CP190_DROME
ID CP190_DROME Reviewed; 1096 AA.
AC Q24478; A4V2Y3; Q9VFA1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Centrosome-associated zinc finger protein CP190;
DE AltName: Full=Protein enhancer of mod(mdg4)4-1;
DE AltName: Full=dMAP190;
GN Name=Cp190; Synonyms=E(mod)4-1; ORFNames=CG6384;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=8586650; DOI=10.1242/jcs.108.11.3377;
RA Whitfield W.G.F., Chaplin M.A., Oegema K., Parry H., Glover D.M.;
RT "The 190 kDa centrosome-associated protein of Drosophila melanogaster
RT contains four zinc finger motifs and binds to specific sites on polytene
RT chromosomes.";
RL J. Cell Sci. 108:3377-3387(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CP60, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=1372522; DOI=10.1091/mbc.3.1.1;
RA Kellogg D.R., Alberts B.M.;
RT "Purification of a multiprotein complex containing centrosomal proteins
RT from the Drosophila embryo by chromatography with low-affinity polyclonal
RT antibodies.";
RL Mol. Biol. Cell 3:1-11(1992).
RN [6]
RP INTERACTION WITH CP60 AND MICROTUBULES, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8491775; DOI=10.1083/jcb.121.4.823;
RA Raff J.W., Kellogg D.R., Alberts B.M.;
RT "Drosophila gamma-tubulin is part of a complex containing two previously
RT identified centrosomal MAPs.";
RL J. Cell Biol. 121:823-835(1993).
RN [7]
RP INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=8522588; DOI=10.1083/jcb.131.5.1261;
RA Oegema K., Whitfield W.G.F., Alberts B.M.;
RT "The cell cycle-dependent localization of the CP190 centrosomal protein is
RT determined by the coordinate action of two separable domains.";
RL J. Cell Biol. 131:1261-1273(1995).
RN [8]
RP INTERACTION WITH CP60, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8590797; DOI=10.1091/mbc.6.12.1673;
RA Kellogg D.R., Oegema K., Raff J., Schneider K., Alberts B.M.;
RT "CP60: a microtubule-associated protein that is localized to the centrosome
RT in a cell cycle-specific manner.";
RL Mol. Biol. Cell 6:1673-1684(1995).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9247191; DOI=10.1242/jcs.110.14.1573;
RA Oegema K., Marshall W.F., Sedat J.W., Alberts B.M.;
RT "Two proteins that cycle asynchronously between centrosomes and nuclear
RT structures: Drosophila CP60 and CP190.";
RL J. Cell Sci. 110:1573-1583(1997).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=9256351; DOI=10.1016/s0925-4773(97)00066-x;
RA Riparbelli M.G., Whitfield W.G.F., Dallai R., Callaini G.;
RT "Assembly of the zygotic centrosome in the fertilized Drosophila egg.";
RL Mech. Dev. 65:135-144(1997).
RN [11]
RP INTERACTION WITH CP60.
RX PubMed=9700165; DOI=10.1083/jcb.142.3.775;
RA Moritz M., Zheng Y., Alberts B.M., Oegema K.;
RT "Recruitment of the gamma-tubulin ring complex to Drosophila salt-stripped
RT centrosome scaffolds.";
RL J. Cell Biol. 142:775-786(1998).
RN [12]
RP FUNCTION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=14996941; DOI=10.1242/jcs.00979;
RA Butcher R.D.J., Chodagam S., Basto R., Wakefield J.G., Henderson D.S.,
RA Raff J.W., Whitfield W.G.F.;
RT "The Drosophila centrosome-associated protein CP190 is essential for
RT viability but not for cell division.";
RL J. Cell Sci. 117:1191-1199(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15479719; DOI=10.1242/jcs.01401;
RA Raynaud-Messina B., Mazzolini L., Moisand A., Cirinesi A.-M., Wright M.;
RT "Elongation of centriolar microtubule triplets contributes to the formation
RT of the mitotic spindle in gamma-tubulin-depleted cells.";
RL J. Cell Sci. 117:5497-5507(2004).
