A0A096LNN3 · A0A096LNN3_HUMAN
- ProteinTranscriptional regulator ATRX
- GeneATRX
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids528 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
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 | chromosome, telomeric region | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Molecular Function | DNA binding | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | DNA repair | |
Biological Process | negative regulation of macromolecule biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscriptional regulator ATRX
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A096LNN3
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,645 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) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 257 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 330 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-103 | Disordered | ||||
Sequence: MMENSKEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQSLPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLK | ||||||
Compositional bias | 14-28 | Polar residues | ||||
Sequence: EKSKSSGSSRSKRKP | ||||||
Compositional bias | 54-69 | Polar residues | ||||
Sequence: NENSENDITMQSLPKG | ||||||
Compositional bias | 78-103 | Basic and acidic residues | ||||
Sequence: VLNEDKDDFKGPEFRSRSKMKTENLK | ||||||
Domain | 104-241 | PHD-type | ||||
Sequence: KRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKK | ||||||
Compositional bias | 390-451 | Basic and acidic residues | ||||
Sequence: KGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEP | ||||||
Region | 390-528 | Disordered | ||||
Sequence: KGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVT | ||||||
Compositional bias | 479-528 | Polar residues | ||||
Sequence: TAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVT |
Sequence similarities
Belongs to the SNF2/RAD54 helicase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length528
- Mass (Da)59,388
- Last updated2014-11-26 v1
- Checksum1207FBFB9975E73E
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P46100 | ATRX_HUMAN | ATRX | 2492 | ||
A0A6Q8PHA4 | A0A6Q8PHA4_HUMAN | ATRX | 858 | ||
A0A096LNW1 | A0A096LNW1_HUMAN | ATRX | 954 | ||
A0A096LNX6 | A0A096LNX6_HUMAN | ATRX | 175 | ||
A0A096LNR8 | A0A096LNR8_HUMAN | ATRX | 66 | ||
A0A096LNL6 | A0A096LNL6_HUMAN | ATRX | 198 | ||
A0A096LNL7 | A0A096LNL7_HUMAN | ATRX | 108 | ||
A0A096LNL9 | A0A096LNL9_HUMAN | ATRX | 1351 | ||
A0A096LPG6 | A0A096LPG6_HUMAN | ATRX | 47 | ||
A0A096LP59 | A0A096LP59_HUMAN | ATRX | 293 | ||
H0Y3T0 | H0Y3T0_HUMAN | ATRX | 198 | ||
A0A087WWG0 | A0A087WWG0_HUMAN | ATRX | 164 |
Features
Showing features for compositional bias, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 14-28 | Polar residues | ||||
Sequence: EKSKSSGSSRSKRKP | ||||||
Compositional bias | 54-69 | Polar residues | ||||
Sequence: NENSENDITMQSLPKG | ||||||
Compositional bias | 78-103 | Basic and acidic residues | ||||
Sequence: VLNEDKDDFKGPEFRSRSKMKTENLK | ||||||
Compositional bias | 390-451 | Basic and acidic residues | ||||
Sequence: KGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPTEEQRTNKSTGGEHKKSDRKEEPQYEP | ||||||
Compositional bias | 479-528 | Polar residues | ||||
Sequence: TAMEVQSSVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVT | ||||||
Non-terminal residue | 528 | |||||
Sequence: T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC233293 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC233305 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138743 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |