Protein:APTX |
Protein Summary |
 Gene summary |
| Gene name: APTX | ASpdb.0 ID: 54840 | Gene | Gene symbol | APTX | Gene ID | 54840 |
| Gene name | aprataxin |
| Synonyms | AOA|AOA1|AXA1|EAOH|EOAHA|FHA-HIT |
| Cytomap | 9p21.1 |
| Type of gene | protein-coding |
| Description | aprataxinforkhead-associated domain histidine triad-like protein |
| Modification date | 20240305 |
| UniProtAcc | Q7Z2E3 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | APTX | GO:0000012 | single strand break repair | 17519253 |
| Gene | APTX | GO:0000785 | chromatin | 15044383|20008512 |
| Gene | APTX | GO:0003682 | chromatin binding | 15044383 |
| Gene | APTX | GO:0003684 | damaged DNA binding | 14755728 |
| Gene | APTX | GO:0003690 | double-stranded DNA binding | 16547001|17276982 |
| Gene | APTX | GO:0003725 | double-stranded RNA binding | 16547001 |
| Gene | APTX | GO:0005654 | nucleoplasm | 15044383|16777843 |
| Gene | APTX | GO:0005730 | nucleolus | 15044383|16777843 |
| Gene | APTX | GO:0008967 | phosphoglycolate phosphatase activity | 17519253 |
| Gene | APTX | GO:0033699 | DNA 5'-adenosine monophosphate hydrolase activity | 16547001|16964241|17276982|17519253 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q7Z2E3-1 | Q7Z2E3-1_4ndg_A.pdb | 4NDG | X-ray | 2.54 | A | 179 | 355 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-10 | 356 | 302 | 59 | 112 | Deletion | none | none | 58 | 58 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-11 | 356 | 306 | 306 | 356 | Substitution | AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ | E | 306 | 306 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-12 | 356 | 49 | 1 | 14 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-12 | 356 | 49 | 60 | 63 | Substitution | QLKA | ESRV | 46 | 49 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-12 | 356 | 49 | 64 | 356 | Deletion | none | none | 49 | 49 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-13 | 356 | 192 | 1 | 14 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-13 | 356 | 192 | 196 | 356 | Substitution | VYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ | PCTSSCDQPGF | 182 | 192 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-2 | 356 | 168 | 1 | 188 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-3 | 356 | 284 | 104 | 175 | Deletion | none | none | 103 | 103 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-4 | 356 | 254 | 1 | 102 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-5 | 356 | 288 | 1 | 14 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-5 | 356 | 288 | 59 | 112 | Deletion | none | none | 44 | 44 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-6 | 356 | 113 | 1 | 193 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-6 | 356 | 113 | 306 | 356 | Substitution | AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ | E | 113 | 113 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-7 | 356 | 342 | 1 | 14 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-8 | 356 | 337 | 175 | 193 | Deletion | none | none | 174 | 174 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-9 | 356 | 292 | 1 | 14 | Deletion | none | none | 0 | 0 |
| Q7Z2E3 | APTX | Q7Z2E3-1 | Q7Z2E3-9 | 356 | 292 | 306 | 356 | Substitution | AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ | E | 292 | 292 |
| Multiple sequence alignment of our canonical and alternatively spliced APTX |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of APTX |
| UniProt-id | ENSG | ENST | ENSP |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000460940.6 | ENSP00000418311.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000464632.6 | ENSP00000418069.2 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000465003.6 | ENSP00000419430.2 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000467331.6 | ENSP00000418733.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000479656.6 | ENSP00000420071.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000482687.6 | ENSP00000419289.2 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000485479.6 | ENSP00000418144.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000494649.5 | ENSP00000417634.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000672519.1 | ENSP00000500320.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000672535.1 | ENSP00000499872.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000672846.1 | ENSP00000500396.1 |
| Q7Z2E3-12 | ENSG00000137074.20 | ENST00000673487.1 | ENSP00000500943.1 |
| Q7Z2E3-2 | ENSG00000137074.20 | ENST00000673598.1 | ENSP00000499991.1 |
| Q7Z2E3-4 | ENSG00000137074.20 | ENST00000672438.1 | ENSP00000499997.1 |
| Q7Z2E3-4 | ENSG00000137074.20 | ENST00000673248.1 | ENSP00000500601.1 |
| Q7Z2E3-4 | ENSG00000137074.20 | ENST00000673416.1 | ENSP00000500738.1 |
