TPR_DROME
ID TPR_DROME Reviewed; 2346 AA.
AC A1Z8P9; O01385;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nucleoprotein TPR;
DE AltName: Full=Megator;
DE AltName: Full=Nuclear envelope antigen Bx34;
GN Name=Mtor {ECO:0000312|FlyBase:FBgn0013756};
GN Synonyms=Bx34 {ECO:0000303|PubMed:9152019,
GN ECO:0000312|FlyBase:FBgn0013756},
GN l(2)k03905 {ECO:0000312|FlyBase:FBgn0013756};
GN ORFNames=CG8274 {ECO:0000312|FlyBase:FBgn0013756};
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9152019; DOI=10.1242/jcs.110.8.927;
RA Zimowska G., Aris J.P., Paddy M.R.;
RT "A Drosophila Tpr protein homolog is localized both in the extrachromosomal
RT channel network and to nuclear pore complexes.";
RL J. Cell Sci. 110:927-944(1997).
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 FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12027452; DOI=10.1006/excr.2002.5525;
RA Zimowska G., Paddy M.R.;
RT "Structures and dynamics of Drosophila Tpr inconsistent with a static,
RT filamentous structure.";
RL Exp. Cell Res. 276:223-232(2002).
RN [5]
RP FUNCTION, INTERACTION WITH CHRO, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15356261; DOI=10.1091/mbc.e04-07-0579;
RA Qi H., Rath U., Wang D., Xu Y.Z., Ding Y., Zhang W., Blacketer M.J.,
RA Paddy M.R., Girton J., Johansen J., Johansen K.M.;
RT "Megator, an essential coiled-coil protein that localizes to the putative
RT spindle matrix during mitosis in Drosophila.";
RL Mol. Biol. Cell 15:4854-4865(2004).
RN [6]
RP FUNCTION, INTERACTION WITH EAST, AND SUBCELLULAR LOCATION.
RX PubMed=15962301; DOI=10.1002/jcb.20495;
RA Qi H., Rath U., Ding Y., Ji Y., Blacketer M.J., Girton J., Johansen J.,
RA Johansen K.M.;
RT "EAST interacts with Megator and localizes to the putative spindle matrix
RT during mitosis in Drosophila.";
RL J. Cell. Biochem. 95:1284-1291(2005).
RN [7]
RP FUNCTION, ASSOCIATION WITH THE MSL COMPLEX, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18562695; DOI=10.1091/mbc.e07-11-1162;
RA Katsani K.R., Karess R.E., Dostatni N., Doye V.;
RT "In vivo dynamics of Drosophila nuclear envelope components.";
RL Mol. Biol. Cell 19:3652-3666(2008).
RN [9]
RP INTERACTION WITH ASATOR.
RX PubMed=19890914; DOI=10.1002/dvdy.22150;
RA Qi H., Yao C., Cai W., Girton J., Johansen K.M., Johansen J.;
RT "Asator, a tau-tubulin kinase homolog in Drosophila localizes to the
RT mitotic spindle.";
RL Dev. Dyn. 238:3248-3256(2009).
RN [10]
RP FUNCTION, INTERACTION WITH MAD2, AND SUBCELLULAR LOCATION.
RX PubMed=19273613; DOI=10.1083/jcb.200811012;
RA Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E.,
RA Tavares A., Johansen J., Johansen K.M., Maiato H.;
RT "Spatiotemporal control of mitosis by the conserved spindle matrix protein
RT Megator.";
RL J. Cell Biol. 184:647-657(2009).
RN [11]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=20174442; DOI=10.1371/journal.pgen.1000846;
RA Vaquerizas J.M., Suyama R., Kind J., Miura K., Luscombe N.M., Akhtar A.;
RT "Nuclear pore proteins nup153 and megator define transcriptionally active
RT regions in the Drosophila genome.";
RL PLoS Genet. 6:E1000846-E1000846(2010).
RN [12]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=22855526; DOI=10.1091/mbc.e12-06-0429;
RA Yao C., Rath U., Maiato H., Sharp D., Girton J., Johansen K.M.,
RA Johansen J.;
RT "A nuclear-derived proteinaceous matrix embeds the microtubule spindle
RT apparatus during mitosis.";
RL Mol. Biol. Cell 23:3532-3541(2012).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26714316; DOI=10.1371/journal.pgen.1005750;
RA Liu Y., Singh S.R., Zeng X., Zhao J., Hou S.X.;
RT "The Nuclear Matrix Protein Megator Regulates Stem Cell Asymmetric Division
RT through the Mitotic Checkpoint Complex in Drosophila Testes.";
RL PLoS Genet. 11:E1005750-E1005750(2015).
RN [14]
RP INTERACTS 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 [15]
RP FUNCTION, INTERACTION WITH MAD1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP THR-1259; THR-1302; THR-1338 AND THR-1390, AND MUTAGENESIS OF THR-1259;
RP THR-1302; THR-1338 AND THR-1390.
RX PubMed=31913420; DOI=10.1083/jcb.201906039;
RA Cunha-Silva S., Osswald M., Goemann J., Barbosa J., Santos L.M.,
RA Resende P., Bange T., Ferras C., Sunkel C.E., Conde C.;
RT "Mps1-mediated release of Mad1 from nuclear pores ensures the fidelity of
RT chromosome segregation.";
RL J. Cell Biol. 219:0-0(2020).
RN [16]
RP FUNCTION, INTERACTION WITH MOF, AND DISRUPTION PHENOTYPE.
RX PubMed=34133927; DOI=10.1016/j.celrep.2021.109236;
RA Aleman J.R., Kuhn T.M., Pascual-Garcia P., Gospocic J., Lan Y., Bonasio R.,
RA Little S.C., Capelson M.;
RT "Correct dosage of X chromosome transcription is controlled by a nuclear
RT pore component.";
RL Cell Rep. 35:109236-109236(2021).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope
CC (PubMed:9152019). Functions as a scaffolding element in the nuclear
CC phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in
CC chromosomal organization and gene expression regulation; stimulates
CC transcription by promoting the formation of an open chromatin
CC environment (PubMed:12027452, PubMed:20174442). Binds chromatin to
CC nucleoporin-associated regions (NARs) that define transcriptionally
CC active regions of the genome (PubMed:20174442). Associates with
CC extended chromosomal regions that alternate between domains of high
CC density binding with those of low occupancy (PubMed:20174442).
CC Preferentially binds to NARs of the male X chromosome
CC (PubMed:20174442). In males, together with Nup153, required for the
CC localization of the male-specific lethal (MSL) histone
CC acetyltransferase complex to the X chromosome and therefore for the
CC transcription of dosage compensation genes (PubMed:16543150). In males,
CC restrains dosage-compensated expression at the level of nascent
CC transcription probably by interacting with the MSL complex and by
CC modulating RNA Polymerase II phosphorylation status and activity
CC (PubMed:34133927). During mitosis forms a gel-like spindle matrix
CC complex together with Skeletor, Chro, east, and Asator embedding the
CC microtubule spindle apparatus (PubMed:15356261, PubMed:15962301,
CC PubMed:19273613, PubMed:22855526). During interphase localizes Mad1 to
CC the nuclear pore complex and thereby might act as a scaffold to
CC assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the
CC structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2)
CC which is essential for spindle-assembly checkpoint (SAC)
CC (PubMed:31913420). During the metaphase-anaphase transition and before
CC chromosome congression, is phosphorylated by Msp-1; this modification
CC releases Mad1 from the nuclear pore complex and thereby promotes
CC assembly of SAC ensuring a timely and effective recruitment of spindle
CC checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores
CC (KT) (PubMed:22855526, PubMed:26714316, PubMed:31913420). In testes,
CC has a role in stem cell asymmetric division and maintenance via
CC regulation of mitotic spindle assembly checkpoint (SAC) complex
CC (PubMed:26714316). {ECO:0000269|PubMed:12027452,
CC ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301,
CC ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19273613,
CC ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526,
CC ECO:0000269|PubMed:26714316, ECO:0000269|PubMed:31913420,
CC ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9152019}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:9152019,
CC PubMed:12027452, PubMed:22855526). Associates with male-specific lethal
CC (MSL) histone acetyltransferase complex (PubMed:16543150). Interacts
CC with Mad2; the interaction is required for efficient recruitment of
CC Mad2 to unattached kinetochore and occurs in a microtubule-independent
CC manner (PubMed:19273613). Interacts with Mad1 (N-terminus)
CC (PubMed:31913420). Interacts with Chro, east and Asator; the
CC interaction is part of a macromolecular complex forming the spindle
CC matrix during mitosis (PubMed:15356261, PubMed:15962301,
CC PubMed:19890914). Interacts with Nup98 (PubMed:28366641). In males,
CC interacts with histone acetyltransferase mof (PubMed:34133927).
CC {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261,
CC ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:19890914,
CC ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:28366641,
CC ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:34133927,
CC ECO:0000269|PubMed:9152019}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12027452,
CC ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442,
CC ECO:0000269|PubMed:22855526}. Nucleus matrix
CC {ECO:0000269|PubMed:9152019}. Nucleus lamina
CC {ECO:0000269|PubMed:15356261}. Nucleus envelope
CC {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucleus
CC membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:22855526};
CC Peripheral membrane protein {ECO:0000305}; Nucleoplasmic side
CC {ECO:0000269|PubMed:12027452}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:22855526,
CC ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:9152019}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15356261,
CC ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:22855526}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19273613}. Midbody
CC {ECO:0000269|PubMed:15356261}. Note=In interphase, localized to the
CC nucleoplasmic side of the nuclear pore complex (NPC) core structure,
CC forming a fibrous structure called the nuclear basket
CC (PubMed:15356261). Enriched at the nuclear lamina and at intranuclear
CC spaces surrounding the chromosomes and the nucleolus (PubMed:15356261,
CC PubMed:15962301). Colocalized with hnRNPs and snRNPs at a single heat
CC shock puff during heat shock (PubMed:12027452). Reorganized during
CC mitosis in a viscous and dynamic nuclear-derived spindle matrix that
CC embeds the microtubule spindle apparatus from pole to pole in a
CC microtubule-independent manner (PubMed:15356261). In prometaphase,
CC localized at the spindle (PubMed:15356261). Localized to spindle
CC midbody at telophase (PubMed:15356261). Recruited to the reforming
CC nuclear envelope in early G1 (PubMed:15356261). Colocalized with
CC Skeletor, Chro and east at the spindle matrix (PubMed:15356261,
CC PubMed:15962301, PubMed:19273613, PubMed:22855526). Colocalized with
CC Mad2 at the spindle matrix and kinetochore (PubMed:19273613).
CC Associated with chromatin (PubMed:20174442).
CC {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261,
CC ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:19273613,
CC ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands, fat body, tracheal
CC tube, esophageal tube and anterior ejaculatory duct (at protein level).
CC {ECO:0000269|PubMed:9152019}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages
CC (PubMed:9152019). Expressed in embryos (at protein level)
CC (PubMed:16543150). {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:9152019}.
CC -!- DOMAIN: The N-terminal coiled-coil domain is required for both nuclear
CC pore complex (NPC) and spindle matrix localization.
CC {ECO:0000269|PubMed:22855526}.
CC -!- DOMAIN: The C-terminal domain is required for interchromosomal
CC localization during interphase (PubMed:15356261). The C-terminal domain
CC is sufficient for localization to the nuclear lamina as well as for
CC spindle localization (PubMed:15356261). {ECO:0000269|PubMed:15356261}.
