Protein:PSEN1 |
Protein Summary |
 Gene summary |
| Gene name: PSEN1 | ASpdb.0 ID: 5663 | Gene | Gene symbol | PSEN1 | Gene ID | 5663 |
| Gene name | presenilin 1 |
| Synonyms | ACNINV3|AD3|FAD|PS-1|PS1|PSNL1|S182 |
| Cytomap | 14q24.2 |
| Type of gene | protein-coding |
| Description | presenilin-1familial Alzheimer Disease |
| Modification date | 20240416 |
| UniProtAcc | P49768 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | PSEN1 | GO:0000776 | kinetochore | 9298903 |
| Gene | PSEN1 | GO:0004175 | endopeptidase activity | 8755489 |
| Gene | PSEN1 | GO:0005640 | nuclear outer membrane | 9246482 |
| Gene | PSEN1 | GO:0005654 | nucleoplasm | - |
| Gene | PSEN1 | GO:0005739 | mitochondrion | 12377771 |
| Gene | PSEN1 | GO:0005783 | endoplasmic reticulum | 9246482|15274632 |
| Gene | PSEN1 | GO:0005790 | smooth endoplasmic reticulum | 10508860 |
| Gene | PSEN1 | GO:0005790 | smooth endoplasmic reticulum | 9632714 |
| Gene | PSEN1 | GO:0005791 | rough endoplasmic reticulum | 9632714 |
| Gene | PSEN1 | GO:0005794 | Golgi apparatus | 9246482|9632714|15274632 |
| Gene | PSEN1 | GO:0005813 | centrosome | 9298903 |
| Gene | PSEN1 | GO:0005886 | plasma membrane | 15274632|21143716 |
| Gene | PSEN1 | GO:0006509 | membrane protein ectodomain proteolysis | 15274632 |
| Gene | PSEN1 | GO:0006974 | DNA damage response | 25542424 |
| Gene | PSEN1 | GO:0007220 | Notch receptor processing | 27608597 |
| Gene | PSEN1 | GO:0016020 | membrane | 22375059|26280335 |
| Gene | PSEN1 | GO:0016235 | aggresome | 21143716 |
| Gene | PSEN1 | GO:0016485 | protein processing | 15274632|27608597 |
| Gene | PSEN1 | GO:0030054 | cell junction | - |
| Gene | PSEN1 | GO:0030426 | growth cone | 15004326 |
| Gene | PSEN1 | GO:0031965 | nuclear membrane | 9298903 |
| Gene | PSEN1 | GO:0032469 | endoplasmic reticulum calcium ion homeostasis | 17431506 |
| Gene | PSEN1 | GO:0034205 | amyloid-beta formation | 27608597 |
| Gene | PSEN1 | GO:0042325 | regulation of phosphorylation | 9689133 |
| Gene | PSEN1 | GO:0042500 | aspartic endopeptidase activity, intramembrane cleaving | 26280335 |
| Gene | PSEN1 | GO:0042982 | amyloid precursor protein metabolic process | 26280335 |
| Gene | PSEN1 | GO:0042987 | amyloid precursor protein catabolic process | 27608597 |
| Gene | PSEN1 | GO:0043005 | neuron projection | 15004326 |
| Gene | PSEN1 | GO:0043066 | negative regulation of apoptotic process | 10805794 |
| Gene | PSEN1 | GO:0043085 | positive regulation of catalytic activity | 15274632 |
| Gene | PSEN1 | GO:0045121 | membrane raft | 20299451 |
| Gene | PSEN1 | GO:0070765 | gamma-secretase complex | 10801983|12297508|26280335 |
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 |
| P49768-1 | P49768-1_5fn5_B.pdb | 5FN5 | EM | 4.3 | B | 68 | 467 |
| 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 |
| P49768 | PSEN1 | P49768-1 | P49768-2 | 467 | 463 | 26 | 29 | Deletion | none | none | 25 | 25 |
| P49768 | PSEN1 | P49768-1 | P49768-3 | 467 | 374 | 26 | 29 | Deletion | none | none | 25 | 25 |
| P49768 | PSEN1 | P49768-1 | P49768-3 | 467 | 374 | 319 | 467 | Substitution | STERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI | RACLPPAAINLLSIAPMAPRLFMPKGACRPTAQKGSHKTLLQRMMMAGSVRNGKPRGTVI | 315 | 374 |
| P49768 | PSEN1 | P49768-1 | P49768-4 | 467 | 184 | 162 | 184 | Substitution | IHAWLIISSLLLLFFFSFIYLGE | SMRHRSLLSTLFFLWLGILVTVT | 162 | 184 |
| P49768 | PSEN1 | P49768-1 | P49768-4 | 467 | 184 | 185 | 467 | Deletion | none | none | 184 | 184 |
| P49768 | PSEN1 | P49768-1 | P49768-5 | 467 | 378 | 319 | 467 | Substitution | STERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI | RACLPPAAINLLSIAPMAPRLFMPKGACRPTAQKGSHKTLLQRMMMAGSVRNGKPRGTVI | 319 | 378 |
| P49768 | PSEN1 | P49768-1 | P49768-6 | 467 | 409 | 319 | 376 | Deletion | none | none | 318 | 318 |
| P49768 | PSEN1 | P49768-1 | P49768-7 | 467 | 434 | 257 | 289 | Deletion | none | none | 256 | 256 |
| Multiple sequence alignment of our canonical and alternatively spliced PSEN1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of PSEN1 |
| UniProt-id | ENSG | ENST | ENSP |
| P49768-1 | ENSG00000080815.20 | ENST00000324501.10 | ENSP00000326366.5 |
| P49768-1 | ENSG00000080815.20 | ENST00000554131.6 | ENSP00000451915.2 |
| P49768-1 | ENSG00000080815.20 | ENST00000700267.1 | ENSP00000514903.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700268.1 | ENSP00000514904.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700269.1 | ENSP00000514905.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700306.1 | ENSP00000514933.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700317.1 | ENSP00000514944.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700321.1 | ENSP00000514948.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700323.1 | ENSP00000514950.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700375.1 | ENSP00000514966.1 |
| P49768-1 | ENSG00000080815.20 | ENST00000700378.1 | ENSP00000514968.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000357710.8 | ENSP00000350342.4 |
| P49768-2 | ENSG00000080815.20 | ENST00000394164.5 | ENSP00000377719.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000553599.6 | ENSP00000452477.2 |