| Q7Z2E3-5 | ENSG00000137074.20 | ENST00000309615.8 | ENSP00000311547.4 |
| Q7Z2E3-5 | ENSG00000137074.20 | ENST00000436040.7 | ENSP00000400806.4 |
| Q7Z2E3-5 | ENSG00000137074.20 | ENST00000476858.6 | ENSP00000419042.2 |
| Q7Z2E3-7 | ENSG00000137074.20 | ENST00000379817.7 | ENSP00000369145.2 |
| Q7Z2E3-7 | ENSG00000137074.20 | ENST00000379819.6 | ENSP00000369147.2 |
| Q7Z2E3-7 | ENSG00000137074.20 | ENST00000463596.6 | ENSP00000419846.1 |
| Q7Z2E3-9 | ENSG00000137074.20 | ENST00000379825.7 | ENSP00000369153.3 |
| Q7Z2E3-9 | ENSG00000137074.20 | ENST00000468275.6 | ENSP00000420263.2 |
| UniProt-id | NM ID | NP ID |
| Q7Z2E3-5 | NM_001195250.1 | NP_001182179.1 |
| Q7Z2E3-5 | NM_001195254.1 | NP_001182183.1 |
| Q7Z2E3-7 | NM_001195248.1 | NP_001182177.1 |
| Q7Z2E3-7 | NM_001195249.1 | NP_001182178.1 |
| Q7Z2E3-7 | NM_175073.2 | NP_778243.1 |
| Q7Z2E3-9 | NM_001195251.1 | NP_001182180.1 |
| Q7Z2E3-9 | NM_175069.2 | NP_778239.1 |
| Amino acid sequences of our canonical and alternatively spliced APTX |
| accession_id | Protein sequence |
| Q7Z2E3-1 | MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKD QEVKLQPGQVLHMVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGH WSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSM |
| Q7Z2E3-10 | MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQ EAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREH LELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMP |
| Q7Z2E3-11 | MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKD QEVKLQPGQVLHMVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGH WSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSM |
| Q7Z2E3-12 | |
| Q7Z2E3-13 | MMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKDQEVKLQPGQVLHMV NELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKM |
| Q7Z2E3-2 | MQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVI |
| Q7Z2E3-3 | MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKD QEVKLQPGQVLHMESLGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDF AGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPS |
| Q7Z2E3-4 | MVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDP KMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDF |
| Q7Z2E3-5 | MMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNS GQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKV IVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKNKKHWNSFNTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQ |
| Q7Z2E3-6 | MQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFD |
| Q7Z2E3-7 | MMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKDQEVKLQPGQVLHMV NELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKM QVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDS |
| Q7Z2E3-8 | MSNVNLSVSDFWRVMMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKD QEVKLQPGQVLHMVNELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKMQVYKD EQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDSPCLKN |
| Q7Z2E3-9 | MMRVCWLVRQDSRHQRIRLPHLEAVVIGRGPETKITDKKCSRQQVQLKAECNKGYVKVKQVGVNPTSIDSVVIGKDQEVKLQPGQVLHMV NELYPYIVEFEEEAKNPGLETHRKRKRSGNSDSIERDAAQEAEAGTGLEPGSNSGQCSVPLKKGKDAPIKKESLGHWSQGLKISMQDPKM QVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSKLRFRLGYHAIPSMSHVHLHVISQDFDS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| APTX (go to UniProt):Q7Z2E3 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Substitution;Start=60;End=63 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=1;End=102 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Domain | 38 | 87 | Note=FHA-like | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Domain | 182 | 287 | Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Domain | 182 | 287 | Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 | Type=Substitution;Start=196;End=356 |
| Q7Z2E3 | Domain | 182 | 287 | Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Domain | 182 | 287 | Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Domain | 182 | 287 | Note=HIT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 | Type=Deletion;Start=175;End=193 |
| Q7Z2E3 | Zinc finger | 331 | 353 | "Note=C2H2-type;Ontology_term=ECO:0000255 | ECO:0000305 |
| Q7Z2E3 | Zinc finger | 331 | 353 | "Note=C2H2-type;Ontology_term=ECO:0000255 | ECO:0000305 |
| Q7Z2E3 | Zinc finger | 331 | 353 | "Note=C2H2-type;Ontology_term=ECO:0000255 | ECO:0000305 |
| Q7Z2E3 | Zinc finger | 331 | 353 | "Note=C2H2-type;Ontology_term=ECO:0000255 | ECO:0000305 |
| Q7Z2E3 | Zinc finger | 331 | 353 | "Note=C2H2-type;Ontology_term=ECO:0000255 | ECO:0000305 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Substitution;Start=60;End=63 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=104;End=175 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=102 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 122 | 167 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 122 | 167 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Region | 122 | 167 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=104;End=175 |