RN [14]
RP FUNCTION, DNA-BINDING, INTERACTION WITH MOD(MDG4) AND SU(HW), AND
RP SUBCELLULAR LOCATION.
RX PubMed=15574329; DOI=10.1016/j.molcel.2004.11.004;
RA Pai C.-Y., Lei E.P., Ghosh D., Corces V.G.;
RT "The centrosomal protein CP190 is a component of the gypsy chromatin
RT insulator.";
RL Mol. Cell 16:737-748(2004).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16051175; DOI=10.1016/j.cub.2005.06.024;
RA Chodagam S., Royou A., Whitfield W.G.F., Karess R., Raff J.W.;
RT "The centrosomal protein CP190 regulates myosin function during early
RT Drosophila development.";
RL Curr. Biol. 15:1308-1313(2005).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=16209949; DOI=10.1016/j.molcel.2005.08.031;
RA Capelson M., Corces V.G.;
RT "The ubiquitin ligase dTopors directs the nuclear organization of a
RT chromatin insulator.";
RL Mol. Cell 20:105-116(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-319; SER-920 AND
RP SER-925, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-229; SER-233;
RP SER-298; THR-603; SER-610; SER-708; SER-723; THR-727; SER-745; SER-748;
RP SER-757; SER-760; THR-817; SER-920; SER-927; THR-936; SER-938; SER-1071 AND
RP SER-1074, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [19]
RP INTERACTION WITH INSV.
RX PubMed=25561495; DOI=10.1101/gad.252122.114;
RA Dai Q., Ren A., Westholm J.O., Duan H., Patel D.J., Lai E.C.;
RT "Common and distinct DNA-binding and regulatory activities of the BEN-solo
RT transcription factor family.";
RL Genes Dev. 29:48-62(2015).
RN [20]
RP INTERACTION WITH NUP98.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
CC -!- FUNCTION: Component of the gypsy chromatin insulator complex which is
CC required for the function of the gypsy chromatin insulator and other
CC endogenous chromatin insulators. Chromatin insulators are regulatory
CC elements which establish independent domains of transcriptional
CC activity within eukaryotic genomes. Insulators have two defining
CC properties; they can block the communication between an enhancer and a
CC promoter when placed between them and can also buffer transgenes from
CC position effect variegation (PEV). Insulators are proposed to structure
CC the chromatin fiber into independent domains of differing
CC transcriptional potential by promoting the formation of distinct
CC chromatin loops. This chromatin looping may involve the formation of
CC insulator bodies, where homotypic interactions between individual
CC subunits of the insulator complex could promote the clustering of
CC widely spaced insulators at the nuclear periphery. Within the gypsy
CC insulator complex, this protein may directly bind to insulator DNA at
CC sites distinct from those recognized by su(Hw). Required during
CC embryogenesis for axial expansion, an actin/myosin dependent process
CC that distributes the dividing nuclei along the anterior-posterior axis
CC of the syncytial embryo. Does not appear to play a crucial role in
CC organizing centrosomal microtubules during mitosis.
CC {ECO:0000269|PubMed:14996941, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:16051175}.
CC -!- SUBUNIT: Component of the gypsy chromatin insulator complex, composed
CC of Cp190, mod(mdg4) and su(Hw) (PubMed:15574329). The gypsy chromatin
CC insulator complex interacts with Topors via mod(mdg4) and su(Hw)
CC (PubMed:15574329). Interacts with Cp60 and microtubules
CC (PubMed:8590797, PubMed:9700165, PubMed:8491775, PubMed:8522588,
CC PubMed:14996941). Interacts with inv (PubMed:25561495). Interacts with
CC Nup98 (PubMed:28366641). {ECO:0000269|PubMed:1372522,
CC ECO:0000269|PubMed:14996941, ECO:0000269|PubMed:15574329,
CC ECO:0000269|PubMed:25561495, ECO:0000269|PubMed:28366641,
CC ECO:0000269|PubMed:8491775, ECO:0000269|PubMed:8522588,
CC ECO:0000269|PubMed:8590797, ECO:0000269|PubMed:9700165}.
CC -!- INTERACTION:
CC Q24478; Q8TA44: CTCF; NbExp=5; IntAct=EBI-868840, EBI-466743;
CC Q24478; Q9VHG5: Ibf1; NbExp=3; IntAct=EBI-868840, EBI-141691;
CC Q24478; Q9VHG6: Ibf2; NbExp=3; IntAct=EBI-868840, EBI-157022;
CC Q24478; Q86B87-1: mod(mdg4); NbExp=4; IntAct=EBI-868840, EBI-1433422;
CC Q24478; P08970: su(Hw); NbExp=4; IntAct=EBI-868840, EBI-101373;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Chromosome.
CC Note=Nucleus in interphase. Colocalizes with other elements of the
CC gypsy chromatin insulator complex at multiple sites on polytene
CC chromosomes and at nuclear insulator bodies.
CC -!- TISSUE SPECIFICITY: Expressed in spermatids but not in mature
CC spermatozoa. Localizes within the spermatids to a sheath of
CC microtubules around the nucleus and to microtubules within the tail.
CC {ECO:0000269|PubMed:9256351}.
CC -!- DEVELOPMENTAL STAGE: Localizes to the centrosome throughout the nuclear
CC division cycle in early syncytial embryos. Localization to the
CC interphase nucleus is seen from nuclear cycle 9 onwards.
CC {ECO:0000269|PubMed:1372522, ECO:0000269|PubMed:8491775,
CC ECO:0000269|PubMed:8586650, ECO:0000269|PubMed:8590797}.
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DR EMBL; Z50021; CAA90324.1; -; mRNA.
DR EMBL; AE014297; AAF55159.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13643.1; -; Genomic_DNA.
DR EMBL; BT010090; AAQ22559.1; -; mRNA.
DR PIR; T13802; T13802.
DR RefSeq; NP_524359.2; NM_079635.3.
DR RefSeq; NP_731998.1; NM_169632.2.
DR PDB; 4U77; X-ray; 2.03 A; A=1-134.
DR PDB; 5EUP; X-ray; 2.50 A; A=1-135.
DR PDB; 6ER1; X-ray; 1.40 A; A=1-126.
DR PDBsum; 4U77; -.
DR PDBsum; 5EUP; -.
DR PDBsum; 6ER1; -.
DR AlphaFoldDB; Q24478; -.
DR SMR; Q24478; -.
DR BioGRID; 66912; 72.
DR IntAct; Q24478; 17.
DR MINT; Q24478; -.
DR STRING; 7227.FBpp0082580; -.
DR iPTMnet; Q24478; -.
DR PaxDb; Q24478; -.
DR PRIDE; Q24478; -.
DR DNASU; 41848; -.
DR EnsemblMetazoa; FBtr0083126; FBpp0082580; FBgn0000283.
DR EnsemblMetazoa; FBtr0083127; FBpp0082581; FBgn0000283.
DR GeneID; 41848; -.
DR KEGG; dme:Dmel_CG6384; -.
DR CTD; 41848; -.
DR FlyBase; FBgn0000283; Cp190.
DR VEuPathDB; VectorBase:FBgn0000283; -.
DR eggNOG; KOG1181; Eukaryota.
DR GeneTree; ENSGT00940000170886; -.
DR HOGENOM; CLU_282038_0_0_1; -.
DR InParanoid; Q24478; -.
DR OMA; MIIEEEH; -.
DR OrthoDB; 327377at2759; -.
