MISP_HUMAN
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 03-AUG-2022, entry version 149.
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 AlphaFoldDB; Q8IVT2; -.
DR BioGRID; 125982; 184.
DR IntAct; Q8IVT2; 112.
DR MINT; Q8IVT2; -.
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; 121 antibodies from 21 providers.
DR DNASU; 126353; -.
DR Ensembl; ENST00000215582.8; ENSP00000215582.4; ENSG00000099812.9.
DR GeneID; 126353; -.
DR KEGG; hsa:126353; -.
DR MANE-Select; ENST00000215582.8; ENSP00000215582.4; NM_173481.4; NP_775752.1.
DR UCSC; uc002lpo.4; human.
DR CTD; 126353; -.
DR DisGeNET; 126353; -.
DR GeneCards; MISP; -.
DR HGNC; HGNC:27000; MISP.
DR HPA; ENSG00000099812; Tissue enriched (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 SignaLink; Q8IVT2; -.
DR BioGRID-ORCS; 126353; 9 hits in 1032 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 ileal mucosa and 132 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
