##gff-version 3 P63244 UniProtKB Chain 1 317 . . . ID=PRO_0000424480;Note=Small ribosomal subunit protein RACK1 P63244 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B alternate;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.9,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:21406692,PMID:22223895,PMID:22814378 P63244 UniProtKB Chain 2 317 . . . ID=PRO_0000127731;Note=Small ribosomal subunit protein RACK1%2C N-terminally processed P63244 UniProtKB Repeat 13 44 . . . Note=WD 1 P63244 UniProtKB Repeat 61 91 . . . Note=WD 2 P63244 UniProtKB Repeat 103 133 . . . Note=WD 3 P63244 UniProtKB Repeat 146 178 . . . Note=WD 4 P63244 UniProtKB Repeat 190 220 . . . Note=WD 5 P63244 UniProtKB Repeat 231 260 . . . Note=WD 6 P63244 UniProtKB Repeat 281 311 . . . Note=WD 7 P63244 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P63244 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine%3B in Guanine nucleotide-binding protein subunit beta-2-like 1%2C N-terminally processed;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.9,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:21406692,PMID:22223895,PMID:22814378 P63244 UniProtKB Modified residue 6 6 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P63244 UniProtKB Modified residue 10 10 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P63244 UniProtKB Modified residue 52 52 . . . Note=Phosphotyrosine%3B by ABL1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19423701;Dbxref=PMID:19423701 P63244 UniProtKB Modified residue 96 96 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P63244 UniProtKB Modified residue 130 130 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P63244 UniProtKB Modified residue 183 183 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68040 P63244 UniProtKB Modified residue 228 228 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11279199;Dbxref=PMID:11279199 P63244 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:28636603,ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163,PMID:28636603 P63244 UniProtKB Modified residue 277 277 . . . Note=Phosphothreonine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28636603;Dbxref=PMID:28636603 P63244 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28636603;Dbxref=PMID:28636603 P63244 UniProtKB Modified residue 279 279 . . . Note=Phosphoserine%3B by viral VacV B1 kinase;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28636603;Dbxref=PMID:28636603 P63244 UniProtKB Modified residue 316 316 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68040 P63244 UniProtKB Mutagenesis 36 38 . . . Note=In DEmut%3B abolishes association with the ribosome and ability to initiate the ribosome quality control (RQC). RDK->DDE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28132843;Dbxref=PMID:28132843 P63244 UniProtKB Mutagenesis 52 52 . . . Note=No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005,ECO:0000269|PubMed:19423701;Dbxref=PMID:11279199,PMID:12400005,PMID:19423701 P63244 UniProtKB Mutagenesis 57 57 . . . Note=Decreased binding to PTK2/FAK1%3B when associated with A-60. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19423701;Dbxref=PMID:19423701 P63244 UniProtKB Mutagenesis 60 60 . . . Note=Decreased binding to PTK2/FAK1%3B when associated with A-57. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19423701;Dbxref=PMID:19423701 P63244 UniProtKB Mutagenesis 127 127 . . . Note=Decreased binding to PTK2/FAK1%3B when associated with A-130. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19423701;Dbxref=PMID:19423701 P63244 UniProtKB Mutagenesis 130 130 . . . Note=Decreased binding to PTK2/FAK1%3B when associated with A-127. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19423701;Dbxref=PMID:19423701 P63244 UniProtKB Mutagenesis 140 140 . . . Note=No effect on binding to SRC. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005;Dbxref=PMID:11279199,PMID:12400005 P63244 UniProtKB Mutagenesis 194 194 . . . Note=No effect on binding to SRC. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005;Dbxref=PMID:11279199,PMID:12400005 P63244 UniProtKB Mutagenesis 228 228 . . . Note=No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC%3B when associated with F-246 and F-302. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005;Dbxref=PMID:11279199,PMID:12400005 P63244 UniProtKB Mutagenesis 246 246 . . . Note=Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC%3B when associated with F-228 and F-302. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005;Dbxref=PMID:11279199,PMID:12400005 P63244 UniProtKB Mutagenesis 276 279 . . . Note=Enhanced translation of mRNAs containing poly-A leaders. STSS->EEEE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28636603;Dbxref=PMID:28636603 P63244 UniProtKB Mutagenesis 278 278 . . . Note=Enhanced translation of mRNAs containing poly-A leaders. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28636603;Dbxref=PMID:28636603 P63244 UniProtKB Mutagenesis 302 302 . . . Note=No effect on binding to SRC. Abolishes phosphorylation by SRC%3B when associated with F-228 and F-246. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11279199,ECO:0000269|PubMed:12400005;Dbxref=PMID:11279199,PMID:12400005 P63244 UniProtKB Sequence conflict 70 111 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P63244 UniProtKB Sequence conflict 94 94 . . . Note=T->TRK;Ontology_term=ECO:0000305;evidence=ECO:0000305 P63244 UniProtKB Sequence conflict 221 221 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P63244 UniProtKB Beta strand 4 11 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 18 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 25 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZV6 P63244 UniProtKB Beta strand 30 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZXH P63244 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 48 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOW P63244 UniProtKB Beta strand 52 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 66 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 75 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 83 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZV6 P63244 UniProtKB Beta strand 87 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Turn 92 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 96 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 108 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 115 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZXG P63244 UniProtKB Beta strand 120 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 129 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 134 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZLW P63244 UniProtKB Beta strand 138 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 144 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4AOW P63244 UniProtKB Beta strand 151 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 160 162 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 164 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 170 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ZXE P63244 UniProtKB Beta strand 174 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Turn 179 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 184 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 195 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7TQL P63244 UniProtKB Beta strand 207 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 215 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Turn 221 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 225 231 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 236 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 243 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 255 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Turn 261 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 265 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 286 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 293 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X P63244 UniProtKB Beta strand 307 313 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7R4X