DR PhylomeDB; Q24478; -.
DR SignaLink; Q24478; -.
DR BioGRID-ORCS; 41848; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41848; -.
DR PRO; PR:Q24478; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000283; Expressed in egg cell and 31 other tissues.
DR Genevisible; Q24478; DM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000242; C:pericentriolar material; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0031208; F:POZ domain binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0140588; P:chromatin looping; IMP:FlyBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IGI:FlyBase.
DR GO; GO:0035191; P:nuclear axial expansion; IMP:FlyBase.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA-binding; Metal-binding; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1096
FT /note="Centrosome-associated zinc finger protein CP190"
FT /id="PRO_0000232629"
FT DOMAIN 30..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 538..561
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 567..590
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 126..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..271
FT /note="Nuclear localization"
FT REGION 366..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..508
FT /note="Centrosomal localization and interaction with
FT microtubules"
FT REGION 608..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 817
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 936
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1061
FT /note="G -> D (in Ref. 1; CAA90324)"
FT /evidence="ECO:0000305"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:6ER1"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6ER1"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:6ER1"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6ER1"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:6ER1"
SQ SEQUENCE 1096 AA; 121679 MW; 5CD5C5492B948D39 CRC64;
MGEVKSVKVD NWGVFFLQKL QNFFNKTDYC DLTLQFRDNS QLKVHRLVLS ACTDYFNVLE
QTCEIVDDAL IMPNEFQADV VVPIVNFMYT GTLEFELKMY GKLLRTAKEM NMTVLLKLLE
AHRRTMENVN RQQRPPSPKG IRRRTVGQPS SGLPQQRVLG PSPQSRNVAT PIAQRANTQR
GSTGNTMSRT SGGSNRSPYG DSSNVKQEPT SPFEQLRKGY NNNKRPAQTS LLSPPSKKPS
LEEVKEFAEQ QRMRKQIAAE YGDNDPEYDG GMLYDDVHAG DDDDDDMPPQ PSTSKQQSPQ
GTQTQLEHGS TTIILKQDSP SQTPTIIVKD SSNAKLNHTK IIAEVLRQYP HIVKGHKNIK
LKIMPNTPAA PTEKSAPATV KPPANQSSAT TSPHKKLHVS FKADKSTPLI TAQQKAASSQ
QKSGTSQTTG NQGTGANPPA NTAAAQKRRI DSKTMHALIA QGAENTTGPW LCLRCGVNGR
PISIPSYRGF RRHLINTHKE TIDPALCEHC GWRSVNNREL HFHMYMEHQT KSLLYTFAEC
ALCNQSYRTK GELEAHINEV HTDDNKQQCI YCNKVFEQEL QLYRHMKSYH KEQALEDGII
DETDEEFLGS QDEEEEAEGD EEQEPEQTGK VRILSDISLP ATSAITVQQA QQEQLQEEDV
EQVQQEVKFV GADGNEVELT DEQRKEILSQ LNQQQAGATA GGVVMVLSEP EAEHVKQETD
EKSLAGTEEE YDDSQIYSEL GAADSVESAK KNIADESKES IDNLEWAENL IAESEEQSNK
EPKSDKPRDD ISEKLKELTG DWTEDENDDD VDDKPATAEL ASELANKDPE PTVHEEEDDI
DLALQSLHKG PEEATEEKAS EESVTSADDA VDAVPNINSQ PEKMDVDSEA ADEKASKAEV
QIKKEAELEN DQEEFIKEDS PIPHSDSVAE LREAVTASEG EDDVHLEADN IRKELLDELI
AEAEKPDQEK DIVQSEENAT TEALDRSVTD EDDLVPPTQV STEQMEIDEP AAEKAAENNE
DTRTADEKEA VEDKPNQTQD VTTAEKPTLE SAKAGDEATS GEAASVDKVK SLISEWGDDD
EDEDENGVSA AAKEEL
