##gff-version 3 P30307 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P30307 UniProtKB Chain 2 473 . . . ID=PRO_0000198647;Note=M-phase inducer phosphatase 3 P30307 UniProtKB Domain 321 428 . . . Note=Rhodanese;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00173 P30307 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P30307 UniProtKB Region 132 158 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P30307 UniProtKB Region 334 379 . . . Note=HIV-1 Vpr binding site P30307 UniProtKB Active site 377 377 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P30304 P30307 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 P30307 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P30307 UniProtKB Modified residue 38 38 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 P30307 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:8119945,ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648,PMID:8119945 P30307 UniProtKB Modified residue 57 57 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P30307 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 P30307 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:18691976,PMID:20068231 P30307 UniProtKB Modified residue 67 67 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:8119945,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231,PMID:8119945 P30307 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8119945;Dbxref=PMID:8119945 P30307 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12595692;Dbxref=PMID:12595692 P30307 UniProtKB Modified residue 130 130 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12595692;Dbxref=PMID:12595692 P30307 UniProtKB Modified residue 168 168 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:8119945,ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976,PMID:8119945 P30307 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine%3B by PLK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14968113;Dbxref=PMID:14968113 P30307 UniProtKB Modified residue 198 198 . . . Note=Phosphoserine%3B by PLK3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14968113;Dbxref=PMID:14968113 P30307 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8119945;Dbxref=PMID:8119945 P30307 UniProtKB Modified residue 216 216 . . . Note=Phosphoserine%3B by CHEK1%2C CHEK2%2C BRSK1%2C MAPK14 AND MARK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11333986,ECO:0000269|PubMed:15150265,ECO:0000269|PubMed:15629715,ECO:0007744|PubMed:23186163;Dbxref=PMID:11333986,PMID:15150265,PMID:15629715,PMID:23186163 P30307 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 P30307 UniProtKB Alternative sequence 66 123 . . . ID=VSP_000863;Note=In isoform 4 and isoform 5. GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP->SPGFFRTSGSAFSWD;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11078813,ECO:0000303|PubMed:11139144;Dbxref=PMID:11078813,PMID:11139144 P30307 UniProtKB Alternative sequence 124 153 . . . ID=VSP_000864;Note=In isoform 2 and isoform 5. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11078813,ECO:0000303|PubMed:11139144;Dbxref=PMID:11078813,PMID:11139144 P30307 UniProtKB Natural variant 14 14 . . . ID=VAR_027922;Note=S->N;Dbxref=dbSNP:rs11567959 P30307 UniProtKB Natural variant 70 70 . . . ID=VAR_027923;Note=R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11139144,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:2195549;Dbxref=dbSNP:rs3734166,PMID:11139144,PMID:15489334,PMID:2195549 P30307 UniProtKB Natural variant 78 78 . . . ID=VAR_027924;Note=S->N;Dbxref=dbSNP:rs11567962 P30307 UniProtKB Natural variant 297 297 . . . ID=VAR_020146;Note=G->R;Dbxref=dbSNP:rs11567997 P30307 UniProtKB Mutagenesis 129 129 . . . Note=Loss of phosphorylation. Severely impairs PLK1-binding. S->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12595692;Dbxref=PMID:12595692 P30307 UniProtKB Mutagenesis 130 130 . . . Note=Loss of phosphorylation. Severely impairs PLK1-binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12595692;Dbxref=PMID:12595692 P30307 UniProtKB Mutagenesis 191 191 . . . Note=Facilitates nuclear exclusion. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14968113;Dbxref=PMID:14968113 P30307 UniProtKB Mutagenesis 191 191 . . . Note=Mimicks phosphorylation state%2C leading to enhanced accumulation in the nucleus. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14968113;Dbxref=PMID:14968113 P30307 UniProtKB Mutagenesis 211 211 . . . Note=Reduces phosphorylation by MARK3 and CHEK1. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 P30307 UniProtKB Mutagenesis 216 216 . . . Note=No effect on interaction with MARK3. Abolishes phosphorylation by MARK3. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 P30307 UniProtKB Mutagenesis 221 221 . . . Note=Abolishes interaction with MARK3. Reduces phosphorylation of S-216 by MARK3. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 P30307 UniProtKB Mutagenesis 242 244 . . . Note=No effect on interaction with MARK3. KKK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12941695;Dbxref=PMID:12941695 P30307 UniProtKB Mutagenesis 352 352 . . . Note=Partial loss of HIV-1 Vpr binding. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14972559;Dbxref=PMID:14972559 P30307 UniProtKB Mutagenesis 359 359 . . . Note=No effect on HIV-1 Vpr binding. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14972559;Dbxref=PMID:14972559 P30307 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3BZI P30307 UniProtKB Beta strand 286 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 300 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 307 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Turn 315 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 322 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 333 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 339 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 350 357 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 369 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 384 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 409 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 415 419 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Turn 420 422 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 427 430 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Beta strand 438 440 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3OP3 P30307 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305 P30307 UniProtKB Modified residue 61 61 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305