| Q7Z2E3 | Region | 122 | 167 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Region | 207 | 211 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 207 | 211 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Substitution;Start=196;End=356 |
| Q7Z2E3 | Region | 269 | 270 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 269 | 270 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Substitution;Start=196;End=356 |
| Q7Z2E3 | Motif | 126 | 131 | Note=Nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Motif | 126 | 131 | Note=Nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305 | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Motif | 126 | 131 | Note=Nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305 | Type=Deletion;Start=104;End=175 |
| Q7Z2E3 | Motif | 126 | 131 | Note=Nuclear localization signal;Ontology_term=ECO:0000305;evidence=ECO:0000305 | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Motif | 272 | 276 | "Note=Histidine triad motif;Ontology_term=ECO:0000255 | ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 |
| Q7Z2E3 | Motif | 272 | 276 | "Note=Histidine triad motif;Ontology_term=ECO:0000255 | ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU00464 |
| Q7Z2E3 | Compositional bias | 122 | 143 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Compositional bias | 122 | 143 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Compositional bias | 122 | 143 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=104;End=175 |
| Q7Z2E3 | Compositional bias | 122 | 143 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=193 |
Gene Isoform Structures and Expression Levels for APTX |
| Gene structures of our canonical and alternative spliced genes of APTX * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q7Z2E3-1 |
| 3D view using mol* of Q7Z2E3-10 |
| 3D view using mol* of Q7Z2E3-11 |
| 3D view using mol* of Q7Z2E3-12 |
| 3D view using mol* of Q7Z2E3-13 |
| 3D view using mol* of Q7Z2E3-2 |
| 3D view using mol* of Q7Z2E3-3 |
| 3D view using mol* of Q7Z2E3-4 |
| 3D view using mol* of Q7Z2E3-5 |
| 3D view using mol* of Q7Z2E3-6 |
| 3D view using mol* of Q7Z2E3-7 |
| 3D view using mol* of Q7Z2E3-8 |
| 3D view using mol* of Q7Z2E3-9 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q7Z2E3-1 |
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| pLDDT distribution across the protein length of Q7Z2E3-10 |
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| pLDDT distribution across the protein length of Q7Z2E3-11 |
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| pLDDT distribution across the protein length of Q7Z2E3-12 |
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| pLDDT distribution across the protein length of Q7Z2E3-13 |
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| pLDDT distribution across the protein length of Q7Z2E3-2 |
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| pLDDT distribution across the protein length of Q7Z2E3-3 |
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| pLDDT distribution across the protein length of Q7Z2E3-4 |
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| pLDDT distribution across the protein length of Q7Z2E3-5 |
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| pLDDT distribution across the protein length of Q7Z2E3-6 |
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| pLDDT distribution across the protein length of Q7Z2E3-7 |
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| pLDDT distribution across the protein length of Q7Z2E3-8 |
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| pLDDT distribution across the protein length of Q7Z2E3-9 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q7Z2E3-1 |
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| Ramachandran plot of Q7Z2E3-10 |
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| Ramachandran plot of Q7Z2E3-11 |
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| Ramachandran plot of Q7Z2E3-12 |
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| Ramachandran plot of Q7Z2E3-2 |
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| Ramachandran plot of Q7Z2E3-7 |
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| Ramachandran plot of Q7Z2E3-8 |
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| Ramachandran plot of Q7Z2E3-9 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q7Z2E3-1 | 0.999 | 216 | 1.021 | 697.319 | 0.57 | 0.69 | 0.938 | 0.49 | 1.02 | 0.481 | 1.053 | 82,83,84,85,91,92,93,94,99,106,177,178,179,180,181 ,182,183,184,185,187,188,194,205,206,207,208,209,2 11,217,225,226,228,265,267,268,269,270,271,276,291 ,292,295,296,300,319,320,321,322,323,324,327 |
