ID   MISP_HUMAN              Reviewed;         679 AA.
AC   Q8IVT2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-SEP-2021, entry version 146.
DE   RecName: Full=Mitotic interactor and substrate of PLK1 {ECO:0000303|PubMed:23574715};
DE   AltName: Full=Mitotic spindle positioning protein {ECO:0000312|HGNC:HGNC:27000};
GN   Name=MISP {ECO:0000312|HGNC:HGNC:27000};
GN   Synonyms=C19orf21 {ECO:0000312|HGNC:HGNC:27000};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; THR-287 AND SER-400, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-164; THR-172; THR-219;
RP   THR-224; SER-284; THR-287; SER-394; SER-395; SER-397; SER-400; SER-430;
RP   SER-541; SER-543; SER-575; THR-577; SER-582 AND SER-675, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; THR-164; SER-214;
RP   THR-219; THR-287; THR-377; SER-394; SER-395; SER-400; SER-471; SER-541;
RP   SER-575; THR-577 AND SER-582, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
RP   FUNCTION, INTERACTION WITH DCTN1; MAPRE1 AND PTK2, SUBCELLULAR LOCATION,
RP   AND PHOSPHORYLATION BY CDK1.
RX   PubMed=23574715; DOI=10.4161/cc.24602;
RA   Maier B., Kirsch M., Anderhub S., Zentgraf H., Kraemer A.;
RT   "The novel actin/focal adhesion-associated protein MISP is involved in
RT   mitotic spindle positioning in human cells.";
RL   Cell Cycle 12:1457-1471(2013).
RN   [8]
RP   FUNCTION, INTERACTION WITH ACTIN AND DCTN1, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-78; THR-164; THR-172; SER-214;
RP   THR-224; SER-284; THR-287; THR-377; SER-382; SER-394; SER-395; SER-397;
RP   SER-575; SER-582 AND SER-586, AND MUTAGENESIS OF SER-78; THR-164; THR-172;
RP   SER-214; THR-224; SER-284; THR-287; THR-377; SER-382; SER-394; SER-395;
RP   SER-397; SER-471; SER-575; SER-582 AND SER-586.
RX   PubMed=23509069; DOI=10.1083/jcb.201207050;
RA   Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P.,
RA   Goenczy P., Hoffmann I.;
RT   "MISP is a novel Plk1 substrate required for proper spindle orientation and
RT   mitotic progression.";
RL   J. Cell Biol. 200:773-787(2013).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-156; THR-164;
RP   THR-179; THR-224; SER-348; SER-394; SER-395; SER-397; SER-400; SER-471;
RP   SER-541; SER-543 AND SER-575, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Plays a role in mitotic spindle orientation and mitotic
CC       progression. Regulates the distribution of dynactin at the cell cortex
CC       in a PLK1-dependent manner, thus stabilizing cortical and astral
CC       microtubule attachments required for proper mitotic spindle
CC       positioning. May link microtubules to the actin cytospkeleton and focal
CC       adhesions. May be required for directed cell migration and centrosome
CC       orientation. May also be necessary for proper stacking of the Golgi
CC       apparatus. {ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:23574715}.
CC   -!- SUBUNIT: Associates with F-actin. Interacts with DCTN1; this
CC       interaction regulates DCTN1 distribution at the cell cortex. Interacts
CC       with PTK2/FAK and MAPRE1. {ECO:0000269|PubMed:23509069,
CC       ECO:0000269|PubMed:23574715}.
CC   -!- INTERACTION:
CC       Q8IVT2; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-2555085, EBI-11519926;
CC       Q8IVT2; Q9H2G9: BLZF1; NbExp=5; IntAct=EBI-2555085, EBI-2548012;
CC       Q8IVT2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-2555085, EBI-11983447;
CC       Q8IVT2; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-2555085, EBI-11976299;
CC       Q8IVT2; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-2555085, EBI-2802782;
CC       Q8IVT2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2555085, EBI-742887;
CC       Q8IVT2; Q96SW2: CRBN; NbExp=3; IntAct=EBI-2555085, EBI-2510250;
CC       Q8IVT2; Q9BQC3: DPH2; NbExp=3; IntAct=EBI-2555085, EBI-10237931;
CC       Q8IVT2; Q7L190: DPPA4; NbExp=3; IntAct=EBI-2555085, EBI-710457;
CC       Q8IVT2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2555085, EBI-2349927;
CC       Q8IVT2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2555085, EBI-744099;
CC       Q8IVT2; P15311: EZR; NbExp=4; IntAct=EBI-2555085, EBI-1056902;
CC       Q8IVT2; Q14192: FHL2; NbExp=3; IntAct=EBI-2555085, EBI-701903;
CC       Q8IVT2; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2555085, EBI-750641;
CC       Q8IVT2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2555085, EBI-618309;
CC       Q8IVT2; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2555085, EBI-7060731;
CC       Q8IVT2; O75031: HSF2BP; NbExp=3; IntAct=EBI-2555085, EBI-7116203;
CC       Q8IVT2; Q16082: HSPB2; NbExp=3; IntAct=EBI-2555085, EBI-739395;
CC       Q8IVT2; Q9UJY1: HSPB8; NbExp=3; IntAct=EBI-2555085, EBI-739074;
CC       Q8IVT2; Q9UKT9: IKZF3; NbExp=5; IntAct=EBI-2555085, EBI-747204;
CC       Q8IVT2; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-2555085, EBI-9658404;
CC       Q8IVT2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-2555085, EBI-11953334;
CC       Q8IVT2; P25800: LMO1; NbExp=8; IntAct=EBI-2555085, EBI-8639312;
CC       Q8IVT2; P25791-3: LMO2; NbExp=5; IntAct=EBI-2555085, EBI-11959475;
CC       Q8IVT2; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-2555085, EBI-2603996;
CC       Q8IVT2; Q6PF18: MORN3; NbExp=3; IntAct=EBI-2555085, EBI-9675802;
CC       Q8IVT2; Q5VZ52: MORN5; NbExp=3; IntAct=EBI-2555085, EBI-12835568;
CC       Q8IVT2; O43482: OIP5; NbExp=3; IntAct=EBI-2555085, EBI-536879;
CC       Q8IVT2; P26367: PAX6; NbExp=3; IntAct=EBI-2555085, EBI-747278;
CC       Q8IVT2; Q99471: PFDN5; NbExp=3; IntAct=EBI-2555085, EBI-357275;
CC       Q8IVT2; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-2555085, EBI-357318;
CC       Q8IVT2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2555085, EBI-10232538;
CC       Q8IVT2; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-2555085, EBI-302355;
CC       Q8IVT2; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-2555085, EBI-10293968;
CC       Q8IVT2; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-2555085, EBI-1567866;
CC       Q8IVT2; Q8N443: RIBC1; NbExp=3; IntAct=EBI-2555085, EBI-10265323;
CC       Q8IVT2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2555085, EBI-726876;
CC       Q8IVT2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-2555085, EBI-6257312;
CC       Q8IVT2; Q15428: SF3A2; NbExp=3; IntAct=EBI-2555085, EBI-2462271;
CC       Q8IVT2; Q13573: SNW1; NbExp=3; IntAct=EBI-2555085, EBI-632715;
CC       Q8IVT2; O14512: SOCS7; NbExp=3; IntAct=EBI-2555085, EBI-1539606;
CC       Q8IVT2; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-2555085, EBI-11995806;
CC       Q8IVT2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-2555085, EBI-3923692;
CC       Q8IVT2; P54274-2: TERF1; NbExp=5; IntAct=EBI-2555085, EBI-711018;
CC       Q8IVT2; Q12933: TRAF2; NbExp=3; IntAct=EBI-2555085, EBI-355744;
CC       Q8IVT2; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-2555085, EBI-492476;
CC       Q8IVT2; Q15654: TRIP6; NbExp=3; IntAct=EBI-2555085, EBI-742327;
CC       Q8IVT2; P61758: VBP1; NbExp=3; IntAct=EBI-2555085, EBI-357430;
CC       Q8IVT2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-2555085, EBI-4395669;
CC       Q8IVT2; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-2555085, EBI-10251462;
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cytoplasm,
CC       cytoskeleton. Cytoplasm, cell cortex. Note=Predominantly localizes to
CC       cortical actin structures during interphase and mitosis. Present in
CC       retraction fibers, which are formed at former adhesion sites during
CC       mitosis, and at spicular membrane protrusions in re-attaching
CC       cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not
CC       detected at microtubules at interphase, nor at spindle during mitosis.
CC   -!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner. Weakly
CC       expressed in G1 and S phases. Expression increases in G2/M phases and
CC       persisting until the end of mitosis (at protein level).
CC       {ECO:0000269|PubMed:23509069}.
CC   -!- PTM: Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for
CC       PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper
CC       spindle orientation at metaphase. {ECO:0000269|PubMed:23509069,
CC       ECO:0000269|PubMed:23574715}.
CC   -!- SIMILARITY: Belongs to the MISP family. {ECO:0000305}.
