##gff-version 3 P15941 UniProtKB Signal peptide 1 23 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10373415,ECO:0000269|PubMed:11341784;Dbxref=PMID:10373415,PMID:11341784 P15941 UniProtKB Chain 24 1255 . . . ID=PRO_0000019277;Note=Mucin-1 P15941 UniProtKB Chain 24 1097 . . . ID=PRO_0000317446;Note=Mucin-1 subunit alpha P15941 UniProtKB Chain 1098 1255 . . . ID=PRO_0000317447;Note=Mucin-1 subunit beta P15941 UniProtKB Topological domain 24 1158 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Transmembrane 1159 1181 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Topological domain 1182 1255 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Repeat 61 80 . . . Note=1%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 81 100 . . . Note=2%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 101 120 . . . Note=3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 121 140 . . . Note=4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 141 160 . . . Note=5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 161 180 . . . Note=6;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 181 200 . . . Note=7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 201 220 . . . Note=8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 221 240 . . . Note=9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 241 260 . . . Note=10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 261 280 . . . Note=11;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 281 300 . . . Note=12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 301 320 . . . Note=13;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 321 340 . . . Note=14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 341 360 . . . Note=15;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 361 380 . . . Note=16;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 381 400 . . . Note=17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 401 420 . . . Note=18;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 421 440 . . . Note=19;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 441 460 . . . Note=20;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 461 480 . . . Note=21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 481 500 . . . Note=22;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 501 520 . . . Note=23;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 521 540 . . . Note=24;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 541 560 . . . Note=25;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 561 580 . . . Note=26;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 581 600 . . . Note=27;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 601 620 . . . Note=28;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 621 640 . . . Note=29;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 641 660 . . . Note=30;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 661 680 . . . Note=31;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 681 700 . . . Note=32;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 701 720 . . . Note=33;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 721 740 . . . Note=34;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 741 760 . . . Note=35;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 761 780 . . . Note=36;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 781 800 . . . Note=37;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 801 820 . . . Note=38;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 821 840 . . . Note=39;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 841 860 . . . Note=40;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 861 880 . . . Note=41;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 881 900 . . . Note=42;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 901 920 . . . Note=43;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 921 940 . . . Note=44;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 941 960 . . . Note=45;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 961 980 . . . Note=46%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 981 1000 . . . Note=47%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Repeat 1001 1020 . . . Note=48%3B approximate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11350974;Dbxref=PMID:11350974 P15941 UniProtKB Domain 1039 1148 . . . Note=SEA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00188 P15941 UniProtKB Region 23 1033 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Region 126 965 . . . Note=42 X 20 AA approximate tandem repeats of P-A-P-G-S-T-A-P-P-A-H-G-V-T-S-A-P-D-T-R P15941 UniProtKB Region 1192 1228 . . . Note=Interaction with P53 P15941 UniProtKB Region 1214 1237 