| P49768-2 | ENSG00000080815.20 | ENST00000556951.6 | ENSP00000450551.2 |
| P49768-2 | ENSG00000080815.20 | ENST00000700265.1 | ENSP00000514901.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700273.1 | ENSP00000514908.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700313.1 | ENSP00000514940.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700322.1 | ENSP00000514949.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700324.1 | ENSP00000514951.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700389.1 | ENSP00000514970.1 |
| P49768-2 | ENSG00000080815.20 | ENST00000700469.1 | ENSP00000515002.1 |
| P49768-3 | ENSG00000080815.20 | ENST00000555386.6 | ENSP00000450845.1 |
| P49768-4 | ENSG00000080815.20 | ENST00000394157.7 | ENSP00000377712.3 |
| P49768-5 | ENSG00000080815.20 | ENST00000553855.5 | ENSP00000452242.1 |
| P49768-5 | ENSG00000080815.20 | ENST00000700436.1 | ENSP00000514987.1 |
| P49768-6 | ENSG00000080815.20 | ENST00000557511.5 | ENSP00000451429.1 |
| UniProt-id | NM ID | NP ID |
| P49768-1 | NM_000021.3 | NP_000012.1 |
| P49768-1 | XM_005267864.2 | XP_005267921.1 |
| P49768-1 | XM_011536972.2 | XP_011535274.1 |
| P49768-2 | NM_007318.2 | NP_015557.2 |
| P49768-2 | XM_005267866.1 | XP_005267923.1 |
| P49768-2 | XM_011536973.1 | XP_011535275.1 |
| P49768-2 | XM_011536974.1 | XP_011535276.1 |
| Amino acid sequences of our canonical and alternatively spliced PSEN1 |
| accession_id | Protein sequence |
| P49768-1 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVT LCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFI YLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRM LVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAA VQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATD |
| P49768-2 | MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMV VVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGE VFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVET AQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQEL SSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQ |
| P49768-3 | MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMV VVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGE VFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVET AQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAERACLPPAAINLLSIAPMAPRLFMPKGACRPTAQKGSHKTLLQRMMM |
| P49768-4 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVT LCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVSMRHRSLLSTLFFLWLGIL |
| P49768-5 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVT LCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFI YLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRM LVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAERACLPPAAINLLSIAPMAPRLFMPKGACRPTAQKGSHKTLLQ |
| P49768-6 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVT LCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFI YLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRM LVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGL |
| P49768-7 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVT LCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFI YLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYSTMVWLVNMAEGDP EAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLV |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| PSEN1 (go to UniProt):P49768 |
| 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 |
| P49768 | Topological domain | 1 | 82 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=26;End=29 |
| P49768 | Topological domain | 1 | 82 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=26;End=29 |
| P49768 | Topological domain | 154 | 166 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=162;End=184 |
| P49768 | Transmembrane | 167 | 189 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=162;End=184 |
| P49768 | Transmembrane | 167 | 189 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 190 | 194 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 195 | 216 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 217 | 220 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 221 | 241 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 242 | 248 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 249 | 272 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 249 | 272 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=257;End=289 |
| P49768 | Topological domain | 273 | 380 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 273 | 380 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 273 | 380 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 273 | 380 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=319;End=376 |
| P49768 | Topological domain | 273 | 380 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=257;End=289 |
