ||||||
Compositional bias | 591-605 | Pro residues | ||||
Sequence: SQGPQGAPYPFPPVP | ||||||
Region | 622-767 | Disordered | ||||
Sequence: ASSPAGYKTASPPGPPPYGKRAPSPGAYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASGPPLSATQIKQEPAEEYETPESPVPPARSPSPPPKVVDVPSHASQSARFN | ||||||
Compositional bias | 683-718 | Pro residues | ||||
Sequence: GTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASG | ||||||
Compositional bias | 736-754 | Pro residues | ||||
Sequence: TPESPVPPARSPSPPPKVV | ||||||
Region | 785-862 | Disordered | ||||
Sequence: VPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPP | ||||||
Compositional bias | 791-843 | Basic and acidic residues | ||||
Sequence: KLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQ | ||||||
Region | 879-894 | Required for interaction with FAT1 | ||||
Sequence: DTPALRTLSEYARPHV | ||||||
Motif | 1033-1041 | Nuclear export signal | ||||
Sequence: ALGNDPLAR | ||||||
Region | 1049-1065 | HX repeat | ||||
Sequence: PHHHQHSHIHSHLHLHQ |
Domain
The HX repeat motif is a specific pH-dependent interaction motif for ions and/or proteins or other biomolecules. This motif could be involved in the control of embryonic development.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,190
- Mass (Da)125,414
- Last updated2011-01-11 v3
- ChecksumB47603486C672637
Sequence caution
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: EKSRQTAKKARVEEASTPKVNKQGRSEEISESESEETNAPKKTKTEQE | ||||||
Sequence conflict | 94 | in Ref. 3; AAB50276 | ||||
Sequence: Missing | ||||||
Compositional bias | 109-127 | Basic and acidic residues | ||||
Sequence: DGRSLNDDGSSDPRDIDQD | ||||||
Compositional bias | 128-154 | Polar residues | ||||
Sequence: NRSTSPSIYSPGSVENDSDSSSGLSQG | ||||||
Compositional bias | 156-178 | Pro residues | ||||
Sequence: ARPYHPPPLFPPSPQPPDSTPRQ | ||||||
Compositional bias | 203-220 | Pro residues | ||||
Sequence: SRMFQAPPGAPPPHPQLY | ||||||
Compositional bias | 255-271 | Polar residues | ||||
Sequence: PPTTPISVSSSGASGAP | ||||||
Compositional bias | 272-311 | Pro residues | ||||
Sequence: PTKPPTTPVGGGNLPSAPPPANFPHVTPNLPPPPALRPLN | ||||||
Sequence conflict | 333 | in Ref. 1; BAA06626 | ||||
Sequence: H → Y | ||||||
Compositional bias | 347-368 | Pro residues | ||||
Sequence: EKGPTLAPSPHSLPPASSSAPA | ||||||
Compositional bias | 370-404 | Polar residues | ||||
Sequence: PMRFPYSSSSSSSAAASSSSSSSSSSASPFPASQA | ||||||
Compositional bias | 414-436 | Polar residues | ||||
Sequence: PPTSLSVSNQPPKYTQPSLPSQA | ||||||
Compositional bias | 459-507 | Polar residues | ||||
Sequence: PGPFPPSTGAQSTAHPPVSTHHHHHQQQQQQQQQQQQQQQQQQQHHGNS | ||||||
Compositional bias | 553-590 | Polar residues | ||||
Sequence: HSQVSYSQAGPNGPPVSSSSNSSSSTSQGSYPCSHPSP | ||||||
Compositional bias | 591-605 | Pro residues | ||||
Sequence: SQGPQGAPYPFPPVP | ||||||
Compositional bias | 683-718 | Pro residues | ||||
Sequence: GTFKPGSPTVGPGPLPPAGPSGLPSLPPPPAAPASG | ||||||
Compositional bias | 736-754 | Pro residues | ||||
Sequence: TPESPVPPARSPSPPPKVV | ||||||
Compositional bias | 791-843 | Basic and acidic residues | ||||
Sequence: KLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQ | ||||||
Sequence conflict | 1033 | in Ref. 1; BAA06626 | ||||
Sequence: A → G |
Polymorphism
The poly-Gln region of ATN1 is highly polymorphic (7 to 23 repeats) in the normal population and is expanded to about 49-75 repeats in DRPLA and HRS patients. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D31840 EMBL· GenBank· DDBJ | BAA06626.1 EMBL· GenBank· DDBJ | mRNA | ||
D38529 EMBL· GenBank· DDBJ | BAA07534.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
U23851 EMBL· GenBank· DDBJ | AAB50276.1 EMBL· GenBank· DDBJ | mRNA | ||
U47924 EMBL· GenBank· DDBJ | AAB51321.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D63808 EMBL· GenBank· DDBJ | BAA23631.1 EMBL· GenBank· DDBJ | Genomic DNA |