CC -!- PTM: Mps1-mediated phosphorylation disrupts interaction with Mad1
CC during mitosis. {ECO:0000269|PubMed:31913420}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the whole body or
CC specifically in the germ line results in a decreased number of germinal
CC stem cells (GSCs) in the testes (PubMed:26714316). RNAi-mediated in the
CC testes results in mislocalization of microtubule-regulating protein
CC Apc2 and shg/E-cadherin, defective centrosome orientation, mitotic
CC spindle formation and chromosome segretation (PubMed:26714316). RNAi-
CC mediated knockdown in male salivary glands increases male-specific gene
CC expression on X chromosome and nuclear expression of roX1 and roX2, two
CC long non-coding RNAs (lncRNAs) part of the males-specific lethal (MSL)
CC complex (PubMed:34133927). Simultaneous RNAi-mediated knockdown of Mtor
CC with RNAi-mediated knockdown of mof or the lncRNAs roX1 or roX2 in male
CC salivary glands results in a rescue of up-regulated X chromosome gene
CC expression (PubMed:34133927). {ECO:0000269|PubMed:26714316,
CC ECO:0000269|PubMed:34133927}.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
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; U91980; AAC47506.1; -; mRNA.
DR EMBL; AE013599; AAF58615.1; -; Genomic_DNA.
DR PIR; T13829; T13829.
DR RefSeq; NP_001260903.1; NM_001273974.1.
DR RefSeq; NP_477067.2; NM_057719.4.
DR AlphaFoldDB; A1Z8P9; -.
DR SMR; A1Z8P9; -.
DR BioGRID; 62050; 23.
DR IntAct; A1Z8P9; 16.
DR MINT; A1Z8P9; -.
DR STRING; 7227.FBpp0304737; -.
DR PaxDb; A1Z8P9; -.
DR PRIDE; A1Z8P9; -.
DR EnsemblMetazoa; FBtr0088033; FBpp0087140; FBgn0013756.
DR EnsemblMetazoa; FBtr0332464; FBpp0304737; FBgn0013756.
DR GeneID; 36264; -.
DR KEGG; dme:Dmel_CG8274; -.
DR UCSC; CG8274-RA; d. melanogaster.
DR CTD; 2475; -.
DR FlyBase; FBgn0013756; Mtor.
DR VEuPathDB; VectorBase:FBgn0013756; -.
DR eggNOG; KOG4674; Eukaryota.
DR GeneTree; ENSGT00730000111014; -.
DR HOGENOM; CLU_001130_0_0_1; -.
DR InParanoid; A1Z8P9; -.
DR OMA; KYDRVDP; -.
DR OrthoDB; 20957at2759; -.
DR PhylomeDB; A1Z8P9; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 36264; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36264; -.
DR PRO; PR:A1Z8P9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013756; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; A1Z8P9; baseline and differential.
DR Genevisible; A1Z8P9; DM.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0070090; C:metaphase plate; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:1990047; C:spindle matrix; IDA:FlyBase.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:FlyBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0007549; P:dosage compensation; IMP:UniProtKB.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:FlyBase.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR GO; GO:0090235; P:regulation of metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0010965; P:regulation of mitotic sister chromatid separation; IMP:FlyBase.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IDA:FlyBase.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; Cell division; Centromere; Chromatin regulator;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding; Kinetochore;
KW Membrane; Mitosis; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport.
