ID  A1Z8P9;
PN  Nucleoprotein TPR;
GN  Mtor;
OS  7227;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0180;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}. Nucleus matrix {ECO:0000269|PubMed:9152019}. Nucleus lamina {ECO:0000269|PubMed:15356261}. Nucleus envelope {ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:9152019}. Nucleus membrane {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:22855526}; Peripheral membrane protein {ECO:0000305}; Nucleoplasmic side {ECO:0000269|PubMed:12027452}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:9152019}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:18562695, ECO:0000269|PubMed:22855526}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19273613}. Midbody {ECO:0000269|PubMed:15356261}. Note=In interphase, localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket (PubMed:15356261). Enriched at the nuclear lamina and at intranuclear spaces surrounding the chromosomes and the nucleolus (PubMed:15356261, PubMed:15962301). Colocalized with hnRNPs and snRNPs at a single heat shock puff during heat shock (PubMed:12027452). Reorganized during mitosis in a viscous and dynamic nuclear-derived spindle matrix that embeds the microtubule spindle apparatus from pole to pole in a microtubule-independent manner (PubMed:15356261). In prometaphase, localized at the spindle (PubMed:15356261). Localized to spindle midbody at telophase (PubMed:15356261). Recruited to the reforming nuclear envelope in early G1 (PubMed:15356261). Colocalized with Skeletor, Chro and east at the spindle matrix (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). Colocalized with Mad2 at the spindle matrix and kinetochore (PubMed:19273613). Associated with chromatin (PubMed:20174442). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526}.
DR  UNIPROT: A1Z8P9;
DR  UNIPROT: O01385;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope (PubMed:9152019). Functions as a scaffolding element in the nuclear phase of the NPC (PubMed:12027452, PubMed:15356261). Plays a role in chromosomal organization and gene expression regulation; stimulates transcription by promoting the formation of an open chromatin environment (PubMed:12027452, PubMed:20174442). Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome (PubMed:20174442). Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy (PubMed:20174442). Preferentially binds to NARs of the male X chromosome (PubMed:20174442). In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes (PubMed:16543150). In males, restrains dosage-compensated expression at the level of nascent transcription probably by interacting with the MSL complex and by modulating RNA Polymerase II phosphorylation status and activity (PubMed:34133927). During mitosis forms a gel-like spindle matrix complex together with Skeletor, Chro, east, and Asator embedding the microtubule spindle apparatus (PubMed:15356261, PubMed:15962301, PubMed:19273613, PubMed:22855526). During interphase localizes Mad1 to the nuclear pore complex and thereby might act as a scaffold to assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2) which is essential for spindle-assembly checkpoint (SAC) (PubMed:31913420). During the metaphase-anaphase transition and before chromosome congression, is phosphorylated by Msp-1; this modification releases Mad1 from the nuclear pore complex and thereby promotes assembly of SAC ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores (KT) (PubMed:22855526, PubMed:26714316, PubMed:31913420). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex (PubMed:26714316). {ECO:0000269|PubMed:12027452, ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15962301, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:20174442, ECO:0000269|PubMed:22855526, ECO:0000269|PubMed:26714316, ECO:0000269|PubMed:31913420, ECO:0000269|PubMed:34133927, ECO:0000269|PubMed:9152019}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9VNZ7; IntAct: EBI-212088; Score: 0.00
DE  Interaction: Q9W1M6; IntAct: EBI-277787; Score: 0.00
DE  Interaction: P92177; IntAct: EBI-8283416; Score: 0.35
DE  Interaction: Q7JQU5; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VBD5; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: C7LA76; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9BIS2; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: P54623; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q8IRG6; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q7KV88; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VFA8; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VWF7; IntAct: EBI-9918472; Score: 0.35
DE  Interaction: Q9VG87; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9VXU3; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q24238; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9VDR4; IntAct: EBI-9943666; Score: 0.35
DE  Interaction: Q9W1X5; IntAct: EBI-9943666; Score: 0.35
GO  GO:0000775;
GO  GO:0005737;
GO  GO:0000791;
GO  GO:0070090;
GO  GO:0030496;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0005652;
GO  GO:0016363;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0005730;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0005819;
GO  GO:1990047;
GO  GO:0051233;
GO  GO:0031490;
GO  GO:0035035;
GO  GO:0043021;
GO  GO:0017056;
GO  GO:0006325;
GO  GO:0006338;
GO  GO:0007549;
GO  GO:0060250;
GO  GO:0048133;
GO  GO:0007094;
GO  GO:0000022;
GO  GO:0006406;
GO  GO:0000122;
GO  GO:0051781;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0045840;
GO  GO:0045944;
GO  GO:0006606;
GO  GO:0006355;
GO  GO:0090235;
GO  GO:0007346;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0060236;
GO  GO:0034976;
GO  GO:0009408;
GO  GO:0051225;
TP  Membrane Topology: Peripheral; Source: UniProt - Curator Inference {ECO:0000305};
SQ  MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNE
SQ  LRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIA
SQ  RVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAV
SQ  KTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQL
SQ  TEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSE
SQ  ELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENK
SQ  KLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASE
SQ  KNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSE
SQ  QPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQK
SQ  EQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEK
SQ  ETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDE
SQ  EKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREH
SQ  GEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLK
SQ  SLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELL
SQ  RSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRN
SQ  NEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAI
SQ  TDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEE
SQ  FKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKN
SQ  RLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDE
SQ  HEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKD
SQ  INQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASI
SQ  RPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTS
SQ  SHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTAT
SQ  APSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKR
SQ  LRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDN
SQ  EGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWK
SQ  QAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSG
SQ  SDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVS
SQ  SEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNR
SQ  FAQRTRNRRPIRRPPPNNFNNGGRFP
//