P0C7T5 · ATX1L_HUMAN
- ProteinAtaxin-1-like
- GeneATXN1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids689 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression (PubMed:21475249).
Can suppress ATXN1 cytotoxicity in spinocerebellar ataxia type 1 (SCA1). In concert with CIC and ATXN1, involved in brain development (By similarity).
Can suppress ATXN1 cytotoxicity in spinocerebellar ataxia type 1 (SCA1). In concert with CIC and ATXN1, involved in brain development (By similarity).
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 | dendrite | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | POZ domain binding | |
Molecular Function | RNA binding | |
Biological Process | brain development | |
Biological Process | extracellular matrix organization | |
Biological Process | learning | |
Biological Process | lung alveolus development | |
Biological Process | memory | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of hematopoietic stem cell proliferation | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | social behavior | |
Biological Process | transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAtaxin-1-like
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP0C7T5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Forms nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus into the cell body and dendrites in Purkinje cells and in inferior olive cells.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_044496 | 313 | in dbSNP:rs7194407 | |||
Sequence: S → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 693 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, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000343709 | 1-689 | UniProt | Ataxin-1-like | |||
Sequence: MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPVVECVVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVVGEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTTQLFSLPCHRLQVGDVCISISLQSLNSNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 245 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 251 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 284 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 284 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 330 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 361 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 366 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 456 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 615 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 685 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Interacts with CIC (By similarity).
Interacts (via AXH domain) with NCOR2. Interacts with ATXN1 (PubMed:16121196).
Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1 for RBPJ-binding (PubMed:21475249).
Found in a complex with CIC and ATXN1 (By similarity).
Interacts (via AXH domain) with NCOR2. Interacts with ATXN1 (PubMed:16121196).
Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1 for RBPJ-binding (PubMed:21475249).
Found in a complex with CIC and ATXN1 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MKPVHERSQECLPPKKRDLPVTS | ||||||
Region | 1-46 | Disordered | ||||
Sequence: MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWS | ||||||
Region | 20-197 | Interaction with NCOR2 and ATXN1 | ||||
Sequence: PVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHS | ||||||
Region | 20-197 | Self-association | ||||
Sequence: PVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHS | ||||||
Compositional bias | 24-44 | Polar residues | ||||
Sequence: EDMGRTTSCSTNHTPSSDASE | ||||||
Region | 185-223 | Disordered | ||||
Sequence: ATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLA | ||||||
Compositional bias | 196-217 | Polar residues | ||||
Sequence: HSFNKAPSATSPSGQLPHHSST | ||||||
Region | 242-297 | Disordered | ||||
Sequence: LHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQ | ||||||
Compositional bias | 252-266 | Polar residues | ||||
Sequence: PVLTPQESQSALEAA | ||||||
Compositional bias | 275-289 | Basic and acidic residues | ||||
Sequence: RERNLVRRESEALDS | ||||||
Region | 357-405 | Disordered | ||||
Sequence: KEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVK | ||||||
Compositional bias | 361-375 | Basic and acidic residues | ||||
Sequence: SPLNLSHHTPDHQGE | ||||||
Domain | 457-588 | AXH | ||||
Sequence: PPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVVGEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTTQLFSLPCHRLQVGDVCISISLQSLNSN | ||||||
Region | 617-647 | Disordered | ||||
Sequence: ELCDSEGKSQPAGEGSRVVEPSQPESGAQAC |
Sequence similarities
Belongs to the ATXN1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length689
- Mass (Da)73,306
- Last updated2008-07-22 v1
- Checksum9C5D3938EF91F2C7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MKPVHERSQECLPPKKRDLPVTS | ||||||
Compositional bias | 24-44 | Polar residues | ||||
Sequence: EDMGRTTSCSTNHTPSSDASE | ||||||
Compositional bias | 196-217 | Polar residues | ||||
Sequence: HSFNKAPSATSPSGQLPHHSST | ||||||
Compositional bias | 252-266 | Polar residues | ||||
Sequence: PVLTPQESQSALEAA | ||||||
Compositional bias | 275-289 | Basic and acidic residues | ||||
Sequence: RERNLVRRESEALDS | ||||||
Compositional bias | 361-375 | Basic and acidic residues | ||||
Sequence: SPLNLSHHTPDHQGE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC010653 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BX537575 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |