| Exon skip ID | chr | Exons involved in exon skipping | Skipped exon | ENSG | ENSTs |
| exon_skip_324963 | 2 | 37571870:37571994:37586722:37587001:37594374:37594551 | 37586722:37587001 | ENSG00000115828.11 | ENST00000537448.1,ENST00000404976.1 |
| exon_skip_324965 | 2 | 37579931:37580078:37585963:37586031:37586722:37587001 | 37585963:37586031 | ENSG00000115828.11 | ENST00000470075.1 |
| exon_skip_324967 | 2 | 37579931:37580078:37586722:37587001:37594374:37594551 | 37586722:37587001 | ENSG00000115828.11 | ENST00000338415.3 |
| exon_skip_324971 | 2 | 37586722:37587001:37594374:37594551:37596827:37596845 | 37594374:37594551 | ENSG00000115828.11 | ENST00000537448.1,ENST00000404976.1,ENST00000338415.3,ENST00000480050.1 |
| exon_skip_324974 | 2 | 37596827:37596927:37599498:37599615:37599824:37599885 | 37599498:37599615 | ENSG00000115828.11 | ENST00000469098.1,ENST00000537448.1,ENST00000404976.1,ENST00000338415.3,ENST00000444022.1 |
| Exon skip ID | chr | Exons involved in exon skipping | Skipped exon | ENSG | ENSTs |
| exon_skip_324963 | 2 | 37571870:37571994:37586722:37587001:37594374:37594551 | 37586722:37587001 | ENSG00000115828.11 | ENST00000404976.1,ENST00000537448.1 |
| exon_skip_324965 | 2 | 37579931:37580078:37585963:37586031:37586722:37587001 | 37585963:37586031 | ENSG00000115828.11 | ENST00000470075.1 |
| exon_skip_324967 | 2 | 37579931:37580078:37586722:37587001:37594374:37594551 | 37586722:37587001 | ENSG00000115828.11 | ENST00000338415.3 |
| exon_skip_324971 | 2 | 37586722:37587001:37594374:37594551:37596827:37596845 | 37594374:37594551 | ENSG00000115828.11 | ENST00000338415.3,ENST00000404976.1,ENST00000537448.1,ENST00000480050.1 |
| exon_skip_324974 | 2 | 37596827:37596927:37599498:37599615:37599824:37599885 | 37599498:37599615 | ENSG00000115828.11 | ENST00000338415.3,ENST00000404976.1,ENST00000537448.1,ENST00000469098.1,ENST00000444022.1 |
| UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
| Q16769 | 89 | 182 | 41 | 89 | Alternative sequence | ID=VSP_038487;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| Q16769 | 89 | 182 | 98 | 100 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 103 | 111 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 116 | 128 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 131 | 140 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 89 | 182 | 139 | 164 | Disulfide bond | Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21671571;Dbxref=PMID:21671571 |
| Q16769 | 89 | 182 | 82 | 96 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 149 | 151 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBB |
| Q16769 | 89 | 182 | 161 | 173 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 175 | 179 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 180 | 182 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YWY |
| Q16769 | 89 | 182 | 159 | 159 | Metal binding | Note=Zinc%3B catalytic |
| Q16769 | 89 | 182 | 144 | 144 | Mutagenesis | Note=Lowers activity by approximately 40%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 89 | 182 | 146 | 146 | Mutagenesis | Note=Lowers activity by approximately 30%25. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 89 | 182 | 160 | 160 | Mutagenesis | Note=Reduces activity by about 50%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 89 | 182 | 160 | 160 | Mutagenesis | Note=Reduces activity by 96%25. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 89 | 182 | 157 | 160 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 201 | 201 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 182 | 241 | 191 | 199 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 204 | 206 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 209 | 212 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 226 | 229 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 241 | 247 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 182 | 241 | 180 | 182 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YWY |
| Q16769 | 182 | 241 | 214 | 224 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 202 | 202 | Metal binding | Note=Zinc%3B catalytic |
| Q16769 | 182 | 241 | 201 | 201 | Mutagenesis | Note=Reduces activity by about 98%25. E->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 182 | 241 | 201 | 201 | Mutagenesis | Note=Abolishes activity. E->L%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 182 | 241 | 207 | 207 | Mutagenesis | Note=Greatly lowers activity. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 182 | 241 | 237 | 240 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 284 | 286 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 293 | 295 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBB |
