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 |
Q9BQ51 | 120 | 210 | 121 | 211 | Alternative sequence | ID=VSP_013740;Note=In isoform 2. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQS->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 121 | 182 | Alternative sequence | ID=VSP_013738;Note=In isoform 3. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRL->DGTQDPSNLAASHFHPLLHHCFHFHSHSDSPKKTTLSKAVFFKRHNKKTCHHNKEGSEQCYL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 183 | 273 | Alternative sequence | ID=VSP_013739;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 20 | 273 | Chain | ID=PRO_0000014555;Note=Programmed cell death 1 ligand 2 |
Q9BQ51 | 120 | 210 | 143 | 192 | Disulfide bond | Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 |
Q9BQ51 | 120 | 210 | 122 | 203 | Domain | Note=Ig-like C2-type |
Q9BQ51 | 120 | 210 | 157 | 157 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 163 | 163 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 189 | 189 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 20 | 220 | Topological domain | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 121 | 211 | Alternative sequence | ID=VSP_013740;Note=In isoform 2. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQS->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 210 | 255 | 183 | 273 | Alternative sequence | ID=VSP_013739;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 210 | 255 | 20 | 273 | Chain | ID=PRO_0000014555;Note=Programmed cell death 1 ligand 2 |
Q9BQ51 | 210 | 255 | 229 | 229 | Natural variant | ID=VAR_022449;Note=F->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11224527,ECO:0000269|PubMed:11283156,ECO:0000269|PubMed:15253154,ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs7854303,PMID:11224527,PMID:112831 |
Q9BQ51 | 210 | 255 | 241 | 241 | Natural variant | ID=VAR_049843;Note=I->T;Dbxref=dbSNP:rs7854413 |
Q9BQ51 | 210 | 255 | 20 | 220 | Topological domain | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 242 | 273 | Topological domain | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 221 | 241 | Transmembrane | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
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 |
Q9BQ51 | 120 | 210 | 121 | 211 | Alternative sequence | ID=VSP_013740;Note=In isoform 2. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQS->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 121 | 182 | Alternative sequence | ID=VSP_013738;Note=In isoform 3. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRL->DGTQDPSNLAASHFHPLLHHCFHFHSHSDSPKKTTLSKAVFFKRHNKKTCHHNKEGSEQCYL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 183 | 273 | Alternative sequence | ID=VSP_013739;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 120 | 210 | 20 | 273 | Chain | ID=PRO_0000014555;Note=Programmed cell death 1 ligand 2 |
Q9BQ51 | 120 | 210 | 143 | 192 | Disulfide bond | Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114 |
Q9BQ51 | 120 | 210 | 122 | 203 | Domain | Note=Ig-like C2-type |
Q9BQ51 | 120 | 210 | 157 | 157 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 163 | 163 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 189 | 189 | Glycosylation | Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 120 | 210 | 20 | 220 | Topological domain | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 121 | 211 | Alternative sequence | ID=VSP_013740;Note=In isoform 2. ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQS->G;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 210 | 255 | 183 | 273 | Alternative sequence | ID=VSP_013739;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15253154;Dbxref=PMID:15253154 |
Q9BQ51 | 210 | 255 | 20 | 273 | Chain | ID=PRO_0000014555;Note=Programmed cell death 1 ligand 2 |
Q9BQ51 | 210 | 255 | 229 | 229 | Natural variant | ID=VAR_022449;Note=F->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11224527,ECO:0000269|PubMed:11283156,ECO:0000269|PubMed:15253154,ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs7854303,PMID:11224527,PMID:112831 |
Q9BQ51 | 210 | 255 | 241 | 241 | Natural variant | ID=VAR_049843;Note=I->T;Dbxref=dbSNP:rs7854413 |
Q9BQ51 | 210 | 255 | 20 | 220 | Topological domain | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 242 | 273 | Topological domain | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
Q9BQ51 | 210 | 255 | 221 | 241 | Transmembrane | Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 |