| Q7Z2E3-10 | 1.011 | 200 | 0.978 | 564.578 | 0.557 | 0.714 | 0.951 | 0.478 | 1.196 | 0.399 | 0.503 | 65,70,71,72,73,74,75,76,77,127,130,131,133,134,136 ,137,139,140,141,142,151,152,153,154,155,157,161,1 63,211,213,214,215,216,220,222,234,237,238,241,242 ,246,273 |
| Q7Z2E3-11 | 1.057 | 100 | 1.014 | 320.019 | 0.454 | 0.784 | 1.094 | 0.777 | 1.217 | 0.638 | 1.017 | 184,185,187,188,194,205,206,207,208,209,211,215,21 7,265,268,269,270,274,276,291,292,295,296,300 |
| Q7Z2E3-12 | 0.821 | 34 | 0.868 | 73.059 | 0.626 | 0.652 | 0.868 | 2.753 | 0.22 | 12.532 | 0.936 | 7,8,9,10,15,16,17,27,28,33,35,44,45
|
| Q7Z2E3-13 | 0.723 | 51 | 0.564 | 89.18 | 0.575 | 0.598 | 0.896 | 0.113 | 1.428 | 0.079 | 0.546 | 1,2,3,4,5,18,19,20,21,51,103,104,105
|
| Q7Z2E3-2 | 0.971 | 109 | 0.987 | 327.908 | 0.612 | 0.655 | 0.883 | 0.252 | 1.059 | 0.238 | 0.614 | 1,2,3,6,7,15,17,19,20,21,23,27,29,31,32,33,35,36,7 7,79,80,81,82,83,84,85,86,88,98,100,103,104,107,10 8,112,139 |
| Q7Z2E3-3 | 1.039 | 119 | 1.003 | 310.072 | 0.42 | 0.757 | 1.046 | 0.565 | 1.199 | 0.471 | 0.917 | 112,113,115,116,122,133,134,135,136,137,139,143,14 5,193,195,196,197,198,202,204,219,220,223,224,228, 255 |
| Q7Z2E3-4 | 1.063 | 98 | 1.033 | 325.507 | 0.391 | 0.803 | 1.071 | 0.754 | 1.161 | 0.65 | 0.721 | 79,82,83,85,86,92,103,104,105,106,107,109,113,115, 163,165,166,167,168,172,174,189,190,193,194,198,22 5 |
| Q7Z2E3-5 | 1.028 | 91 | 1.006 | 290.521 | 0.483 | 0.79 | 1.101 | 0.696 | 1.118 | 0.623 | 0.81 | 116,117,119,120,137,139,140,141,143,147,149,197,20 0,201,202,206,208,223,224,227,228,232,259 |
| Q7Z2E3-6 | 0.745 | 57 | 0.724 | 210.259 | 0.7 | 0.581 | 0.788 | 0.265 | 1.025 | 0.258 | 0.563 | 14,15,16,18,22,24,72,74,75,76,77,81,83,93,95,98,99 ,101,102,103,107 |
| Q7Z2E3-7 | 0.974 | 88 | 0.959 | 292.236 | 0.532 | 0.727 | 1.002 | 0.312 | 1.1 | 0.283 | 0.674 | 39,65,66,67,70,72,88,91,92,93,168,169,211,212,213, 214,252,253,254,255,256,257,258,277,286,305,306,30 7,309,310,313 |
| Q7Z2E3-8 | 1.001 | 182 | 0.989 | 725.788 | 0.635 | 0.7 | 0.869 | 0.447 | 1.138 | 0.393 | 0.743 | 43,52,53,54,55,56,57,76,77,78,79,86,105,106,175,18 6,188,189,190,192,196,198,200,204,206,207,208,209, 246,247,248,249,250,251,252,253,255,257,272,273,27 6,277,281,300,301,305,308,309 |
| Q7Z2E3-9 | 1.034 | 117 | 1.078 | 380.387 | 0.575 | 0.696 | 0.965 | 0.712 | 0.857 | 0.832 | 1.089 | 39,63,75,164,165,166,167,170,171,173,174,180,191,1 92,193,194,195,197,201,203,251,253,254,255,256,260 ,262,277,278,280,281,282,286 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-1_4ndg_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-10.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-11.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-12.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-13.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-2.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-3.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-4.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-5.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-6.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-7.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-8.pdb |
| 3D view using mol* of Q7Z2E3-1_4ndg_A_Q7Z2E3-9.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-10.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-11.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-12.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-13.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-2.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-3.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-4.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-5.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-6.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-7.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-8.pdb |
| 3D view using mol* of Q7Z2E3-1_Q7Z2E3-9.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-10.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-11.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-12.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-13.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-2.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-3.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-4.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-5.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-6.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-7.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-8.png |
