##gff-version 3 P46527 UniProtKB Chain 1 198 . . . ID=PRO_0000190084;Note=Cyclin-dependent kinase inhibitor 1B P46527 UniProtKB Region 1 34 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46527 UniProtKB Region 51 91 . . . Note=Interaction with CDK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28666995;Dbxref=PMID:28666995 P46527 UniProtKB Region 85 198 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46527 UniProtKB Motif 153 169 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 P46527 UniProtKB Compositional bias 158 172 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46527 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine%3B by UHMK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10831586,ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:14504289,ECO:0007744|PubMed:23186163;Dbxref=PMID:10831586,PMID:12042314,PMID:12093740,PMID:14504289,PMID:23186163 P46527 UniProtKB Modified residue 74 74 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17254967;Dbxref=PMID:17254967 P46527 UniProtKB Modified residue 88 88 . . . Note=Phosphotyrosine%3B by ABL%2C LYN%2C SRC and JAK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195327,ECO:0000269|PubMed:17254966,ECO:0000269|PubMed:17254967,ECO:0000269|PubMed:21423214;Dbxref=PMID:16195327,PMID:17254966,PMID:17254967,PMID:21423214 P46527 UniProtKB Modified residue 89 89 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16195327;Dbxref=PMID:16195327 P46527 UniProtKB Modified residue 157 157 . . . Note=Phosphothreonine%3B by CaMK1%2C PKB/AKT1 and PIM1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12244301,ECO:0000269|PubMed:12244303,ECO:0000269|PubMed:18593906,ECO:0000269|PubMed:23707388;Dbxref=PMID:12244301,PMID:12244303,PMID:18593906,PMID:23707388 P46527 UniProtKB Modified residue 170 170 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P46414 P46527 UniProtKB Modified residue 187 187 . . . Note=Phosphothreonine%3B by PKB/AKT1%2C CDK1 and CDK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10323868,ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:16209941,ECO:0000269|PubMed:23478441;Dbxref=PMID:10323868,PMID:12042314,PMID:16209941,PMID:23478441 P46527 UniProtKB Modified residue 198 198 . . . Note=Phosphothreonine%3B by CaMK1%2C PKB/AKT1%2C RPS6KA1%2C RPS6KA3 and PIM1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:14504289,ECO:0000269|PubMed:15280662,ECO:0000269|PubMed:18593906,ECO:0000269|PubMed:23707388;Dbxref=PMID:12042314,PMID:14504289,PMID:15280662,PMID:18593906,PMID:23707388 P46527 UniProtKB Natural variant 15 15 . . . ID=VAR_011871;Note=R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2066828 P46527 UniProtKB Natural variant 69 69 . . . ID=VAR_064429;Note=Found in a patient with multiple endocrine tumors%3B germline mutation%3B reduced expression levels%3B shows impaired binding to CDK2. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20824794;Dbxref=dbSNP:rs777354267,PMID:20824794 P46527 UniProtKB Natural variant 109 109 . . . ID=VAR_011872;Note=V->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|Ref.3,ECO:0000269|Ref.4;Dbxref=dbSNP:rs2066827,PMID:15489334 P46527 UniProtKB Mutagenesis 10 10 . . . Note=Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:15280662;Dbxref=PMID:12042314,PMID:12093740,PMID:15280662 P46527 UniProtKB Mutagenesis 10 10 . . . Note=Exported to the cytoplasm. Inhibits cell cycle arrest. S->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:15280662;Dbxref=PMID:12042314,PMID:12093740,PMID:15280662 P46527 UniProtKB Mutagenesis 10 10 . . . Note=Increased stability in vivo and in vitro. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:15280662;Dbxref=PMID:12042314,PMID:12093740,PMID:15280662 P46527 UniProtKB Mutagenesis 74 74 . . . Note=No change in binding CDK4 and no inhibition of CDK4 activity. Translocates to nucleus. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195327,ECO:0000269|PubMed:19075005;Dbxref=PMID:16195327,PMID:19075005 P46527 UniProtKB Mutagenesis 88 88 . . . Note=Abolishes LYN-mediated phosphorylation%2C reduces CDK2-mediated phosphorylation on T-187%2C has greater cell cycle arrest into S-phase%2C no effect on binding CDK2 complexes%2C reduced CDK4 binding and inhibits CDK4 enzyme activity. No nuclear translocation. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding%3B when associated with F-89. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195327,ECO:0000269|PubMed:17254966,ECO:0000269|PubMed:19075005;Dbxref=PMID:16195327,PMID:17254966,PMID:19075005 P46527 UniProtKB Mutagenesis 89 89 . . . Note=No effect on binding CDK2 complexes%2C reduced CDK4 binding and greatly inhibits CDK4 enzyme activity. No nuclear translocation. Inhibits in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding%3B when associated with F-88. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16195327,ECO:0000269|PubMed:17254966,ECO:0000269|PubMed:19075005;Dbxref=PMID:16195327,PMID:17254966,PMID:19075005 P46527 UniProtKB Mutagenesis 157 157 . . . Note=Greatly reduced PKB/AKT1-mediated phosphorylation. Nuclear location. Inhibits cyclin E/CDK2 cell cycle progression. No effect on binding AKT1. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation%3B when associated with A-198. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12244301,ECO:0000269|PubMed:12244303,ECO:0000269|PubMed:14504289,ECO:0000269|PubMed:15280662;Dbxref=PMID:12042314,PMID:12244301,PMID:12244303,PMID:14504289,PMID:15280662 P46527 UniProtKB Mutagenesis 161 161 . . . Note=No change in PKB/AKT1-mediated phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12244301;Dbxref=PMID:12244301 P46527 UniProtKB Mutagenesis 162 162 . . . Note=No change in PKB/AKT1-mediated phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12244301;Dbxref=PMID:12244301 P46527 UniProtKB Mutagenesis 185 185 . . . Note=Strongly reduced ubiquitination by a TRIM21-containing SCF(SKP2) complex. E->A%2CD%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16209941;Dbxref=PMID:16209941 P46527 UniProtKB Mutagenesis 187 187 . . . Note=No change in PKB/AKT1- nor UHMK1-mediated phosphorylation. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:15280662,ECO:0000269|PubMed:16209941,ECO:0000269|PubMed:16880511;Dbxref=PMID:12042314,PMID:12093740,PMID:15280662,PMID:16209941,PMID:16880511 P46527 UniProtKB Mutagenesis 187 187 . . . Note=Abolishes phosphorylation-dependent ubiquitination. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:12093740,ECO:0000269|PubMed:15280662,ECO:0000269|PubMed:16209941,ECO:0000269|PubMed:16880511;Dbxref=PMID:12042314,PMID:12093740,PMID:15280662,PMID:16209941,PMID:16880511 P46527 UniProtKB Mutagenesis 198 198 . . . Note=Abolishes PKB/AKT1-mediated phosphorylation. 46%25 cytoplasmic location. Greatly reduced binding to YWHAQ. Equally reduced binding%3B when associated with A-10 and A-187. No nuclear import%3B when associated with A-157. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation%3B when associated with A-157. T->A%2CD;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12042314,ECO:0000269|PubMed:14504289,ECO:0000269|PubMed:15280662;Dbxref=PMID:12042314,PMID:14504289,PMID:15280662 P46527 UniProtKB Sequence conflict 22 22 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P46527 UniProtKB Helix 38 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ATH P46527 UniProtKB Turn 50 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JSU P46527 UniProtKB Helix 55 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ATH P46527 UniProtKB Turn 64 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ATH P46527 UniProtKB Beta strand 71 78 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ATH P46527 UniProtKB Helix 86 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JSU