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 24-JAN-2024, entry version 184. DE RecName: Full=Centrosome-associated zinc finger protein Cp190 {ECO:0000305}; DE AltName: Full=Centrosomal protein 190kD {ECO:0000305}; DE AltName: Full=Microtubule associated protein 190kD {ECO:0000305}; DE Short=dMAP190; DE AltName: Full=Protein enhancer of mod(mdg4)4-1; 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 FUNCTION, INTERACTION WITH PITA AND ZIPIC, SUBCELLULAR LOCATION, AND RP DEVELOPMENTAL STAGE. RX PubMed=25342723; DOI=10.1101/gr.174169.114; RA Maksimenko O., Bartkuhn M., Stakhov V., Herold M., Zolotarev N., Jox T., RA Buxa M.K., Kirsch R., Bonchuk A., Fedotova A., Kyrchanova O., Renkawitz R., RA Georgiev P.; RT "Two new insulator proteins, Pita and ZIPIC, target CP190 to chromatin."; RL Genome Res. 25:89-99(2015). RN [21] 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). RN [22] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH PITA. RX PubMed=33752739; DOI=10.1186/s13072-021-00391-x; RA Sabirov M., Kyrchanova O., Pokholkova G.V., Bonchuk A., Klimenko N., RA Belova E., Zhimulev I.F., Maksimenko O., Georgiev P.; RT "Mechanism and functional role of the interaction between CP190 and the RT architectural protein Pita in Drosophila melanogaster."; RL Epigenetics Chromatin 14:16-16(2021). CC -!- FUNCTION: Plays a central role in chromatin domain organization and CC boundary function through recruitment by a range of insulator DNA- CC binding proteins, including ZIPIC, pita, CTCF, su(Hw) and others CC (PubMed:25342723, PubMed:33752739). Together with pita and CTCF CC cooperatively binds to and regulates the activity of the Miscadastral CC pigmentation (MCP) insulator (PubMed:25342723). Recruitment of Cp190 CC together with Chro/chromator induces chromatin decondensation CC (PubMed:33752739). Component of the gypsy chromatin insulator complex CC which is required for the function of the gypsy chromatin insulator and CC other endogenous chromatin insulators (PubMed:15574329). Chromatin CC insulators are regulatory elements that establish independent domains CC of transcriptional activity within eukaryotic genomes. Insulators have CC two defining properties; they can block the communication between an CC enhancer and a promoter when placed between them and can also buffer CC transgenes from position effect variegation (PEV). Insulators are CC proposed to structure the chromatin fiber into independent domains of CC differing transcriptional potential by promoting the formation of CC distinct chromatin loops to form topologically associating domains CC (TADs). This chromatin looping may involve the formation of insulator CC bodies, where homotypic interactions between individual subunits of the CC insulator complex could promote the clustering of widely spaced CC insulators at the nuclear periphery. Within the gypsy insulator CC complex, this protein may directly bind to insulator DNA at sites CC distinct from those recognized by su(Hw) (PubMed:15574329). Required CC during embryogenesis for axial expansion, an actin/myosin dependent CC process that distributes the dividing nuclei along the anterior- CC posterior axis of the syncytial embryo (PubMed:16051175). Localizes to CC centrosomes and recruits CP60 during mitosis but does not appear to CC play a crucial role in organizing centrosomal microtubules CC (PubMed:14996941, PubMed:16051175). {ECO:0000269|PubMed:14996941, CC ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:16051175, CC ECO:0000269|PubMed:25342723, ECO:0000269|PubMed:33752739}. 