| P49768 | Transmembrane | 381 | 401 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Transmembrane | 381 | 401 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 381 | 401 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 402 | 407 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 402 | 407 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 402 | 407 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Transmembrane | 408 | 428 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Transmembrane | 408 | 428 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 408 | 428 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 429 | 432 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 429 | 432 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 429 | 432 | Note=Cytoplasmic;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Transmembrane | 433 | 453 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Transmembrane | 433 | 453 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Transmembrane | 433 | 453 | Note=Helical;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 454 | 467 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Topological domain | 454 | 467 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Deletion;Start=185;End=467 |
| P49768 | Topological domain | 454 | 467 | Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26280335;Dbxref=PMID:26280335 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 13 | 68 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Region | 13 | 68 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Region | 288 | 290 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 288 | 290 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Deletion;Start=257;End=289 |
| P49768 | Region | 305 | 333 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 305 | 333 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 305 | 333 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 305 | 333 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=319;End=376 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Deletion;Start=319;End=376 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Deletion;Start=319;End=376 |
| P49768 | Region | 377 | 381 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 377 | 381 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 377 | 381 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 432 | 434 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 432 | 434 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 432 | 434 | Note=Important for cleavage of target proteins;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30598546;Dbxref=PMID:30598546 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Substitution;Start=319;End=467 |
| P49768 | Motif | 433 | 435 | Note=PAL;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16305624;Dbxref=PMID:16305624 | Type=Substitution;Start=319;End=467 |
| P49768 | Motif | 433 | 435 | Note=PAL;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16305624;Dbxref=PMID:16305624 | Type=Deletion;Start=185;End=467 |
| P49768 | Motif | 433 | 435 | Note=PAL;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16305624;Dbxref=PMID:16305624 | Type=Substitution;Start=319;End=467 |
| P49768 | Compositional bias | 13 | 27 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Compositional bias | 13 | 27 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Compositional bias | 28 | 47 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Compositional bias | 28 | 47 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=26;End=29 |
| P49768 | Compositional bias | 305 | 329 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=319;End=467 |
| P49768 | Compositional bias | 305 | 329 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=185;End=467 |
| P49768 | Compositional bias | 305 | 329 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=319;End=467 |
| P49768 | Compositional bias | 305 | 329 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=319;End=376 |
Gene Isoform Structures and Expression Levels for PSEN1 |
| Gene structures of our canonical and alternative spliced genes of PSEN1 * 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 P49768-1 |
| 3D view using mol* of P49768-2 |
| 3D view using mol* of P49768-3 |
| 3D view using mol* of P49768-4 |
| 3D view using mol* of P49768-5 |
| 3D view using mol* of P49768-6 |
| 3D view using mol* of P49768-7 |
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 P49768-1 |
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| pLDDT distribution across the protein length of P49768-2 |
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| pLDDT distribution across the protein length of P49768-3 |
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| pLDDT distribution across the protein length of P49768-4 |
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| pLDDT distribution across the protein length of P49768-5 |
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| pLDDT distribution across the protein length of P49768-6 |
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| pLDDT distribution across the protein length of P49768-7 |
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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 P49768-1 |
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| Ramachandran plot of P49768-2 |
