Q7TQC5
Gene name |
Aptx |
Protein name |
Aprataxin |
Names |
Forkhead-associated domain histidine triad-like protein, FHA-HIT |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:66408 |
EC number |
3.6.1.71: In phosphorus-containing anhydrides |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q7TQC5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7TQC5-F1 | Predicted | AlphaFoldDB |
25 variants for Q7TQC5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs27816827 | 2 | P>R | No | EVA | |
| rs3388680984 | 9 | R>Q | No | EVA | |
| rs3388657132 | 13 | L>S | No | EVA | |
| rs3388677511 | 79 | I>V | No | EVA | |
| rs241058898 | 85 | K>M | No | EVA | |
| rs255215510 | 86 | K>M | No | EVA | |
| rs224198323 | 86 | K>Q | No | EVA | |
| rs3388675057 | 112 | S>I | No | EVA | |
| rs27760375 | 114 | N>D | No | EVA | |
| rs3388664646 | 121 | K>R | No | EVA | |
| rs3388677436 | 149 | V>M | No | EVA | |
| rs212905249 | 154 | D>G | No | EVA | |
| rs265728792 | 176 | K>N | No | EVA | |
| rs3388670703 | 185 | D>Y | No | EVA | |
| rs3388676295 | 205 | L>I | No | EVA | |
| rs3388657070 | 206 | P>L | No | EVA | |
| rs3388664578 | 232 | E>V | No | EVA | |
| rs3388671637 | 233 | K>N | No | EVA | |
| rs237910483 | 237 | D>E | No | EVA | |
| rs3388678778 | 237 | D>Y | No | EVA | |
| rs864264411 | 312 | L>R | No | EVA | |
| rs3388664639 | 320 | H>N | No | EVA | |
| rs3394184225 | 329 | I>S | No | EVA | |
| rs3394203039 | 330 | P>Q | No | EVA | |
| rs3393877929 | 333 | K>Q | No | EVA |
2 associated diseases with Q7TQC5
[MIM: 613402]: Microcephaly, seizures, and developmental delay (MCSZ)
An autosomal recessive neurodevelopmental disorder characterized by infantile-onset seizures, microcephaly, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly. {ECO:0000269|PubMed:20118933, ECO:0000269|PubMed:27232581, ECO:0000269|PubMed:28453785}. Note=The disease is caused by variants affecting the gene represented in this entry.
[MIM: 616267]: Ataxia-oculomotor apraxia 4 (AOA4)
An autosomal recessive disease characterized by cerebellar ataxia, oculomotor apraxia, areflexia and peripheral neuropathy. {ECO:0000269|PubMed:25728773}. Note=The disease is caused by variants affecting the gene represented in this entry.
Without disease ID
- An autosomal recessive neurodevelopmental disorder characterized by infantile-onset seizures, microcephaly, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly. {ECO:0000269|PubMed:20118933, ECO:0000269|PubMed:27232581, ECO:0000269|PubMed:28453785}. Note=The disease is caused by variants affecting the gene represented in this entry.
- An autosomal recessive disease characterized by cerebellar ataxia, oculomotor apraxia, areflexia and peripheral neuropathy. {ECO:0000269|PubMed:25728773}. Note=The disease is caused by variants affecting the gene represented in this entry.
6 regional properties for Q7TQC5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Rho GTPase-activating protein domain | 656 - 844 | IPR000198 |
| domain | WW domain | 265 - 298 | IPR001202-1 |
| domain | WW domain | 359 - 391 | IPR001202-2 |
| domain | SH3 domain | 12 - 74 | IPR001452 |
| domain | Pleckstrin homology domain | 463 - 577 | IPR001849 |
| domain | ARHGAP12, SH3 domain | 15 - 74 | IPR035491 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.1.71 | In phosphorus-containing anhydrides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromatin | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
14 GO annotations of molecular function
| Name | Definition |
|---|---|
| chromatin binding | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
| damaged DNA binding | Binding to damaged DNA. |
| DNA 5'-adenosine monophosphate hydrolase activity | Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus. |
| DNA-3'-diphospho-5'-guanosine diphosphatase | Catalysis of the reaction: (DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate + GMP. |
| double-stranded DNA binding | Binding to double-stranded DNA. |
| double-stranded RNA binding | Binding to double-stranded RNA. |
| metal ion binding | Binding to a metal ion. |
| mismatched DNA binding | Binding to a double-stranded DNA region containing one or more mismatches. |
| phosphoglycolate phosphatase activity | Catalysis of the reaction: 2-phosphoglycolate + H(2)O = glycolate + phosphate. |
| phosphoprotein binding | Binding to a phosphorylated protein. |
| polynucleotide 3'-phosphatase activity | Catalysis of the reaction: 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. Hydrolyzes the free 3'-phosphate resulting from single strand breaks in DNA due to oxidative damage. |
| protein N-terminus binding | Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. |
| single-strand break-containing DNA binding | Binding to damaged DNA containing single-strand breaks (SSBs). |
| single-stranded DNA binding | Binding to single-stranded DNA. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to DNA damage stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| DNA ligation | The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase. |
| double-strand break repair | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. |
| regulation of protein stability | Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation. |
| response to hydrogen peroxide | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus. |
| single strand break repair | The repair of single strand breaks in DNA. Repair of such breaks is mediated by the same enzyme systems as are used in base excision repair. |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q7YRZ2 | APTX | Aprataxin | Bos taurus (Bovine) | PR |
| Q96T60 | PNKP | Bifunctional polynucleotide phosphatase/kinase | Homo sapiens (Human) | PR |
| Q7Z2E3 | APTX | Aprataxin | Homo sapiens (Human) | PR |
| Q9JLV6 | Pnkp | Bifunctional polynucleotide phosphatase/kinase | Mus musculus (Mouse) | PR |
| Q7YRZ1 | APTX | Aprataxin | Sus scrofa (Pig) | PR |
| Q19683 | F21D5.5 | Uncharacterized protein F21D5.5 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPEAVAKMRV | CWLVRQDSRH | QRIKLPHLEA | VVIGRSPETK | ITDKKCSRQQ | VQLKAECNKG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YVKVQQMGVN | PTSIDSGVIG | KDQEKKLLPG | QVLHMVNGLY | PYIVEFEEVA | ESPNLTQRKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KRSDCDSEEM | EAESGTGLAP | GSSPSQCSVS | PKKDKNGATK | KESLGHWSQG | LKMSMKDPKM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QVYKDDQVVV | IKDKYPKARH | HWLVLPWASI | SSLKVVTSEH | LELLKHMHAV | GEKVIADFAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SSKLRFRLGY | HAIPSMSHVH | LHVISQDFDS | PCLKNKKHWN | SFNTEYFLES | QAVIKMVQEA |
| 310 | 320 | 330 | 340 | ||
| GRVTVKDGTC | ELLKLPLRCH | ECQQLLPSIP | QLKEHLRKHW | GG |