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). Interacts (via BTB domain) with pita (via CC region between the ZAD domain and the first zinc finger domain); the CC interaction is direct (PubMed:25342723, PubMed:33752739). Interacts CC with ZIPIC (via region between the ZAD domain and the first Zinc finger CC domain); the interaction is direct (PubMed:25342723). CC {ECO:0000269|PubMed:1372522, ECO:0000269|PubMed:14996941, CC ECO:0000269|PubMed:15574329, ECO:0000269|PubMed:25342723, CC ECO:0000269|PubMed:25561495, ECO:0000269|PubMed:28366641, CC ECO:0000269|PubMed:33752739, ECO:0000269|PubMed:8491775, CC ECO:0000269|PubMed:8522588, ECO:0000269|PubMed:8590797, CC ECO:0000269|PubMed:9700165}. CC -!- INTERACTION: CC Q24478; Q8T051: CG4639; NbExp=7; IntAct=EBI-868840, EBI-192200; CC Q24478; Q24478: Cp190; NbExp=3; IntAct=EBI-868840, EBI-868840; CC Q24478; Q8TA44: CTCF; NbExp=5; IntAct=EBI-868840, EBI-466743; CC Q24478; Q9VS55: CTCF; NbExp=5; IntAct=EBI-868840, EBI-149931; CC Q24478; Q9VBN9: Dmel\CG4730; NbExp=10; IntAct=EBI-868840, EBI-127047; 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; Q95RQ8: pita; NbExp=8; IntAct=EBI-868840, EBI-114363; CC Q24478; P08970: su(Hw); NbExp=12; IntAct=EBI-868840, EBI-101373; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14996941, CC ECO:0000269|PubMed:25342723}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:14996941, ECO:0000269|PubMed:8491775, CC ECO:0000269|PubMed:8522588, ECO:0000269|PubMed:8590797}. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14996941}. Chromosome CC {ECO:0000269|PubMed:25342723}. Note=Localizes to nucleus during CC interphase and to the centrosome during mitosis. Colocalizes with other CC elements of the gypsy chromatin insulator complex at multiple sites on CC polytene chromosomes and at nuclear insulator bodies. On polytene CC chromosomes of third-instar larvae colocalizes with pita and ZIPIC CC (PubMed:25342723). {ECO:0000269|PubMed:25342723}. 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: Expressed in 0-12 hour old embryos and 3rd instar CC larvae (at protein level) (PubMed:25342723). Localizes to the CC centrosome throughout the nuclear division cycle in early syncytial CC embryos. Localization to the interphase nucleus is seen from nuclear CC cycle 9 onwards. {ECO:0000269|PubMed:1372522, CC ECO:0000269|PubMed:25342723, ECO:0000269|PubMed:8491775, CC ECO:0000269|PubMed:8586650, ECO:0000269|PubMed:8590797}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 73. DR IntAct; Q24478; 19. DR MINT; Q24478; -. DR STRING; 7227.FBpp0082581; -. DR iPTMnet; Q24478; -. DR PaxDb; 7227-FBpp0082580; -. DR DNASU; 41848; -. DR EnsemblMetazoa; FBtr0083126; FBpp0082580; FBgn0000283. DR EnsemblMetazoa; FBtr0083127; FBpp0082581; FBgn0000283. DR GeneID; 41848; -. DR KEGG; dme:Dmel_CG6384; -. DR AGR; FB:FBgn0000283; -. 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; CGWRSAN; -. DR OrthoDB; 3682083at2759; -. DR PhylomeDB; Q24478; -. DR Reactome; R-DME-212436; Generic Transcription Pathway. 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 cell types or tissues. 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:0042802; F:identical protein binding; IPI:IntAct. 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: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:0006355; P:regulation of DNA-templated transcription; IMP:FlyBase. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd18311; BTB_POZ_CP190-like; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 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 PANTHER; PTHR24394:SF38; CENTROSOME-ASSOCIATED ZINC FINGER PROTEIN CP190; 1. DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1. DR Pfam; PF00651; BTB; 1. DR SMART; SM00225; BTB; 1. DR SMART; SM00355; ZnF_C2H2; 4. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR PROSITE; PS50097; BTB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. DR Genevisible; Q24478; DM. 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 245..468 FT /note="Centrosomal targeting M domain involved in FT interaction with ZIPIC" FT /evidence="ECO:0000269|PubMed:25342723" 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 //