ID  F6ZDS4;
PN  Nucleoprotein TPR;
GN  Tpr;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Nucleus Position: SL-0185;
SL  Comments: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side {ECO:0000250|UniProtKB:P12270}. Nucleus envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}. Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear foci with IFI204 (By similarity). In interphase, localizes to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Detected exclusively to the cytoplasmic margin of NPC (By similarity). Docking to the inner nucleoplasmic side of the NPC is mediated through binding to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC is a stepwise process in which Trp-containing peripheral structures assemble after other components, including p62. Detected as filaments that emanate from the nuclear basket of the NPC and extend to the nucleolus to delineate a chromatin-free network extending from the nuclear envelope to the perinucleolar region. Detected in diffuse and discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling protein imported into the nucleus in a XPO1/CRM1- and Importin alpha/Importin beta receptor-dependent manner. Remains localized to the nuclear membrane after poliovirus (PV) infection. During mitosis, remains associated with the nuclear envelope until prometaphase. Associated with the mitotic spindle from late prometaphase until anaphase. 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. Recruited to the reforming nuclear envelope during telophase and cytokinesis. Detected at kinetochores during prometaphase. Colocalizes with MAD2L1 in the spindle matrix but not at kinetochore. Colocalizes with dynein, dynactin, tubulin at kinetochore during the metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic spindle (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
DR  UNIPROT: F6ZDS4;
DR  UNIPROT: Q8R4A0;
DR  UNIPROT: Q921B9;
DR  Pfam: PF07926;
DE  Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral chromatin compartmentalization in interphase, and in the mitotic spindle checkpoint signaling during mitosis. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with NUP153, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Negatively regulates both the association of CTE-containing mRNA with large polyribosomes and translation initiation. Does not play any role in Rev response element (RRE)-mediated export of unspliced mRNAs. Implicated in nuclear export of mRNAs transcribed from heat shock gene promoters; associates both with chromatin in the HSP70 promoter and with mRNAs transcribed from this promoter under stress- induced conditions. Plays a limited role in the regulation of nuclear protein export. Modulates the nucleocytoplasmic transport of activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the XPO1/CRM1-mediated nuclear export complex. Also plays a role as a structural and functional element of the perinuclear chromatin distribution; involved in the formation and/or maintenance of NPC- associated perinuclear heterochromatin exclusion zones (HEZs). Finally, acts as a spatial regulator of the spindle-assembly checkpoint (SAC) response ensuring a timely and effective recruitment of spindle checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore during the metaphase-anaphase transition before chromosome congression. Its N-terminus is involved in activation of oncogenic kinases (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
