##gff-version 3 Q13191 UniProtKB Chain 1 982 . . . ID=PRO_0000055860;Note=E3 ubiquitin-protein ligase CBL-B Q13191 UniProtKB Domain 35 343 . . . Note=Cbl-PTB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00839 Q13191 UniProtKB Domain 931 970 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 Q13191 UniProtKB Zinc finger 373 412 . . . Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175 Q13191 UniProtKB Region 35 167 . . . Note=4H Q13191 UniProtKB Region 168 240 . . . Note=EF-hand-like Q13191 UniProtKB Region 241 343 . . . Note=SH2-like Q13191 UniProtKB Region 344 372 . . . Note=Linker Q13191 UniProtKB Region 466 571 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Region 543 568 . . . Note=Interaction with VAV1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399639;Dbxref=PMID:9399639 Q13191 UniProtKB Region 688 731 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Region 769 929 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Region 891 927 . . . Note=Interaction with SH3KBP1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12177062;Dbxref=PMID:12177062 Q13191 UniProtKB Compositional bias 468 487 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 541 569 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 697 712 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 714 728 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 817 832 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 836 850 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Compositional bias 879 898 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13191 UniProtKB Binding site 221 221 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22681 Q13191 UniProtKB Binding site 223 223 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22681 Q13191 UniProtKB Binding site 225 225 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22681 Q13191 UniProtKB Binding site 227 227 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22681 Q13191 UniProtKB Binding site 232 232 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22681 Q13191 UniProtKB Binding site 286 286 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q13191 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine%3B by PKC/PRKCQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19549985;Dbxref=PMID:19549985 Q13191 UniProtKB Modified residue 363 363 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20525694;Dbxref=PMID:20525694 Q13191 UniProtKB Modified residue 476 476 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8K4S7 Q13191 UniProtKB Modified residue 480 480 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3TTA7 Q13191 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3TTA7 Q13191 UniProtKB Modified residue 521 521 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q13191 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q13191 UniProtKB Modified residue 529 529 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q13191 UniProtKB Modified residue 634 634 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8K4S7 Q13191 UniProtKB Modified residue 665 665 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10022120;Dbxref=PMID:10022120 Q13191 UniProtKB Modified residue 709 709 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10022120;Dbxref=PMID:10022120 Q13191 UniProtKB Modified residue 889 889 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3TTA7 Q13191 UniProtKB Alternative sequence 767 770 . . . ID=VSP_005730;Note=In isoform Truncated 2. DVFD->TYRI;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7784085;Dbxref=PMID:7784085 Q13191 UniProtKB Alternative sequence 771 982 . . . ID=VSP_005731;Note=In isoform Truncated 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7784085;Dbxref=PMID:7784085 Q13191 UniProtKB Alternative sequence 811 982 . . . ID=VSP_005729;Note=In isoform Truncated 1. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7784085;Dbxref=PMID:7784085 Q13191 UniProtKB Natural variant 257 257 . . . ID=VAR_088738;Note=In ADMIO3%3B likely pathogenic. H->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36006710;Dbxref=PMID:36006710 Q13191 UniProtKB Natural variant 436 436 . . . ID=VAR_088739;Note=In ADMIO3%3B uncertain significance. C->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36006710;Dbxref=PMID:36006710 Q13191 UniProtKB Natural variant 468 982 . . . ID=VAR_088740;Note=In ADMIO3%3B likely pathogenic. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36006710;Dbxref=PMID:36006710 Q13191 UniProtKB Natural variant 584 584 . . . ID=VAR_025303;Note=R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17853100,PMID:15489334 Q13191 UniProtKB Natural variant 883 883 . . . ID=VAR_039241;Note=N->D;Dbxref=dbSNP:rs35835913 Q13191 UniProtKB Mutagenesis 298 298 . . . Note=Inhibits interaction with SYK. No effect on E3 activity. G->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10022120,ECO:0000269|PubMed:11087752;Dbxref=PMID:10022120,PMID:11087752 Q13191 UniProtKB Mutagenesis 363 363 . . . Note=Decreases affinity for E2 ubiquitin-conjugating enzymes. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20525694;Dbxref=PMID:20525694 Q13191 UniProtKB Mutagenesis 373 373 . . . Note=Abolishes E3 activity but does not affect binding to substrates. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11087752,ECO:0000269|PubMed:11375397;Dbxref=PMID:11087752,PMID:11375397 Q13191 UniProtKB Mutagenesis 665 665 . . . Note=Slightly inhibits interaction with CRKL. Abolishes interaction with CRKL%3B when associated with F-709. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10022120;Dbxref=PMID:10022120 Q13191 UniProtKB Mutagenesis 709 709 . . . Note=Inhibits interaction with CRKL. Abolishes interaction with CRKL%3B when associated with F-665. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10022120;Dbxref=PMID:10022120 Q13191 UniProtKB Mutagenesis 904 904 . . . Note=No effect on interaction with CD2AP. Reduced interaction with SH3KBP1. Strongly reduced interaction with SH3KBP1%3B when associated with A-911. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16228008,ECO:0000269|PubMed:17020880;Dbxref=PMID:16228008,PMID:17020880 Q13191 UniProtKB Mutagenesis 907 907 . . . Note=No effect on interaction with SH3KBP1. Reduced interaction with CD2AP. Strongly reduced interaction with CD2AP%3B when associated with A-911. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17020880;Dbxref=PMID:17020880 Q13191 UniProtKB Mutagenesis 911 911 . . . Note=Reduced interaction with CD2AP and with SH3KBP1. Strongly reduced interaction with CD2AP%3B when associated with A-907. Strongly reduced interaction with SH3KBP1%3B when associated with A-904. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16228008,ECO:0000269|PubMed:17020880;Dbxref=PMID:16228008,PMID:17020880 Q13191 UniProtKB Mutagenesis 937 937 . . . Note=Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. A->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17679095;Dbxref=PMID:17679095 Q13191 UniProtKB Mutagenesis 940 940 . . . Note=Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17679095;Dbxref=PMID:17679095 Q13191 UniProtKB Mutagenesis 943 944 . . . Note=Abolishes interaction with ubiquitinated proteins. GY->AQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15273720;Dbxref=PMID:15273720 Q13191 UniProtKB Mutagenesis 946 946 . . . Note=Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17679095;Dbxref=PMID:17679095 Q13191 UniProtKB Mutagenesis 966 966 . . . Note=Interferes with dimerization. Reduced E3 ubiquitin-protein ligase activity. Reduced levels of tyrosine phosphorylation. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17679095;Dbxref=PMID:17679095 Q13191 UniProtKB Mutagenesis 967 967 . . . Note=No effect on interaction with ubiquitinated proteins. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15273720;Dbxref=PMID:15273720 Q13191 UniProtKB Sequence conflict 210 210 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13191 UniProtKB Sequence conflict 911 911 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13191 UniProtKB Helix 43 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 63 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 69 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 74 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 95 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 105 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 129 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 138 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 162 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 168 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 176 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 190 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 194 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 210 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 225 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 230 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 243 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 246 253 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VGO Q13191 UniProtKB Helix 266 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 282 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 289 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 295 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 306 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 312 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PFV Q13191 UniProtKB Helix 316 325 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 332 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VGO Q13191 UniProtKB Helix 342 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3PFV Q13191 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 357 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Turn 365 367 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Turn 374 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 377 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 383 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 394 402 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 417 420 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Beta strand 422 424 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZNI Q13191 UniProtKB Helix 933 941 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OOA Q13191 UniProtKB Helix 946 955 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OOA Q13191 UniProtKB Turn 956 958 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OOA Q13191 UniProtKB Helix 960 970 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OOA