FT CHAIN 1..2346
FT /note="Nucleoprotein TPR"
FT /id="PRO_0000422103"
FT REGION 622..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1655
FT /note="Interacts with Mad1"
FT /evidence="ECO:0000269|PubMed:31913420"
FT REGION 1621..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..190
FT /evidence="ECO:0000255"
FT COILED 217..366
FT /evidence="ECO:0000255"
FT COILED 395..493
FT /evidence="ECO:0000255"
FT COILED 565..596
FT /evidence="ECO:0000255"
FT COILED 643..1158
FT /evidence="ECO:0000255"
FT COILED 1196..1247
FT /evidence="ECO:0000255"
FT COILED 1281..1536
FT /evidence="ECO:0000255"
FT COILED 1579..1627
FT /evidence="ECO:0000255"
FT COMPBIAS 622..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..2019
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2140..2159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2246..2262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31913420"
FT MOD_RES 1302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31913420"
FT MOD_RES 1338
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31913420"
FT MOD_RES 1390
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1259
FT /note="T->A: Retains binding to Mad1; when associated with
FT A-1302; A-1338 and A-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1259
FT /note="T->D: Loss of binding to Mad1 and reduction of
FT closed-Mad2 levels at unattached kinetochores; when
FT associated with D-1302; D-1338 and D-1390 or with D-1338
FT and D-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1302
FT /note="T->A: Retains binding to Mad1; when associated with
FT A-1259; A-1338 and A-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1302
FT /note="T->D: Loss of binding to Mad1 and reduction of
FT closed-Mad2 levels at unattached kinetochores; when
FT associated with D-1259; D-1338 and D-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1338
FT /note="T->A: Retains binding to Mad1; when associated with
FT A-1259; A-1302 and A-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1338
FT /note="T->D: Loss of binding to Mad1 and reduction of
FT closed-Mad2 levels at unattached kinetochores; when
FT associated with D-1259; D-1302 and D-1390 or with D-1259
FT and D-1390."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1390
FT /note="T->A: Retains binding to Mad1; when associated with
FT A-1259; A-1302 and A-1338."
FT /evidence="ECO:0000269|PubMed:31913420"
FT MUTAGEN 1390
FT /note="T->D: Loss of binding to Mad1 and reduction of
FT closed-Mad2 levels at unattached kinetochores; when
FT associated with D-1259; D-1302 and D-1338 or with D-1259
FT and D-1338."
FT /evidence="ECO:0000269|PubMed:31913420"
FT CONFLICT 648
FT /note="E -> K (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="E -> G (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="K -> T (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="P -> H (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="E -> V (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="A -> S (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142
