##gff-version 3 Q9UGJ0 UniProtKB Chain 1 569 . . . ID=PRO_0000204381;Note=5'-AMP-activated protein kinase subunit gamma-2 Q9UGJ0 UniProtKB Domain 275 335 . . . Note=CBS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 Q9UGJ0 UniProtKB Domain 357 415 . . . Note=CBS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 Q9UGJ0 UniProtKB Domain 430 492 . . . Note=CBS 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 Q9UGJ0 UniProtKB Domain 504 562 . . . Note=CBS 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00703 Q9UGJ0 UniProtKB Region 1 222 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UGJ0 UniProtKB Motif 370 391 . . . Note=AMPK pseudosubstrate Q9UGJ0 UniProtKB Compositional bias 1 17 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UGJ0 UniProtKB Compositional bias 102 175 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UGJ0 UniProtKB Compositional bias 193 217 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UGJ0 UniProtKB Binding site 302 302 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 302 302 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 302 302 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 302 302 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 317 322 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 317 322 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 317 322 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 362 362 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 362 362 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 362 362 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 383 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 383 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 383 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 383 383 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 384 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 402 402 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 402 402 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 402 402 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 432 432 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 458 459 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 474 477 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 474 477 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 474 477 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 501 501 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 501 501 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 501 501 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 530 531 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 530 531 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 530 531 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 530 530 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Binding site 546 549 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P80385 Q9UGJ0 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 71 71 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q9UGJ0 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 138 138 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 143 143 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 165 165 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Modified residue 196 196 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q91WG5 Q9UGJ0 UniProtKB Alternative sequence 1 241 . . . ID=VSP_000261;Note=In isoform B. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11112354,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334,ECO:0000303|Ref.1,ECO:0000303|Ref.5;Dbxref=PMID:11112354,PMID:14702039,PMID:15489334 Q9UGJ0 UniProtKB Alternative sequence 1 44 . . . ID=VSP_015589;Note=In isoform C. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9UGJ0 UniProtKB Natural variant 6 6 . . . ID=VAR_048250;Note=M->L;Dbxref=dbSNP:rs3207363 Q9UGJ0 UniProtKB Natural variant 302 302 . . . ID=VAR_013264;Note=In WPW and CMH6%3B impaired AMP- and ATP-binding. R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11407343,ECO:0000269|PubMed:11827995,ECO:0000269|PubMed:14722619;Dbxref=dbSNP:rs121908987,PMID:11407343,PMID:11827995,PMID:14722619 Q9UGJ0 UniProtKB Natural variant 350 350 . . . ID=VAR_013265;Note=In CMH6%3B severe. R->RL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11371514;Dbxref=PMID:11371514 Q9UGJ0 UniProtKB Natural variant 383 383 . . . ID=VAR_013266;Note=In CMH6%3B severe%3B impaired AMP- and ATP-binding. H->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11371514,ECO:0000269|PubMed:14722619;Dbxref=dbSNP:rs121908988,PMID:11371514,PMID:14722619 Q9UGJ0 UniProtKB Natural variant 400 400 . . . ID=VAR_013267;Note=In CMH6%3B severe%3B impaired AMP- and ATP-binding. T->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11827995,ECO:0000269|PubMed:14722619;Dbxref=dbSNP:rs28938173,PMID:11827995,PMID:14722619 Q9UGJ0 UniProtKB Natural variant 488 488 . . . ID=VAR_013268;Note=In CMH6%3B severe. N->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11827995;Dbxref=dbSNP:rs121908989,PMID:11827995 Q9UGJ0 UniProtKB Natural variant 531 531 . . . ID=VAR_032909;Note=In WPW%3B absence of cardiac hypertrophy%3B onset in childhood%3B impaired AMP- and ATP-binding. R->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11748095,ECO:0000269|PubMed:14722619;Dbxref=dbSNP:rs121908990,PMID:11748095,PMID:14722619 Q9UGJ0 UniProtKB Natural variant 531 531 . . . ID=VAR_013269;Note=In GSDH%3B reduction of binding affinities for AMP and ATP%3B loss of cooperative binding%3B enhanced basal activity%3B increased phosphorylation of the alpha-subunit. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15877279;Dbxref=dbSNP:rs121908991,PMID:15877279 Q9UGJ0 UniProtKB Mutagenesis 387 387 . . . Note=Induces phosphorylation by AMPK. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17255938;Dbxref=PMID:17255938