##gff-version 3 P60484 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P60484 UniProtKB Chain 2 403 . . . ID=PRO_0000215904;Note=Phosphatidylinositol 3%2C4%2C5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN P60484 UniProtKB Domain 14 185 . . . Note=Phosphatase tensin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590 P60484 UniProtKB Domain 190 350 . . . Note=C2 tensin-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00589 P60484 UniProtKB Region 338 348 . . . Note=Required for interaction with NOP53;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15355975;Dbxref=PMID:15355975 P60484 UniProtKB Region 352 403 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P60484 UniProtKB Motif 401 403 . . . Note=PDZ domain-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08586 P60484 UniProtKB Compositional bias 353 370 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P60484 UniProtKB Compositional bias 371 385 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P60484 UniProtKB Active site 124 124 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00590 P60484 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P60484 UniProtKB Modified residue 294 294 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O08586 P60484 UniProtKB Modified residue 319 319 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Modified residue 321 321 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Modified residue 336 336 . . . Note=Phosphotyrosine%3B by FRK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19345329;Dbxref=PMID:19345329 P60484 UniProtKB Modified residue 366 366 . . . Note=Phosphothreonine%3B by GSK3-beta and PLK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12297295,ECO:0000269|PubMed:20940307,ECO:0007744|PubMed:24275569;Dbxref=PMID:12297295,PMID:20940307,PMID:24275569 P60484 UniProtKB Modified residue 370 370 . . . Note=Phosphoserine%3B by CK2 and PLK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11035045,ECO:0000269|PubMed:12297295,ECO:0000269|PubMed:20940307;Dbxref=PMID:11035045,PMID:12297295,PMID:20940307 P60484 UniProtKB Modified residue 380 380 . . . Note=Phosphoserine%3B by ROCK1 and CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11035045;Dbxref=PMID:11035045 P60484 UniProtKB Modified residue 382 382 . . . Note=Phosphothreonine%3B by ROCK1 and CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11035045;Dbxref=PMID:11035045 P60484 UniProtKB Modified residue 383 383 . . . Note=Phosphothreonine%3B by ROCK1 and CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11035045;Dbxref=PMID:11035045 P60484 UniProtKB Modified residue 385 385 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11035045,ECO:0000269|PubMed:12297295;Dbxref=PMID:11035045,PMID:12297295 P60484 UniProtKB Modified residue 401 401 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10646847;Dbxref=PMID:10646847 P60484 UniProtKB Cross-link 13 13 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716620;Dbxref=PMID:18716620 P60484 UniProtKB Cross-link 289 289 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716620;Dbxref=PMID:18716620 P60484 UniProtKB Alternative sequence 1 1 . . . ID=VSP_055420;Note=In isoform alpha. M->MERGGEAAAAAAAAAAAPGRGSESPVTISRAGNAGELVSPLLLPPTRRRRRRHIQGPGPVLNLPSAAAAPPVARAPEAAGGGSRSEDYSSSPHSAAAAARPLAAEEKQAQSLQPSSSRRSSHYPAAVQSQAAAERGASATAKSRAISILQKKPRHQQLLPSLSSFFFSHRLPDM;Ontology_term=ECO:0000305;evidence=ECO:0000305 P60484 UniProtKB Alternative sequence 55 70 . . . ID=VSP_055421;Note=In isoform 3. RFLDSKHKNHYKIYNL->S;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.7 P60484 UniProtKB Alternative sequence 165 190 . . . ID=VSP_055422;Note=In isoform 3. GVTIPSQRRYVYYYSYLLKNHLDYRP->ADPTGGIPDKGIIVIGDGSSMDVIAP;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.7 P60484 UniProtKB Alternative sequence 191 403 . . . ID=VSP_055423;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.7 P60484 UniProtKB Natural variant 10 10 . . . ID=VAR_026248;Note=Retains phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3%3B retains the ability to bind phospholipid membranes. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 15 15 . . . ID=VAR_007457;Note=In glioma. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9090379;Dbxref=dbSNP:rs1064794096,PMID:9090379 P60484 UniProtKB Natural variant 16 16 . . . ID=VAR_026249;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains the ability to bind phospholipid membranes. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 19 19 . . . ID=VAR_018100;Note=In malignant melanoma%3B somatic mutation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10978354;Dbxref=dbSNP:rs121909233,PMID:10978354 P60484 UniProtKB Natural variant 20 20 . . . ID=VAR_026250;Note=Reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains phosphatase activity towards PtdIns(3%2C4%2C5)P3. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs1064795967,PMID:10866302 P60484 UniProtKB Natural variant 27 27 . . . ID=VAR_026251;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs886041877,PMID:10866302 P60484 UniProtKB Natural variant 33 33 . . . ID=VAR_008733;Note=In CWS1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10234502;Dbxref=dbSNP:rs1554893765,PMID:10234502 P60484 UniProtKB Natural variant 34 34 . . . ID=VAR_008734;Note=In CWS1. A->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10400993,ECO:0000269|PubMed:11494117;Dbxref=PMID:10400993,PMID:11494117 P60484 UniProtKB Natural variant 35 35 . . . ID=VAR_008036;Note=In CWS1. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9425889;Dbxref=dbSNP:rs121909225,PMID:9425889 P60484 UniProtKB Natural variant 36 36 . . . ID=VAR_007458;Note=In glioma. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9090379;Dbxref=dbSNP:rs1554893792,PMID:9090379 P60484 UniProtKB Natural variant 36 36 . . . ID=VAR_026252;Note=In endometrial hyperplasia. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9635567;Dbxref=dbSNP:rs786204854,PMID:9635567 P60484 UniProtKB Natural variant 42 42 . . . ID=VAR_007459;Note=In glioma%3B retains phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3%3B retains the ability to bind phospholipid membranes. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9090379;Dbxref=PMID:9090379 P60484 UniProtKB Natural variant 47 47 . . . ID=VAR_011587;Note=In CWS1. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11494117;Dbxref=dbSNP:rs786204855,PMID:11494117 P60484 UniProtKB Natural variant 57 57 . . . ID=VAR_007460;Note=In glioma%3B loss of protein phosphatase activity. L->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9090379,ECO:0000269|PubMed:9256433;Dbxref=dbSNP:rs786202398,PMID:9090379,PMID:9256433 P60484 UniProtKB Natural variant 61 61 . . . ID=VAR_018101;Note=Found in a patient with congenital cardiac disease%2C macrocephaly%2C ventriculomegaly%2C skeletal defects%2C anal atresia%2C tracheoesophageal fistula%2C renal anomalies%3B uncertain significance. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11748304;Dbxref=dbSNP:rs121909236,PMID:11748304 P60484 UniProtKB Natural variant 61 61 . . . ID=VAR_026253;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs398123316,PMID:10866302 P60484 UniProtKB Natural variant 65 403 . . . ID=VAR_078705;Note=In MCEPHAS. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26637798;Dbxref=PMID:26637798 P60484 UniProtKB Natural variant 67 67 . . . ID=VAR_007461;Note=In CWS1. I->R P60484 UniProtKB Natural variant 68 68 . . . ID=VAR_007462;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3%3B retains the ability to bind phospholipid membranes. Y->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10400993,ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:11494117,ECO:0000269|PubMed:9600246;Dbxref=dbSNP:rs398123317,PMID:10400993,PMID:10866302,PMID:11494117,PMID:9600246 P60484 UniProtKB Natural variant 70 70 . . . ID=VAR_018102;Note=In CWS1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9832031;Dbxref=dbSNP:rs121909226,PMID:9832031 P60484 UniProtKB Natural variant 71 71 . . . ID=VAR_026254;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 93 93 . . . ID=VAR_032634;Note=In MCEPHAS. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15805158;Dbxref=dbSNP:rs121909238,PMID:15805158 P60484 UniProtKB Natural variant 93 93 . . . ID=VAR_026255;Note=In CWS1. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs786204927,PMID:10866302 P60484 UniProtKB Natural variant 105 105 . . . ID=VAR_026256;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. C->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 105 105 . . . ID=VAR_008735;Note=In CWS1. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10400993,ECO:0000269|PubMed:11494117;Dbxref=dbSNP:rs587782343,PMID:10400993,PMID:11494117 P60484 UniProtKB Natural variant 107 107 . . . ID=VAR_026257;Note=In CWS1 and glioblastoma%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. D->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9331071;Dbxref=dbSNP:rs57374291,PMID:10866302,PMID:9331071 P60484 UniProtKB Natural variant 112 112 . . . ID=VAR_007807;Note=In CWS1 and LDD%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10051160,ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9600246;Dbxref=dbSNP:rs121909230,PMID:10051160,PMID:10866302,PMID:9600246 P60484 UniProtKB Natural variant 112 112 . . . ID=VAR_026258;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 119 119 . . . ID=VAR_011588;Note=In multiple cancers. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10807691;Dbxref=dbSNP:rs139767111,PMID:10807691 P60484 UniProtKB Natural variant 121 121 . . . ID=VAR_018103;Note=In HNSCC. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11801303;Dbxref=dbSNP:rs121909237,PMID:11801303 P60484 UniProtKB Natural variant 121 121 . . . ID=VAR_026259;Note=In glioblastoma%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9331071;Dbxref=PMID:10866302,PMID:9331071 P60484 UniProtKB Natural variant 123 123 . . . ID=VAR_007463;Note=In CWS1. H->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10234502,ECO:0000269|PubMed:9259288;Dbxref=dbSNP:rs121909222,PMID:10234502,PMID:9259288 P60484 UniProtKB Natural variant 123 123 . . . ID=VAR_026260;Note=In endometrial cancer%3B loss of protein phosphatase activity. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256433;Dbxref=dbSNP:rs786204931,PMID:9256433 P60484 UniProtKB Natural variant 124 124 . . . ID=VAR_007464;Note=In CWS1. C->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10234502,ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9259288;Dbxref=dbSNP:rs121909223,PMID:10234502,PMID:10866302,PMID:9259288 P60484 UniProtKB Natural variant 124 124 . . . ID=VAR_018104;Note=In CWS1%3B phosphatase-dead protein with neither lipid nor protein phosphatase activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11230179,ECO:0000269|PubMed:9811831;Dbxref=dbSNP:rs121909223,PMID:11230179,PMID:9811831 P60484 UniProtKB Natural variant 126 126 . . . ID=VAR_076551;Note=In a patient with prostate cancer%3B reduced phosphatase activity towards PtdIns(3%2C4%2C5)%3B shifts its activity from phosphatidylinositol phosphate 3-phosphatase to phosphatidylinositol phosphate 5-phosphatase%3B disrupts PI3K/ATK signaling%3B reduced cell migration. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26504226;Dbxref=PMID:26504226 P60484 UniProtKB Natural variant 129 129 . . . ID=VAR_007465;Note=In CWS1%3B no lipid phosphatase activity but retains protein phosphatase activity%3B retains ability to inhibit focal adhesion formation. G->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:11230179,ECO:0000269|PubMed:9140396,ECO:0000269|PubMed:9616126,ECO:0000269|PubMed:9811831;Dbxref=dbSNP:rs121909218,PMID:10866302,PMID:11230179,PMID:9140396,PMID:9616126,PMID:9811831 P60484 UniProtKB Natural variant 129 129 . . . ID=VAR_007466;Note=In glioblastoma%3B severely reduced protein phosphatase activity%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9072974,ECO:0000269|PubMed:9256433,ECO:0000269|PubMed:9331071;Dbxref=dbSNP:rs786204929,PMID:10866302,PMID:9072974,PMID:9256433,PMID:9331071 P60484 UniProtKB Natural variant 130 130 . . . ID=VAR_026261;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs121909224,PMID:10866302 P60484 UniProtKB Natural variant 130 130 . . . ID=VAR_007467;Note=In CWS1 and endometrial hyperplasia%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. R->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9635567;Dbxref=dbSNP:rs121909229,PMID:10866302,PMID:9635567 P60484 UniProtKB Natural variant 130 130 . . . ID=VAR_007468;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9915974;Dbxref=dbSNP:rs121909229,PMID:10866302,PMID:9915974 P60484 UniProtKB Natural variant 131 131 . . . ID=VAR_076762;Note=In MCEPHAS. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23160955;Dbxref=dbSNP:rs397514560,PMID:23160955 P60484 UniProtKB Natural variant 132 132 . . . ID=VAR_032635;Note=In one patient with clinical findings suggesting hamartoma tumor syndrome. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16752378;Dbxref=dbSNP:rs121909241,PMID:16752378 P60484 UniProtKB Natural variant 133 133 . . . ID=VAR_026262;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P3. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 134 134 . . . ID=VAR_007469;Note=In prostate cancer%3B no effect on protein phosphatase activity%3B reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P3 but retains PtdIns(3%2C4%2C5)P3 phosphatase activity. M->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9072974,ECO:0000269|PubMed:9256433;Dbxref=PMID:10866302,PMID:9072974,PMID:9256433 P60484 UniProtKB Natural variant 135 135 . . . ID=VAR_008736;Note=In CWS1. I->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10400993,ECO:0000269|PubMed:11494117;Dbxref=dbSNP:rs587782360,PMID:10400993,PMID:11494117 P60484 UniProtKB Natural variant 136 136 . . . ID=VAR_007808;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P3. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9735393;Dbxref=dbSNP:rs786204859,PMID:10866302,PMID:9735393 P60484 UniProtKB Natural variant 137 137 . . . ID=VAR_008737;Note=In CWS1. A->AN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9345101;Dbxref=PMID:9345101 P60484 UniProtKB Natural variant 155 155 . . . ID=VAR_026263;Note=In CWS1%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs1060500126,PMID:10866302 P60484 UniProtKB Natural variant 158 158 . . . ID=VAR_011589;Note=In multiple cancers. V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10807691;Dbxref=PMID:10807691 P60484 UniProtKB Natural variant 165 165 . . . ID=VAR_008739;Note=In CWS1. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10234502;Dbxref=PMID:10234502 P60484 UniProtKB Natural variant 165 165 . . . ID=VAR_026264;Note=In glioblastoma%3B severely reduced protein phosphatase activity%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9256433,ECO:0000269|PubMed:9331071;Dbxref=dbSNP:rs587782603,PMID:10866302,PMID:9256433,PMID:9331071 P60484 UniProtKB Natural variant 165 165 . . . ID=VAR_008738;Note=In CWS1. G->V;Dbxref=dbSNP:rs786204863 P60484 UniProtKB Natural variant 167 167 . . . ID=VAR_076763;Note=In MCEPHAS. T->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23160955;Dbxref=dbSNP:rs397514559,PMID:23160955 P60484 UniProtKB Natural variant 167 167 . . . ID=VAR_026265;Note=In breast cancer%3B severely reduced protein phosphatase activity. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9256433;Dbxref=PMID:9256433 P60484 UniProtKB Natural variant 170 170 . . . ID=VAR_026266;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 170 170 . . . ID=VAR_007470;Note=In CWS1%3B severely reduced protein phosphatase activity%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. S->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10400993,ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:11494117,ECO:0000269|PubMed:9241266,ECO:0000269|PubMed:9256433;Dbxref=dbSNP:rs121909221,PMID:10400993,PMID:10866302,PMID:11494117,PMID:9241266,PMID:9256433 P60484 UniProtKB Natural variant 173 173 . . . ID=VAR_026267;Note=In endometrial hyperplasia%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3%3B retains ability to bind phospholipid membranes. R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9635567;Dbxref=dbSNP:rs121913293,PMID:10866302,PMID:9635567 P60484 UniProtKB Natural variant 173 173 . . . ID=VAR_026268;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs121913294,PMID:10866302 P60484 UniProtKB Natural variant 173 173 . . . ID=VAR_026269;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs121913294,PMID:10866302 P60484 UniProtKB Natural variant 174 174 . . . ID=VAR_026270;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs587782316,PMID:10866302 P60484 UniProtKB Natural variant 191 191 . . . ID=VAR_026271;Note=In endometrial hyperplasia. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9635567;Dbxref=PMID:9635567 P60484 UniProtKB Natural variant 217 217 . . . ID=VAR_018105;Note=In malignant melanoma%3B somatic mutation. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10978354;Dbxref=dbSNP:rs121909234,PMID:10978354 P60484 UniProtKB Natural variant 227 227 . . . ID=VAR_026272;Note=Reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains PtdIns(3%2C4%2C5)P3 phosphatase activity. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs905615413,PMID:10866302 P60484 UniProtKB Natural variant 234 234 . . . ID=VAR_018106;Note=In GLM2%3B not capable of inducing apoptosis%3B induced increased cell proliferation%3B led to high constitutive AKT1 activation which could not be increased further by stimulation with insulin. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12085208;Dbxref=dbSNP:rs121909235,PMID:12085208 P60484 UniProtKB Natural variant 241 241 . . . ID=VAR_032636;Note=In MCEPHAS. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15805158;Dbxref=dbSNP:rs121909240,PMID:15805158 P60484 UniProtKB Natural variant 246 246 . . . ID=VAR_008740;Note=In CWS1. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10400993;Dbxref=dbSNP:rs587782350,PMID:10400993 P60484 UniProtKB Natural variant 251 251 . . . ID=VAR_026273;Note=Loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 252 252 . . . ID=VAR_032637;Note=In MCEPHAS. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15805158;Dbxref=dbSNP:rs121909239,PMID:15805158 P60484 UniProtKB Natural variant 289 289 . . . ID=VAR_008741;Note=In CWS1%3B reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes%3B predominantly nuclear. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:18716620,ECO:0000269|PubMed:9797362;Dbxref=dbSNP:rs562015640,PMID:10866302,PMID:18716620,PMID:9797362 P60484 UniProtKB Natural variant 290 290 . . . ID=VAR_025167;Note=V->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.10;Dbxref=dbSNP:rs35600253 P60484 UniProtKB Natural variant 319 319 . . . ID=VAR_026274;Note=In glioma%3B reduced tumor suppressor activity%3B fails to inactivate AKT/PKB. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10468583,ECO:0000269|PubMed:9090379;Dbxref=PMID:10468583,PMID:9090379 P60484 UniProtKB Natural variant 331 331 . . . ID=VAR_026275;Note=In CWS1%3B reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B retains ability to bind phospholipid membranes. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 341 341 . . . ID=VAR_026276;Note=In CWS1%3B loss of interaction with NOP53%3B decreased phosphorylation at S-380%3B decreased stability%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. F->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:15355975;Dbxref=dbSNP:rs1554825652,PMID:10866302,PMID:15355975 P60484 UniProtKB Natural variant 342 342 . . . ID=VAR_026277;Note=In CWS1%3B reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4 but PtdIns(3%2C4%2C5)P3 phosphatase activity is similar to wild-type. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=dbSNP:rs398123314,PMID:10866302 P60484 UniProtKB Natural variant 343 343 . . . ID=VAR_008742;Note=In CWS1%3B loss of interaction with NOP53%3B decreased phosphorylation at S-380%3B decreased stability%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. V->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:15355975,ECO:0000269|PubMed:9399897;Dbxref=PMID:10866302,PMID:15355975,PMID:9399897 P60484 UniProtKB Natural variant 345 345 . . . ID=VAR_026278;Note=In glioblastoma%3B reduced tumor suppressor activity%3B loss of interaction with NOP53%3B decreased phosphorylation at S-380%3B decreased stability%3B loss of phosphatase activity towards Ins(1%2C3%2C4%2C5)P4%3B reduced ability to inactivate AKT/PKB%3B retains ability to bind phospholipid membranes. L->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10468583,ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:15355975,ECO:0000269|PubMed:9331071;Dbxref=PMID:10468583,PMID:10866302,PMID:15355975,PMID:9331071 P60484 UniProtKB Natural variant 347 347 . . . ID=VAR_008743;Note=In CWS1%3B reduced phosphatase activity towards Ins(1%2C3%2C4%2C5)P4. F->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10866302,ECO:0000269|PubMed:9399897;Dbxref=PMID:10866302,PMID:9399897 