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| Ramachandran plot of P49768-5 |
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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 |
| P49768-1 | 1.14 | 231 | 1.229 | 1059.184 | 0.547 | 0.751 | 0.919 | 2.028 | 0.497 | 4.08 | 1.464 | 78,79,81,82,85,140,143,144,147,150,151,166,169,170 ,173,229,233,237,253,256,257,261,262,268,269,271,2 72,273,282,283,285,286,287,379,380,381,382,383,384 ,385,387,388,418,419,422,423,425,426,430,431,432,4 33,434,435 |
| P49768-2 | 1.137 | 234 | 1.227 | 1237.887 | 0.634 | 0.744 | 0.861 | 1.671 | 0.488 | 3.421 | 1.236 | 70,73,74,77,78,81,136,139,140,142,143,145,146,147, 149,157,158,161,162,165,166,168,169,173,225,229,24 9,252,253,257,258,264,265,267,268,278,279,281,282, 283,375,377,378,379,380,381,383,384,414,415,418,41 9,421,422,426,427,428,429,430,431 |
| P49768-3 | 1.152 | 110 | 1.277 | 380.73 | 0.645 | 0.696 | 0.772 | 2.288 | 0.246 | 9.288 | 1.738 | 81,84,85,88,143,146,147,150,158,162,165,166,168,16 9,173,222,223,225,226,229,264,267,268,278,279,281, 282,283,284 |
| P49768-4 | 1.031 | 180 | 1.102 | 543.998 | 0.659 | 0.642 | 0.785 | 0.999 | 0.684 | 1.46 | 1 | 70,73,74,77,80,83,84,87,88,91,95,98,99,102,103,142 ,145,146,150,153,154,156,157,158,159,160,162,163,1 65,166,167,170,171,174,175,177,178,179,181,182 |
| P49768-5 | 1.093 | 75 | 1.177 | 211.974 | 0.519 | 0.775 | 0.913 | 2.705 | 0.313 | 8.638 | 1.17 | 143,144,147,150,151,153,154,162,165,166,169,253,25 6,257,267,268,271,272,275,282,283,286,287 |
| P49768-6 | 1.133 | 283 | 1.219 | 1396.353 | 0.618 | 0.749 | 0.87 | 1.85 | 0.523 | 3.534 | 1.054 | 74,75,77,78,81,82,85,113,115,116,139,140,142,143,1 44,146,147,149,150,151,153,162,165,166,169,170,173 ,177,229,233,236,237,240,241,253,256,257,261,262,2 68,269,271,272,273,282,283,285,286,287,316,319,321 ,322,323,324,325,326,327,329,330,360,364,365,367,3 68,372,373,374,375,376,377 |
| P49768-7 | 1.061 | 666 | 1.127 | 2201.374 | 0.574 | 0.691 | 0.852 | 0.95 | 0.699 | 1.358 | 1.277 | 75,77,78,79,80,81,82,84,85,87,88,91,140,143,144,14 6,147,150,151,165,166,169,170,172,173,177,212,213, 214,215,216,217,219,220,222,223,224,226,227,228,22 9,233,237,249,252,253,256,257,259,260,261,263,264, 265,267,268,269,270,273,322,325,326,328,329,330,33 1,332,333,334,335,336,337,338,339,340,341,342,343, 344,345,346,347,348,349,350,351,352,353,354,355,38 6,389,390,392,393,397,398,399,400,401,402 |
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 P49768-1_P49768-1_5fn5_B.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P49768-1_5fn5_B_P49768-2.pdb |
| 3D view using mol* of P49768-1_5fn5_B_P49768-3.pdb |
| 3D view using mol* of P49768-1_5fn5_B_P49768-4.pdb |
| 3D view using mol* of P49768-1_5fn5_B_P49768-5.pdb |
| 3D view using mol* of P49768-1_5fn5_B_P49768-6.pdb |
| 3D view using mol* of P49768-1_5fn5_B_P49768-7.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P49768-1_P49768-2.pdb |
| 3D view using mol* of P49768-1_P49768-3.pdb |
| 3D view using mol* of P49768-1_P49768-4.pdb |
| 3D view using mol* of P49768-1_P49768-5.pdb |
| 3D view using mol* of P49768-1_P49768-6.pdb |
| 3D view using mol* of P49768-1_P49768-7.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P49768-1_vs_P49768-2.png |
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| ./stats/secondary_structure/figure/P49768-1_vs_P49768-3.png |
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| ./stats/secondary_structure/figure/P49768-1_vs_P49768-4.png |
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| ./stats/secondary_structure/figure/P49768-1_vs_P49768-5.png |
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| ./stats/secondary_structure/figure/P49768-1_vs_P49768-6.png |
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| ./stats/secondary_structure/figure/P49768-1_vs_P49768-7.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P49768-1_vs_P49768-2.png |
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| ./stats/relative_asa/P49768-1_vs_P49768-3.png |
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| ./stats/relative_asa/P49768-1_vs_P49768-4.png |
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| ./stats/relative_asa/P49768-1_vs_P49768-5.png |
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| ./stats/relative_asa/P49768-1_vs_P49768-6.png |
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| ./stats/relative_asa/P49768-1_vs_P49768-7.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 322 | 450 | Note=Required for interaction with CTNNB1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9738936;Dbxref=PMID:9738936 | Type=Deletion;Start=319;End=376 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 372 | 399 | Note=Required for interaction with CTNND2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10037471;Dbxref=PMID:10037471 | Type=Deletion;Start=319;End=376 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Substitution;Start=319;End=467 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Deletion;Start=185;End=467 |
