| 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 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| 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 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 1 | 62 | Alternative sequence | ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 6 | 15 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 17 | 19 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 22 | 30 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 33 | 40 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 52 | 56 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 53 | 53 | Binding site | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 5 | 108 | Domain | Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 45 | 48 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1UNQ |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Modified residue | Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 17 | 17 | Mutagenesis | Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 20 | 20 | Mutagenesis | Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 25 | 25 | Mutagenesis | Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 17 | 17 | Natural variant | ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 25 | 25 | Natural variant | ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 14 | 19 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 15 | 58 | 23 | 25 | Region | Note=Inositol-(1%2C3%2C4%2C5)-tetrakisphosphate binding |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 150 | 158 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 160 | 169 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 175 | 182 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 161 | 161 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 179 | 179 | Binding site | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 147 | 149 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 183 | 188 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Modified residue | Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 176 | 176 | Mutagenesis | Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 167 | 167 | Natural variant | ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 156 | 164 | Nucleotide binding | Note=ATP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 173 | 174 | Sequence conflict | Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 145 | 189 | 170 | 172 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 213 | 218 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 220 | 227 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 230 | 230 | Binding site | Note=Inhibitor%3B via amide nitrogen |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 228 | 230 | Region | Note=Inhibitor binding |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 211 | 234 | 212 | 212 | Sequence conflict | Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 274 | 274 | Active site | Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 234 | 234 | Binding site | Note=Inhibitor |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 1 | 480 | Chain | ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 150 | 408 | Domain | Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 235 | 242 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 247 | 268 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:4GV1 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| P31749 | 234 | 276 | 246 | 246 | Sequence conflict | Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
| Depth of coverage in three exons | Mutation description |
 | Sample: TCGA-DD-A1EG-01 |
| Cancer type: LIHC |
| ESID: exon_skip_116330 |
| Skipped exon start: 105239215 |
| Skipped exon end: 105239429 |
| Mutation start: 105239385 |
| Mutation end: 105239385 |
| Mutation type: Frame_Shift_Del |
| Reference seq: C |
| Mutation seq: - |
| AAchange: p.G334fs |
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