P60484 UniProtKB Natural variant 348 348 . . . ID=VAR_026279;Note=In endometrial hyperplasia%3B reduced phosphatase activity towards PtdIns(3%2C4%2C5)P3%3B mildly reduced tumor suppressor activity%3B reduced ability to inactivate AKT/PKB. T->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10468583,ECO:0000269|PubMed:9635567;Dbxref=PMID:10468583,PMID:9635567 P60484 UniProtKB Natural variant 369 369 . . . ID=VAR_026280;Note=Retains Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3 phosphatase activity%3B retains ability to bind phospholipid membranes. V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Natural variant 401 401 . . . ID=VAR_026281;Note=Retains Ins(1%2C3%2C4%2C5)P4 and PtdIns(3%2C4%2C5)P3 phosphatase activity%3B retains ability to bind phospholipid membranes. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10866302;Dbxref=PMID:10866302 P60484 UniProtKB Mutagenesis 1 1 . . . Note=Prevents expression of isoform 1 and increased expression of isoform alpha. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24768297;Dbxref=PMID:24768297 P60484 UniProtKB Mutagenesis 13 13 . . . Note=Nuclear. Cytoplasmic%3B when associated with E-289. Shows less tumor suppressive ability%3B when associated with E-289. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716620;Dbxref=PMID:18716620 P60484 UniProtKB Mutagenesis 92 92 . . . Note=700-fold reduction in phosphatase activity towards PtdIns(3%2C4%2C5)P3. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10555148,ECO:0000269|PubMed:9616126;Dbxref=PMID:10555148,PMID:9616126 P60484 UniProtKB Mutagenesis 93 93 . . . Note=75%25 reduction in phosphatase activity towards PtdIns(3%2C4%2C5)P3. Modest reduction in phosphatase activity towards PtdIns(3%2C4)P2. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 124 124 . . . Note=Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9616126;Dbxref=PMID:9616126 P60484 UniProtKB Mutagenesis 124 124 . . . Note=Loss of phosphatidylinositol-3%2C4%2C5-trisphosphate 3-phosphatase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9593664;Dbxref=PMID:9593664 P60484 UniProtKB Mutagenesis 125 125 . . . Note=Reduced phosphatase activity towards PtdIns(3%2C4%2C5)P3%2C PtdIns(3%2C4)P2 and PtdIns(3)P. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 126 126 . . . Note=Does not reduce phosphatase activity towards PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26504226;Dbxref=PMID:26504226 P60484 UniProtKB Mutagenesis 126 126 . . . Note=Does not reduce phosphatase activity towards PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26504226;Dbxref=PMID:26504226 P60484 UniProtKB Mutagenesis 126 126 . . . Note=Does not reduce phosphatase activity towards PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26504226;Dbxref=PMID:26504226 P60484 UniProtKB Mutagenesis 128 128 . . . Note=85%25 reduction in phosphatase activity towards PtdIns(3%2C4%2C5)P3. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 128 128 . . . Note=Does not reduce phosphatase activity towards PtdIns(3%2C4%2C5)P3. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 130 130 . . . Note=Does not affect the ability to inhibit AKT/PKB activation. R->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9811831;Dbxref=PMID:9811831 P60484 UniProtKB Mutagenesis 167 167 . . . Note=60%25 reduction in phosphatase activity towards PtdIns(3%2C4%2C5)P3. T->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 171 171 . . . Note=75%25 reduction in phosphatase activity towards PtdIns(3%2C4%2C5)P3. Q->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 229 229 . . . Note=No effect on interaction with DLC1 or p85. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 232 232 . . . Note=No effect on interaction with DLC1 or p85. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 263 269 . . . Note=Reduces the growth suppression activity and cells show anchorage-independent growth. Reduces binding to phospholipid membranes in vitro. Phosphatase activity towards PtdIns(3%2C4%2C5)P3 is not affected. KMLKKDK->AAGAADA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 289 289 . . . Note=Cytoplasmic%3B when associated with E-13. Shows less tumor suppressive ability%3B when associated with E-13. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18716620;Dbxref=PMID:18716620 P60484 UniProtKB Mutagenesis 319 319 . . . Note=Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain%3B when associated with A-321. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 319 319 . . . Note=Constitutive interaction with DLC1. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 319 319 . . . Note=Constitutive interaction with DLC1 and interaction with p85 following EGF stimulation. T->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 321 321 . . . Note=Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain%3B when associated with A-319. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 321 321 . . . Note=Constitutive interaction with DLC1. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26166433;Dbxref=PMID:26166433 P60484 UniProtKB Mutagenesis 327 335 . . . Note=Reduces growth suppression activity and promotes anchorage-independent growth. Reduces binding to phospholipid membranes in vitro%3B phosphatase activity towards PtdIns(3%2C4%2C5)P3 is not affected. KANKDKANR->AAGADAANA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10555148;Dbxref=PMID:10555148 P60484 UniProtKB Mutagenesis 336 336 . . . Note=Significantly lower phosphatase activity%2C reduced protein stability and decreased growth-inhibitory effect. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19345329;Dbxref=PMID:19345329 P60484 UniProtKB Mutagenesis 366 366 . . . Note=Decreased stability. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20940307;Dbxref=PMID:20940307 P60484 UniProtKB Mutagenesis 370 370 . . . Note=Decreased stability. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20940307;Dbxref=PMID:20940307 P60484 UniProtKB Mutagenesis 401 401 . . . Note=Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding. T->A P60484 UniProtKB Mutagenesis 402 402 . . . Note=No effect on MAGI2-%2C MAST2- and DLG1-binding. K->A P60484 UniProtKB Mutagenesis 402 402 . . . Note=Loss of DLG1-%2C MAGI2-%2C MAGI3- and MAST2-binding. Decrease of protein stability. K->W P60484 UniProtKB Mutagenesis 403 403 . . . Note=Loss of DLG1-%2C MAGI2-%2C MAGI3-%2C MAST1-%2C MAST2- and MAST3-binding. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15951562;Dbxref=PMID:15951562 P60484 UniProtKB Helix 8 10 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7JUL P60484 UniProtKB Turn 19 22 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 23 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 32 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 44 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Helix 50 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 61 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 65 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 78 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Beta strand 85 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 98 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 101 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 118 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 129 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 148 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 169 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 192 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 206 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Beta strand 213 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 222 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 238 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 262 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Beta strand 268 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 280 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZZ P60484 UniProtKB Beta strand 310 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5BZX P60484 UniProtKB Beta strand 315 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Helix 328 330 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 335 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 342 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1D5R P60484 UniProtKB Beta strand 395 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KYL