DE  Interaction: Q7TPH6; IntAct: EBI-16731507; Score: 0.35
DE  Interaction: P83510; IntAct: EBI-16734044; Score: 0.35
GO  GO:0005737;
GO  GO:0005868;
GO  GO:0019898;
GO  GO:0000776;
GO  GO:0072686;
GO  GO:0005635;
GO  GO:0042405;
GO  GO:0031965;
GO  GO:0034399;
GO  GO:0005643;
GO  GO:0044615;
GO  GO:0005634;
GO  GO:0003682;
GO  GO:0070840;
GO  GO:0031072;
GO  GO:0051019;
GO  GO:0003729;
GO  GO:0042803;
GO  GO:0017056;
GO  GO:0015631;
GO  GO:0051301;
GO  GO:0034605;
GO  GO:0035457;
GO  GO:0007094;
GO  GO:0006406;
GO  GO:0031990;
GO  GO:0046832;
GO  GO:0000122;
GO  GO:0045947;
GO  GO:0006999;
GO  GO:0006913;
GO  GO:0031453;
GO  GO:0090316;
GO  GO:0090267;
GO  GO:0046827;
GO  GO:0042307;
GO  GO:0006611;
GO  GO:0006606;
GO  GO:0010965;
GO  GO:1901673;
GO  GO:0032880;
GO  GO:0070849;
GO  GO:0006405;
GO  GO:0006404;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:P12270};
SQ  MTSGGSASRSGHRGVPMTSRGFDGSRRGSLRRAGARETASEAADGAAPAAGLRASPCSLASPSAAAAVAAIPADMAAVLQ
SQ  QVLERPELNKLPKSTQNKLEKFLAEQQSEIDCLKGRHEKFKVESEQQYFEIEKRLSQSQERLVTETRECQNLRLELEKLN
SQ  NQVKVLTEKTKELETAQDRNLGIQSQFTRAKEELEAEKRDLIRTNERLSQEVEYLTEDVKRLNEKLKESNTTKGELQLKL
SQ  DELQASDVAVKYREKRLEQEKELLHNQNSWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVLRLEEQMNGLKTS
SQ  NEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVDELHKLLKEAGEANKTIQD
SQ  HLLQVEESKDQMEKEMLEKIGKLEKELENANDLLSATKRKGAILSEEELAAMSPTAAAVAKIVKPGMKLTELYNAYVETQ
SQ  DQLLLEKQENKRINKYLDEIVKEVEAKAPILKRQREEYERAQKAVASLSAKLEQAMKEIQRLQEDTDKANKHSSVLERDN
SQ  QRMEIQIKDLSQQIRVLLMELEEARGNHVIRDEEVSSADISSSSEVISQHLVSYRNIEELQQQNQRLLFALRELGETRER
SQ  EEQETTSSKIAELQHKLENSLAELEQLRESRQHQMQLVDSIVRQRDMYRILLSQTTGMAIPLQASSLDDISLLSTPKRSS
SQ  TSQTVSTPAPEPVIDSTEAIEAKAALKQLQEIFENYKKEKIDSEKLQNEQLEKLQEQVTDLRSQNTKISTQLDFASKRYE
SQ  MLQDNVEGYRREITSLQERNQKLTATTQKQEQIINTMTQDLRGANEKLAVAEVRAENLKKEKEMLKLSEVRLSQQRESLL
SQ  AEQRGQNLLLTNLQTIQGILERSETETKQRLNSQIEKLEHEISHLKKKLENEVEQRHTLTRNLDVQLLDTKRQLDTEINL
SQ  HLNTKELLKNAQKDIATLKQHLNNMEAQLASQSTQRTGKGQPGDRDDVDDLKSQLRQAEEQVNDLKERLKTSTSNVEQYR
SQ  AMVTSLEDSLNKEKQVTEEVHKNIEVRLKESAEFQTQLEKKLMEVEKEKQELQDDKRKAIESMEQQLSELKKTLSTVQNE
SQ  VQEALQRASTALSNEQQARRDCQEQAKIAVEAQNKYERELMLHAADVEALQAAKEQVSKMTSIRQHLEETTQKAESQLLE
SQ  CKASWEERERVLKDEVSKSVSRCEDLEKQNRLLHDQIEKLSDKVVTSMKDAVQAPLNVSLNEEGKSQEQILEILRFIRRE
SQ  KEIAETRFEVAQVESLRYRQRVELLERELQELQDSLNVEREKVQVTAKTMAQHEELMKKTETMNVVMETNKMLREEKERL
SQ  EQNLQQMQAKVRKLELDILPLQEANAELSEKSGMLQAEKKLLEEDVKRWKARNQQLINQQKDPDTEEYRKLLSEKEIHTK
SQ  RIQQLNEEVGRLKAEIARSNASLTNNQNLIQSLREDLSKARTEKEGIQKDLDAKIIDIQEKVKTITQVKKIGRRYKTQFE
SQ  ELKAQQNKAMETSTQSSGDHQEQHISVQEMQELKDTLSQSETKTKSLEGQVENLQKTLSEKETEARSLQEQTVQLQSELS
SQ  RLRQDLQDKTTEEQLRQQMNEKTWKTLALAKSKITHLSGVKDQLTKEIEELKQRNGALDQQKDELDVRMTALKSQYEGRI
SQ  SRLERELREHQERHLEQRDEPQEPTNKAPEQQRQITLKTTPASGERGIASTSDPPTANIKPTPVVSTPSKVTAAAMAGNK
SQ  STPRASIRPMVTPATVTNPTTTPTATVMPTTQVESQEAMQSEGPVEHVPVFGNASGSVRSTSPNVQPSISQPILTVQQQT
SQ  QATAFVQPTQQSHPQIEPTNQELSPNIVEVVQSSPVERPSTSTAVFGTVSATPSSSLPKRTREEEEDSTMEAGDQVSEDT
SQ  VEMPLPKKLKMVTPVGTEEEVMAEESTDGEAETQAYNQDSQDSIGEGVTQGDYTPMEDSEETSQSLQIDLGPLQSDQQTT
SQ  SSQDGQGKGDDVIVIDSDDEDDDEENDGEHEDYEEDEDDDDDEEDDTGMGDEGEDSNEGTGSADGNDGYEADDAEGGDGT
SQ  DPGTETEESMGGAESHQRAADSQNSGEGNTSAAESSFSQEVAREQQPTSASERQTPQAPQSPRRPPHPLPPRLTIHAPPQ
SQ  ELGPPVQRIQMTRRQSVGRGLQLTPGIGGMQQHFFDDEDRTVPSTPTLVVPHRTDGFAEAIHSPQVAGVPRFRFGPPEDM
SQ  PQTSSSHSDLGQLASQGGLGMYETPLFLAHEEESGGRSVPTTPLQVAAPVTVFTESTTSDASEHASQSVPMVTTSTGTLS
SQ  TTNETAAGDDGDEVFVEAESEGISSEAGLEIDSQQEEEPVQASDESDLPSTSQDPPSSSSVDTSSSQPKPFRRVRLQTTL
SQ  RQGVRGRQFNRQRGISHAMGGRGGINRGNIN
//