1KHX
Crystal structure of a phosphorylated Smad2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:12193595 |
Chain | Residue | Details |
A | SER245 | |
A | SER250 | |
A | SER255 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER458 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER460 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000255|PROSITE-ProRule:PRU00439, ECO:0000269|PubMed:8980228 |
Chain | Residue | Details |
A | SER464 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by TGFBR1 => ECO:0000255|PROSITE-ProRule:PRU00439, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:8980228, ECO:0000269|PubMed:9136927, ECO:0000269|PubMed:9346908 |
Chain | Residue | Details |
A | SEP465 | |
A | SEP467 |