FT /note="A -> S (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1596
FT /note="A -> V (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 1889
FT /note="S -> L (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 2058
FT /note="I -> T (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
FT CONFLICT 2146
FT /note="A -> V (in Ref. 1; AAC47506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2346 AA; 262353 MW; C61BFD3F9C350B21 CRC64;
MDLSGPQTLN NILQPDELKL VPEDVQKKLS EYINNFSDEY CKNRAAANRL AEAEQKKEEL
ENKMEDYLVK FTSFELNVNE LRTHLDQMSS ERVNLMDTIA KGEQTISQLR KEKASVVEER
DSMMKVIERQ QAELERLKQD LHTYQQQLSS AIAAKCEAIA RVDEIQSKEV ALELKENRME
SERDMLHKEI LLISGDLNKS NAELQNIRRE HTINTMQLQS CLKEKTESLK LMQEQYEQAV
KTIGELTSKI EMQNDTAFKQ NQATEEYVGK LKKELDAKEK LFEIFKSTES DHLIQREELL
QGISEIKRLL EEAEEQCAQL TEQMETMKQK HSAELDEQNK KIQAMEQELA SANDLLKQAR
ESNLESAICQ LAPSAAVASR LIRSDLSLTE LYSMYAKSSE ELEMRNCEIE QLKLQLKSII
AEISESAPIL EKQNSDYQKM KETNSELLRE HDELLQNKLC LERELERALS TLNHNQNENK
KLKQTHTDLS RQVCMLLDEL NCIRAGVKHV RIQPTRQLPT SESLISDNLV TFSSIEELVD
RNTYLLNMSR ELTELLEASE KNQDKMLLEQ SKNHIRKLDA RFAELEDLLT QKNNTVTTLL
SKCDRYKKLY FAAQKKLGQN TVDLDDSNLE PNDSALDTSE QPAANFEESR KLEKRVRQLE
QQLEGEVKKY ASLKENYDYY TSEKRKNDAL AQEQFDSMRK EVRELTSSNC KLMNTTEFQK
EQIELLHKNI GTYKQQVTTL EERTKNYEKT IIKHEQTVHL LKDEMMAAHR KHAAADAEAQ
SLRQENRILR DTSSRLQIEK ETYHREQQSQ SLLLNSLEFI KTNLERSEME GRQRLEQRLD
DTVRELAAQR RHFQEEEEKF RESINEFKRQ AETAIKLKDE EKQLADKWQA ELTSVREELA
EKVNKVNELS KKLQEVLTPT LNDNPITAAN KRAREFELKL DQATVEIESL TKELAKTREH
GEQFYKMSQS AESEIKRLHE LHGELVAKQE EEIKKLRSSE AELKTRISDL EAEAMLSNVT
EQSKTVNQSG QLKSAQDDLK SLLEKLTEAN CTIRTLRSEN TSLVESLNAA EVKYANGMIQ
HSADIQELTR YKAEFFKAND ELNQLKSGRE SLQAAYDELL RSNAEAQKLL DKEREESEKR
VADLHALNSN LHDQIEALAS KLAVLASQSQ NPNSSLNESA MDGDQSLNAS GLTAAEEGRN
NEQLLKIIKF LRKEKDLFAA KLDILKAENA RLISEHAIQQ KKVDELNGYL NQERAKSQTD
VVSANKHEEV LRKIETLNAI TDSNRILREE RNALTLRVAE LTDRISSVEK ELFPLQCSNK
ELTSKIEEIN VENTSLRTEA IKWRQRANAL VEKSNRNPEE FKRLQAEREH LAKLLTAEKE
LNKKQSDELT VLKQRMNTEI PMLNKQMQIL DEARKKQVDE FTNLKQNNTR QTQDIMELKN
RLLQKEEELL KANEELETKD KTIADKETKE LQLRKLAKRY KDFYIGLQSQ GGGTESAAEL
EKVRSELEEV NNQLRALKDE HEKITKECDE VKKRTEPETD TSAIRQEYKA KLDKLVVDLT
VARTDLVNQE TTFAGTKSSY DETIARLEKE LQENIAANKD INQRLTRENE SLHMRINQLT
RQLGSQQSTK PSTSSVAEKG NISESSPRTA NVKPMSGSAT VQQSATVTPW RGGETPLASI
RPISVQNSRT AAILPTSQQP PAGSSTSTSS SSSSSSTSTT SAAGGGSSAV AQTALVPPQQ
QVHTTGSAAL ESMASSSPTS SHTDYMPSTS SASVAVAAIP PMGASSAAES SQEAESIQHP
QQNDSQLFVG GAQQQVVALV SPRVEGSSSS SSSTSVPTAT APSIQDGGSQ SQQPSTSGSS
SSSSTVVSSH SRHTPSSSNV TTTQAGCSSQ GIKRPRDIEG DSSTGTEEGV AEKMSKITKR
LRGPMHSGEL SAGHIGDSGM DVDQMPTSSQ RDQEDDIQVV DSDDEEDVLA DADDGPIDGG
EAEQEGYEDS YEQDNEMDDN EGGDDDNDIA VDAQDNNEVD IEVPEQHMQA QEESQSLDNQ
AIATASASTQ ENNQSQAITS GSGESSNPVT LPQAEASNWK QAAASTSTAA ARRNESSVEI
VSSPQVSNFC EQPARLESAE VDGTAEVAGG APHESAGPSD TGAASASSPQ KQSEAGESSG
SDALKAADDG GDHADGTDNA READEAFAEE TMATGQGEDS QPLGNDNPNV GTSQSEVSHN
QANLGEGNPT EDSEGADGVS SEGEKQAVGV EEEGREAEAT SPSENTRFRT LRSAVPTRRG
HRAMRGGSPN SQNRPQRIVW QRDTSPGNIQ QNQMSANNNR FAQRTRNRRP IRRPPPNNFN
NGGRFP