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Region 1223 1230 . . . Note=Required for interaction with GSK3B P15941 UniProtKB Region 1233 1241 . . . Note=Required for interaction with beta- and gamma-catenins P15941 UniProtKB Motif 1203 1206 . . . Note=Interaction with GRB2 P15941 UniProtKB Motif 1229 1232 . . . Note=Interaction with SRC and ESR1 P15941 UniProtKB Motif 1243 1246 . . . Note=Required for interaction with AP1S2 P15941 UniProtKB Compositional bias 23 83 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Compositional bias 89 118 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Compositional bias 953 1033 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Compositional bias 1217 1237 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P15941 UniProtKB Site 1097 1098 . . . Note=Cleavage%3B by autolysis P15941 UniProtKB Modified residue 1203 1203 . . . Note=Phosphotyrosine%3B by PDGFR;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14521915,ECO:0000269|PubMed:17545600;Dbxref=PMID:14521915,PMID:17545600 P15941 UniProtKB Modified residue 1212 1212 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14521915;Dbxref=PMID:14521915 P15941 UniProtKB Modified residue 1218 1218 . . . Note=Phosphotyrosine%3B by PDGFR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17545600;Dbxref=PMID:17545600 P15941 UniProtKB Modified residue 1224 1224 . . . Note=Phosphothreonine%3B by PKC/PRKCD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11877440;Dbxref=PMID:11877440 P15941 UniProtKB Modified residue 1227 1227 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:9819408,ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163,PMID:9819408 P15941 UniProtKB Modified residue 1229 1229 . . . Note=Phosphotyrosine%3B by CSK%2C EGFR and SRC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11152665,ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:14521915,ECO:0000269|PubMed:17545600;Dbxref=PMID:11152665,PMID:11483589,PMID:14521915,PMID:17545600 P15941 UniProtKB Modified residue 1243 1243 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14521915;Dbxref=PMID:14521915 P15941 UniProtKB Lipidation 1184 1184 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16507569;Dbxref=PMID:16507569 P15941 UniProtKB Lipidation 1186 1186 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16507569;Dbxref=PMID:16507569 P15941 UniProtKB Glycosylation 131 131 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:7744025,ECO:0000305|PubMed:9597769;Dbxref=PMID:7744025,PMID:9597769 P15941 UniProtKB Glycosylation 139 139 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:7744025,ECO:0000305|PubMed:9597769;Dbxref=PMID:7744025,PMID:9597769 P15941 UniProtKB Glycosylation 140 140 . . . Note=O-linked (GalNAc...) serine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 144 144 . . . Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 957 957 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 975 975 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 1029 1029 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 1055 1055 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Glycosylation 1133 1133 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P15941 UniProtKB Alternative sequence 19 21 . . . ID=VSP_003281;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.25 P15941 UniProtKB Alternative sequence 19 19 . . . ID=VSP_003280;Note=In isoform 2%2C isoform Y-LSP%2C isoform E2%2C isoform J13%2C isoform S2 and isoform T10. T->TATTAPKPAT;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:22941036,ECO:0000303|PubMed:2318825,ECO:0000303|PubMed:2597151,ECO:0000303|PubMed:8608966,ECO:0000303|Ref.15;Dbxref=PMID:15489334,PMID:22941036,PMID:2318825,PMID:2597151,PMID:8608966 P15941 UniProtKB Alternative sequence 20 31 . . . ID=VSP_003282;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.25 P15941 UniProtKB Alternative sequence 54 1151 . . . ID=VSP_047872;Note=In isoform E2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22941036;Dbxref=PMID:22941036 P15941 UniProtKB Alternative sequence 54 1093 . . . ID=VSP_047873;Note=In isoform T10. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22941036;Dbxref=PMID:22941036 P15941 UniProtKB Alternative sequence 54 1053 . . . ID=VSP_003285;Note=In isoform J13%2C isoform Y%2C isoform Y-LSP and isoform S2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:15969018,ECO:0000303|PubMed:22941036,ECO:0000303|PubMed:7925397,ECO:0000303|PubMed:9212228,ECO:0000303|Ref.15;Dbxref=PMID:15489334,PMID:15969018,PMID:22941036,PMID:7925397,PMID:9212228 P15941 UniProtKB Alternative sequence 54 1035 . . . ID=VSP_003286;Note=In isoform 8%2C isoform 9 and isoform M6. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|PubMed:9212228,ECO:0000303|Ref.12,ECO:0000303|Ref.16;Dbxref=PMID:22941036,PMID:9212228 P15941 UniProtKB Alternative sequence 54 96 . . . ID=VSP_047575;Note=In isoform ZD. VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQ->IPAPTTTKSCRETFLKCFCRFINKGVFWASPILSSGQDLWWYN;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15623537,ECO:0000303|PubMed:22941036;Dbxref=PMID:15623537,PMID:22941036 P15941 UniProtKB Alternative sequence 54 87 . . . ID=VSP_035046;Note=In isoform F. VSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPA->IPAPTTTKSCRETFLKCFCRFINKGVFWASPILS;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.14 P15941 UniProtKB Alternative sequence 54 70 . . . ID=VSP_003283;Note=In isoform 6. VSMTSSVLSSHSPGSGS->IPAPTTTKSCRETFLKW;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|PubMed:9212228;Dbxref=PMID:22941036,PMID:9212228 P15941 UniProtKB Alternative sequence 71 1095 . . . ID=VSP_003284;Note=In isoform 6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|PubMed:9212228;Dbxref=PMID:22941036,PMID:9212228 P15941 UniProtKB Alternative sequence 88 1139 . . . ID=VSP_035047;Note=In isoform F. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.14 P15941 UniProtKB Alternative sequence 97 1255 . . . ID=VSP_047576;Note=In isoform ZD. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15623537,ECO:0000303|PubMed:22941036;Dbxref=PMID:15623537,PMID:22941036 P15941 UniProtKB Alternative sequence 1077 1181 . . . ID=VSP_003287;Note=In isoform 9 and isoform S2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|Ref.12,ECO:0000303|Ref.15;Dbxref=PMID:22941036 P15941 UniProtKB Alternative sequence 1077 1087 . . . ID=VSP_003288;Note=In isoform 5. FLQIYKQGGFL->VSIGLSFPMLP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2351132;Dbxref=PMID:2351132 P15941 UniProtKB Alternative sequence 1088 1255 . . . ID=VSP_003289;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2351132;Dbxref=PMID:2351132 P15941 UniProtKB Alternative sequence 1141 1180 . . . ID=VSP_046962;Note=In isoform M6. VSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIA->GCLSVPPKELRAAGHLSSPGYLPSYERVPHLPHPWALCAP;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|Ref.16;Dbxref=PMID:22941036 P15941 UniProtKB Alternative sequence 1181 1255 . . . ID=VSP_046963;Note=In isoform M6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:22941036,ECO:0000303|Ref.16;Dbxref=PMID:22941036 P15941 UniProtKB Alternative sequence 1232 1255 . . . ID=VSP_047874;Note=In isoform J13. VSAGNGGSSLSYTNPAVAATSANL->RQNGWSTMPRGALPEESQG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:22941036;Dbxref=PMID:22941036 P15941 UniProtKB Natural variant 1117 1117 . . . ID=VAR_019390;Note=V->M;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15969018,ECO:0000269|PubMed:22941036,ECO:0000269|Ref.17;Dbxref=dbSNP:rs1611770,PMID:15969018,PMID:22941036 P15941 UniProtKB Natural variant 1142 1142 . . . ID=VAR_019391;Note=S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.17;Dbxref=dbSNP:rs11465207 P15941 UniProtKB Mutagenesis 1098 1098 . . . Note=Completely abrogates cleavage. S->A%2CD%2CE%2CF%2CG%2CH%2CI%2CK%2CL%2CM%2CN%2CP%2CQ%2CR%2CV%2CW%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987679;Dbxref=PMID:15987679 P15941 UniProtKB Mutagenesis 1098 1098 . . . Note=Almost complete cleavage. S->C%2CT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15987679;Dbxref=PMID:15987679 P15941 UniProtKB Mutagenesis 1116 1116 . . . Note=Greatly reduced formation of isoform 5/isoform Y complex. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10197628;Dbxref=PMID:10197628 P15941 UniProtKB Mutagenesis 1116 1116 . . . Note=No effect on formation of isoform 5/isoform Y complex. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10197628;Dbxref=PMID:10197628 P15941 UniProtKB Mutagenesis 1184 1184 . . . Note=S-palmitoylation reduced by 50%25. Complete loss of palmitoylation%2C no effect on endocytosis%2C recycling inhibited and AP1S1 binding reduced by 30%25%3B when associated with C-1186. Accumulates in intracellular compartments%3B when associated with C-1186 and N-1203. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16507569;Dbxref=PMID:16507569 P15941 UniProtKB Mutagenesis 1186 1186 . . . Note=S-palmitoylation reduced by 50%25. Complete loss of palmitoylation%2C no effect on endocytosis%2C recycling inhibited%2C and AP1S1 binding reduced by 30%25%3B when associated with C-1184. Accumulates in intracellular compartments%3B when associated with C-1184 and N-1203. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16507569;Dbxref=PMID:16507569 P15941 UniProtKB Mutagenesis 1187 1189 . . . Note=No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin. RRK->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12939402,ECO:0000269|PubMed:16507569;Dbxref=PMID:12939402,PMID:16507569 P15941 UniProtKB Mutagenesis 1187 1189 . . . Note=No effect on palmitoylation. RRK->QQQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12939402,ECO:0000269|PubMed:16507569;Dbxref=PMID:12939402,PMID:16507569 P15941 UniProtKB Mutagenesis 1191 1191 . . . Note=No effect on EGFR-mediated phosphorylation. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:15471854;Dbxref=PMID:11483589,PMID:15471854 P15941 UniProtKB Mutagenesis 1191 1191 . . . Note=No effect on endocytosis. Y->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:15471854;Dbxref=PMID:11483589,PMID:15471854 P15941 UniProtKB Mutagenesis 1203 1203 . . . Note=No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness. Y->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:15471854,ECO:0000269|PubMed:16507569,ECO:0000269|PubMed:17545600;Dbxref=PMID:11483589,PMID:15471854,PMID:16507569,PMID:17545600 P15941 UniProtKB Mutagenesis 1203 1203 . . . Note=No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:15471854,ECO:0000269|PubMed:16507569,ECO:0000269|PubMed:17545600;Dbxref=PMID:11483589,PMID:15471854,PMID:16507569,PMID:17545600 P15941 UniProtKB Mutagenesis 1203 1203 . . . Note=Reduced endocytosis by 30%25. Greatly reduced binding to AP1S2 and GRB2. Binding AP1S1 reduced by 25%25. Reduced endocytosis by 77%25%3B when associated with N-1243. Accumulates in intracellular compartments%3B when associated with C-1184 and C-1186. Y->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:15471854,ECO:0000269|PubMed:16507569,ECO:0000269|PubMed:17545600;Dbxref=PMID:11483589,PMID:15471854,PMID:16507569,PMID:17545600 P15941 UniProtKB Mutagenesis 1209 1209 . . . Note=Some reduction in EGFR-mediated phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11483589;Dbxref=PMID:11483589 P15941 UniProtKB Mutagenesis 1218 1218 . . . Note=No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:17545600;Dbxref=PMID:11483589,PMID:17545600 P15941 UniProtKB Mutagenesis 1223 1223 . . . Note=No change in PRKCD- nor GSK3B-mediated phosphorylation. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11877440,ECO:0000269|PubMed:9819408;Dbxref=PMID:11877440,PMID:9819408 P15941 UniProtKB Mutagenesis 1224 1224 . . . Note=Loss of PRKCD-mediated phosphorylation. Decreased PRKCD binding. No increased binding to CTNNB1 in the presence of autophosphorylated PRKCD. Increases formation of E-cadherin/beta-catenin complex. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11877440;Dbxref=PMID:11877440 P15941 UniProtKB Mutagenesis 1227 1227 . . . Note=No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11877440,ECO:0000269|PubMed:9819408;Dbxref=PMID:11877440,PMID:9819408 P15941 UniProtKB Mutagenesis 1229 1229 . . . Note=Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11152665,ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:14688481,ECO:0000269|PubMed:15471854;Dbxref=PMID:11152665,PMID:11483589,PMID:14688481,PMID:15471854 P15941 UniProtKB Mutagenesis 1229 1229 . . . Note=No effect on endocytosis. Y->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11152665,ECO:0000269|PubMed:11483589,ECO:0000269|PubMed:14688481,ECO:0000269|PubMed:15471854;Dbxref=PMID:11152665,PMID:11483589,PMID:14688481,PMID:15471854 P15941 UniProtKB Mutagenesis 1243 1243 . . . Note=Reduces binding to AP1S2 by 33%25. Greatly reduced binding to GRB2. Reduced endocytosis by 50%25. Reduced endocytosis by 77%25%3B when associated with N-1203. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15471854;Dbxref=PMID:15471854 P15941 UniProtKB Sequence conflict 2 2 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 134 134 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 154 154 . . . Note=P->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 1021 1021 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 1143 1143 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 1193 1193 . . . Note=Q->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 1231 1231 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Sequence conflict 1251 1251 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P15941 UniProtKB Beta strand 1042 1052 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Helix 1056 1059 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Helix 1064 1080 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Turn 1082 1085 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Beta strand 1086 1096 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Beta strand 1099 1107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Turn 1109 1111 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Helix 1114 1132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM P15941 UniProtKB Beta strand 1136 1142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2ACM