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| ./stats/secondary_structure/figure/Q7Z2E3-1_vs_Q7Z2E3-9.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-10.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-11.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-12.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-13.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-2.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-3.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-4.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-5.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-6.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-7.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-8.png |
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| ./stats/relative_asa/Q7Z2E3-1_vs_Q7Z2E3-9.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Substitution;Start=60;End=63 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=188 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=104;End=175 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=102 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=59;End=112 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=193 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 1 | 110 | Note=Interactions with ADPRT/PARP1 and NCL | Type=Deletion;Start=1;End=14 |
| Q7Z2E3 | Region | 207 | 211 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 207 | 211 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Substitution;Start=196;End=356 |
| Q7Z2E3 | Region | 269 | 270 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Deletion;Start=64;End=356 |
| Q7Z2E3 | Region | 269 | 270 | Note=Interaction with DNA substrate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24362567;Dbxref=PMID:24362567 | Type=Substitution;Start=196;End=356 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to APTX |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to APTX |
| Previous studies relating to the alternative splicing of APTX and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| APTX | 15276230 | Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia. | Early-onset ataxia with ocular motor apraxia and hypoalbuminemia (EAOH) is one of the most common forms of autosomal recessive cerebellar ataxia. We identified six new alternative transcripts produced by the aprataxin gene responsible for EAOH. Total eight transcripts encoded truncated proteins that were located within the nucleus or cytoplasm and showed different binding abilities to wild-type (WT) aprataxin. Thus, the alternative splicing increases the molecular diversity of aprataxin and the expression profiles of these transcripts in various tissues may be related to the tissue-specific phenotypes. | D001072 | Apraxias |
| APTX | 15276230 | Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia. | Early-onset ataxia with ocular motor apraxia and hypoalbuminemia (EAOH) is one of the most common forms of autosomal recessive cerebellar ataxia. We identified six new alternative transcripts produced by the aprataxin gene responsible for EAOH. Total eight transcripts encoded truncated proteins that were located within the nucleus or cytoplasm and showed different binding abilities to wild-type (WT) aprataxin. Thus, the alternative splicing increases the molecular diversity of aprataxin and the expression profiles of these transcripts in various tissues may be related to the tissue-specific phenotypes. | D001259 | Ataxia |
| APTX | 15276230 | Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia. | Early-onset ataxia with ocular motor apraxia and hypoalbuminemia (EAOH) is one of the most common forms of autosomal recessive cerebellar ataxia. We identified six new alternative transcripts produced by the aprataxin gene responsible for EAOH. Total eight transcripts encoded truncated proteins that were located within the nucleus or cytoplasm and showed different binding abilities to wild-type (WT) aprataxin. Thus, the alternative splicing increases the molecular diversity of aprataxin and the expression profiles of these transcripts in various tissues may be related to the tissue-specific phenotypes. | D034141 | Hypoalbuminemia |
| APTX | 15276230 | Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia. | Early-onset ataxia with ocular motor apraxia and hypoalbuminemia (EAOH) is one of the most common forms of autosomal recessive cerebellar ataxia. We identified six new alternative transcripts produced by the aprataxin gene responsible for EAOH. Total eight transcripts encoded truncated proteins that were located within the nucleus or cytoplasm and showed different binding abilities to wild-type (WT) aprataxin. Thus, the alternative splicing increases the molecular diversity of aprataxin and the expression profiles of these transcripts in various tissues may be related to the tissue-specific phenotypes. | D015835 | Ocular Motility Disorders |
Clinically important variants in APTX |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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