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DR   EMBL; BC042125; AAH42125.1; -; mRNA.
DR   EMBL; BC052236; AAH52236.1; -; mRNA.
DR   CCDS; CCDS12042.1; -.
DR   PIR; T00636; T00636.
DR   RefSeq; NP_775752.1; NM_173481.3.
DR   RefSeq; XP_011525987.1; XM_011527685.2.
DR   RefSeq; XP_011525988.1; XM_011527686.2.
DR   BioGRID; 125982; 128.
DR   IntAct; Q8IVT2; 111.
DR   STRING; 9606.ENSP00000215582; -.
DR   ChEMBL; CHEMBL4295893; -.
DR   GlyGen; Q8IVT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IVT2; -.
DR   PhosphoSitePlus; Q8IVT2; -.
DR   BioMuta; MISP; -.
DR   DMDM; 73620663; -.
DR   EPD; Q8IVT2; -.
DR   jPOST; Q8IVT2; -.
DR   MassIVE; Q8IVT2; -.
DR   MaxQB; Q8IVT2; -.
DR   PaxDb; Q8IVT2; -.
DR   PeptideAtlas; Q8IVT2; -.
DR   PRIDE; Q8IVT2; -.
DR   ProteomicsDB; 70765; -.
DR   Antibodypedia; 22380; 119 antibodies.
DR   DNASU; 126353; -.
DR   Ensembl; ENST00000215582; ENSP00000215582; ENSG00000099812.
DR   GeneID; 126353; -.
DR   KEGG; hsa:126353; -.
DR   UCSC; uc002lpo.4; human.
DR   CTD; 126353; -.
DR   DisGeNET; 126353; -.
DR   GeneCards; MISP; -.
DR   HGNC; HGNC:27000; MISP.
DR   HPA; ENSG00000099812; Group enriched (gallbladder, intestine).
DR   MIM; 615289; gene.
DR   neXtProt; NX_Q8IVT2; -.
DR   OpenTargets; ENSG00000099812; -.
DR   PharmGKB; PA134861073; -.
DR   VEuPathDB; HostDB:ENSG00000099812; -.
DR   eggNOG; ENOG502RZZI; Eukaryota.
DR   GeneTree; ENSGT00940000154739; -.
DR   HOGENOM; CLU_404873_0_0_1; -.
DR   InParanoid; Q8IVT2; -.
DR   OMA; WGQDEPQ; -.
DR   OrthoDB; 481627at2759; -.
DR   PhylomeDB; Q8IVT2; -.
DR   TreeFam; TF334067; -.
DR   PathwayCommons; Q8IVT2; -.
DR   BioGRID-ORCS; 126353; 5 hits in 977 CRISPR screens.
DR   ChiTaRS; MISP; human.
DR   GenomeRNAi; 126353; -.
DR   Pharos; Q8IVT2; Tbio.
DR   PRO; PR:Q8IVT2; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8IVT2; protein.
DR   Bgee; ENSG00000099812; Expressed in mucosa of transverse colon and 161 other tissues.
DR   Genevisible; Q8IVT2; HS.
DR   GO; GO:0005884; C:actin filament; IMP:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0031616; C:spindle pole centrosome; IMP:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IMP:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0051660; P:establishment of centrosome localization; IMP:UniProtKB.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR   GO; GO:0051640; P:organelle localization; IMP:UniProtKB.
DR   GO; GO:1904776; P:regulation of protein localization to cell cortex; IMP:UniProtKB.
DR   InterPro; IPR029304; AKAP2_C.
DR   InterPro; IPR042779; MISP/MISP3.
DR   PANTHER; PTHR18839; PTHR18839; 2.
DR   Pfam; PF15304; AKAP2_C; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell cycle; Cell division; Cell junction; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Mitotic interactor and substrate of PLK1"
FT                   /id="PRO_0000079381"
FT   REGION          151..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          545..569
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        452..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         78
FT                   /note="Phosphoserine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         164
FT                   /note="Phosphothreonine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         172
FT                   /note="Phosphothreonine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         214
FT                   /note="Phosphoserine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         219
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         224
FT                   /note="Phosphothreonine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         284
FT                   /note="Phosphoserine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976"
FT   MOD_RES         287
FT                   /note="Phosphothreonine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         377
FT                   /note="Phosphothreonine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         382
FT                   /note="Phosphoserine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MOD_RES         394
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         395
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         397
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         471
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         543
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         575
FT                   /note="Phosphoserine; by CDK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         577
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         582
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT   MOD_RES         586
FT                   /note="Phosphoserine; by PLK1; in vitro"
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         99
FT                   /note="A -> T (in dbSNP:rs45477999)"
FT                   /id="VAR_061629"
FT   VARIANT         156
FT                   /note="S -> G (in dbSNP:rs3746173)"
FT                   /id="VAR_033754"
FT   VARIANT         232
FT                   /note="K -> R (in dbSNP:rs3746175)"
FT                   /id="VAR_033755"
FT   VARIANT         269
FT                   /note="S -> N (in dbSNP:rs35384259)"
FT                   /id="VAR_050910"
FT   VARIANT         653
FT                   /note="E -> G (in dbSNP:rs8107847)"
FT                   /id="VAR_033756"
FT   MUTAGEN         78
FT                   /note="S->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-164; A-172; A-214; A-
FT                   224; A-284; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         164
FT                   /note="T->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-172; A-214; A-
FT                   224; A-284; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         172
FT                   /note="T->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-214; A-
FT                   224; A-284; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         214
FT                   /note="S->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   224; A-284; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         224
FT                   /note="T->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   214; A-284; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         284
FT                   /note="S->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   214; A-224; A-287; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         287
FT                   /note="T->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   214; A-224; A-284; A-377 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         377
FT                   /note="T->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   214; A-224; A-284; A-287 and A-575."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         382
FT                   /note="S->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-394; A-395; A-397; A-
FT                   471; A-582 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         394
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-395; A-397; A-471; A-582 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         394
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-395; D-397; D-471; D-582 and D-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         395
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-394; A-397; A-471; A-582 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         395
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-394; D-397; D-471; D-582 and D-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         397
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-394; A-395; A-471; A-582 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         397
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-394; D-395; D-471; D-582 and D-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         471
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-394; A-395; A-397; A-582 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         471
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-394; D-395; D-397; D-582 and D-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         575
FT                   /note="S->A: Almost complete loss of CDK1 phosphorylation
FT                   in vitro, loss of PLK1-binding, no effect on cortical
FT                   localization; when associated with A-78; A-164; A-172; A-
FT                   214; A-224; A-284; A-287 and A-377."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         582
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-394; A-395; A-397; A-471 and A-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         582
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-394; D-395; D-397; D-471 and D-586."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         586
FT                   /note="S->A: Drastic reduction in PLK1 phosphorylation in
FT                   vitro, no effect on cortical localization; when associated
FT                   with A-382; A-394; A-395; A-397; A-471 and A-582."
FT                   /evidence="ECO:0000269|PubMed:23509069"
FT   MUTAGEN         586
FT                   /note="S->D: No effect on cortical localization; when
FT                   associated with D-394; D-395; D-397; D-471 and D-582."
FT                   /evidence="ECO:0000269|PubMed:23509069"
SQ   SEQUENCE   679 AA;  75357 MW;  D2881CF5087E61F8 CRC64;
     MDRVTRYPIL GIPQAHRGTG LVLDGDTSYT YHLVCMGPEA SGWGQDEPQT WPTDHRAQQG
     VQRQGVSYSV HAYTGQPSPR GLHSENREDE GWQVYRLGAR DAHQGRPTWA LRPEDGEDKE
     MKTYRLDAGD ADPRRLCDLE RERWAVIQGQ AVRKSSTVAT LQGTPDHGDP RTPGPPRSTP
     LEENVVDREQ IDFLAARQQF LSLEQANKGA PHSSPARGTP AGTTPGASQA PKAFNKPHLA
     NGHVVPIKPQ VKGVVREENK VRAVPTWASV QVVDDPGSLA SVESPGTPKE TPIEREIRLA
     QEREADLREQ RGLRQATDHQ ELVEIPTRPL LTKLSLITAP RRERGRPSLY VQRDIVQETQ
     REEDHRREGL HVGRASTPDW VSEGPQPGLR RALSSDSILS PAPDARAADP APEVRKVNRI
     PPDAYQPYLS PGTPQLEFSA FGAFGKPSSL STAEAKAATS PKATMSPRHL SESSGKPLST
     KQEASKPPRG CPQANRGVVR WEYFRLRPLR FRAPDEPQQA QVPHVWGWEV AGAPALRLQK
     SQSSDLLERE RESVLRREQE VAEERRNALF PEVFSPTPDE NSDQNSRSSS QASGITGSYS
     VSESPFFSPI HLHSNVAWTV EDPVDSAPPG QRKKEQWYAG INPSDGINSE VLEAIRVTRH
     KNAMAERWES RIYASEEDD
//