| P49768 | Region | 464 | 467 | Note=Interaction with MTCH1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10551805;Dbxref=PMID:10551805 | Type=Substitution;Start=319;End=467 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to PSEN1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P49768 | PSEN1 | DB12005 | Nirogacestat | approved, investigational | inhibitor |
Related Diseases to PSEN1 |
| Previous studies relating to the alternative splicing of PSEN1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| PSEN1 | 7550356 | The structure of the presenilin 1 (S182) gene and identification of six novel mutations in early onset AD families. | Genetic linkage studies place a gene causing early onset familial Alzheimer's disease (FAD) on chromosome 14q24.3 (refs 1-4). Five mutations within the S182 (Presenilin 1: PS-1) gene, which maps to this region, have recently been reported in several early onset FAD kindreds. We have localized the PS-1 gene to a 75 kb region and present the structure of this gene, evidence for alternative splicing and describe six novel mutations in early onset FAD pedigrees all of which alter residues conserved in the STM2 (Presenilin 2: PS-2) gene. | D000544 | Alzheimer Disease |
| PSEN1 | 8641442 | Identification and characterization of presenilin I-467, I-463 and I-374. | We cloned a novel isoform of presenilin I (presenilin I-374) besides previously published presenilin I-467 and I-463 in human lymphocytes. Presenilin I-463 was identical to presenilin I-467 except a 12 bp nucleotides deletion in its amino terminal region. Another isoform, presenilin I-374 was produced by an alternative splicing with an additional exon consisting of 92 bp nucleotides (exon 11), which resulted in the frame shift with a stop codon to generate a truncated presenilin consisting of 374 amino acids. The transcripts for presenilin I-467/463 was ubiquitously detected while that for presenilin I-374 was selectively detected in liver, spleen, kidney. Abnormal behavior of presenilin I on gel electrophoresis was found with affinity-purified antibodies against presenilin I. | D000544 | Alzheimer Disease |
| PSEN1 | 8875251 | The presenilin genes: a new gene family involved in Alzheimer disease pathology. | A positional cloning approach has led to the identification of two closely related genes, the presenilins (PS), for autosomal dominant presenile Alzheimer disease (AD): PS-1 at 14q24.3 and PS-2 at 1q31-q42. The PS-1 gene was identified by direct cDNA selection of yeast artificial chromosomes containing the candidate chromosomal region. Subsequently, the PS-2 gene was identified due to its high sequence homology with PS-1 and its location within the candidate region defined by linkage studies. To date, 30 different missense mutations and one in-frame splice site mutation were described in PS-1, while only two missense mutations were detected in PS-2, suggesting that PS-1 mutations are more frequently involved in familial presenile AD. The PS transcripts encode novel proteins that resemble integral transmembrane proteins of roughly 450 amino acids and at least seven transmembrane domains. The genomic organization of the PS genes is very similar showing that full length PS-1 and PS-2 are encoded by 10 exons. However, different alternative splicing patterns have been observed for PS-1 and PS-2 indicating that the corresponding proteins (ps-1 and ps-2) may have similar but not identical biological functions. | D000544 | Alzheimer Disease |
| PSEN1 | 9073509 | Analysis of the 5' sequence, genomic structure, and alternative splicing of the presenilin-1 gene (PSEN1) associated with early onset Alzheimer disease. | Mutations in the human presenilin genes (PSEN1 and PSEN2) are associated with early onset familial Alzheimer disease. The presenilin genes encode integral membrane proteins with similar structures, which suggests that they may have closely related, but as yet unknown functions. Analysis of the 5' upstream sequence and the structure of the PSEN1 gene reveals that the 5' sequence contains multiple putative transcription regulatory elements including clusters of STAT elements involved in transcriptional activation in response to signal transduction. The first four exons contain untranslated sequences, with Exons 1 and 2 representing alternate initial transcription sites. The function of these alternate initial exons is unclear. Exon 4 bears the first ATG sequence. The last 12 bp of Exon 4 is used as an alternative splice donor site. Exon 9 is alternately spliced in leukocytes, but not in most other tissues. Splicing of Exon 9 is predicted to cause significant structural changes to the protein. The majority of transcripts expressed in most tissues are polyadenylated 1127 bp from the TAG stop codon in Exon 13. A small proportion of transcripts contain the same 5'UTR and ORF but are polyadenylated 4435 bp from the stop codon. The longer polyadenylated transcripts contain three additional palindromes and at least one additional stem-loop structure with stabilities greater than -16 kcal/mol. | D000544 | Alzheimer Disease |
Clinically important variants in PSEN1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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