| Q16769 | 274 | 313 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 274 | 313 | 296 | 296 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
| Q16769 | 274 | 313 | 265 | 280 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 308 | 311 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 304 | 304 | Mutagenesis | Note=Lowers activity by approximately 35%25. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 274 | 313 | 305 | 305 | Mutagenesis | Note=Abolishes activity. D->A%2CE%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 274 | 313 | 305 | 305 | Mutagenesis | Note=Reduces activity by 99%25. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 274 | 313 | 312 | 314 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
| Q16769 | 89 | 182 | 41 | 89 | Alternative sequence | ID=VSP_038487;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| Q16769 | 89 | 182 | 98 | 100 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 103 | 111 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 116 | 128 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 131 | 140 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 89 | 182 | 139 | 164 | Disulfide bond | Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21671571;Dbxref=PMID:21671571 |
| Q16769 | 89 | 182 | 82 | 96 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 149 | 151 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBB |
| Q16769 | 89 | 182 | 161 | 173 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 175 | 179 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 89 | 182 | 180 | 182 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YWY |
| Q16769 | 89 | 182 | 159 | 159 | Metal binding | Note=Zinc%3B catalytic |
| Q16769 | 89 | 182 | 144 | 144 | Mutagenesis | Note=Lowers activity by approximately 40%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 89 | 182 | 146 | 146 | Mutagenesis | Note=Lowers activity by approximately 30%25. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 89 | 182 | 160 | 160 | Mutagenesis | Note=Reduces activity by about 50%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 89 | 182 | 160 | 160 | Mutagenesis | Note=Reduces activity by 96%25. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 89 | 182 | 157 | 160 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 201 | 201 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18072935;Dbxref=PMID:18072935 |
| Q16769 | 182 | 241 | 191 | 199 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 204 | 206 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 209 | 212 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 226 | 229 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 241 | 247 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 182 | 241 | 180 | 182 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4YWY |
| Q16769 | 182 | 241 | 214 | 224 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 182 | 241 | 202 | 202 | Metal binding | Note=Zinc%3B catalytic |
| Q16769 | 182 | 241 | 201 | 201 | Mutagenesis | Note=Reduces activity by about 98%25. E->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 182 | 241 | 201 | 201 | Mutagenesis | Note=Abolishes activity. E->L%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 182 | 241 | 207 | 207 | Mutagenesis | Note=Greatly lowers activity. W->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 182 | 241 | 237 | 240 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 284 | 286 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 293 | 295 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:3PBB |
| Q16769 | 274 | 313 | 29 | 361 | Chain | ID=PRO_0000022195;Note=Glutaminyl-peptide cyclotransferase |
| Q16769 | 274 | 313 | 296 | 296 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
| Q16769 | 274 | 313 | 265 | 280 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 308 | 311 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |
| Q16769 | 274 | 313 | 304 | 304 | Mutagenesis | Note=Lowers activity by approximately 35%25. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16135565;Dbxref=PMID:16135565 |
| Q16769 | 274 | 313 | 305 | 305 | Mutagenesis | Note=Abolishes activity. D->A%2CE%2CL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 274 | 313 | 305 | 305 | Mutagenesis | Note=Reduces activity by 99%25. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16135565,ECO:0000269|PubMed:18072935;Dbxref=PMID:16135565,PMID:18072935 |
| Q16769 | 274 | 313 | 312 | 314 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:2AFW |