TPR_MOUSE
ID TPR_MOUSE Reviewed; 2431 AA.
AC F6ZDS4; Q8R4A0; Q921B9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Nucleoprotein TPR;
DE AltName: Full=NPC-associated intranuclear protein;
DE AltName: Full=Translocated promoter region and nuclear basket protein;
GN Name=Tpr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-1274, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Ola;
RX PubMed=12424524; DOI=10.1007/s00412-002-0208-2;
RA Kuznetsov N.V., Sandblad L., Hase M.E., Hunziker A., Hergt M., Cordes V.C.;
RT "The evolutionarily conserved single-copy gene for murine Tpr encodes one
RT prevalent isoform in somatic cells and lacks paralogs in higher
RT eukaryotes.";
RL Chromosoma 111:236-255(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1229-2431, INTERACTION WITH IFI203 AND
RP IFI204, AND SUBCELLULAR LOCATION.
RC TISSUE=Fibroblast;
RX PubMed=12513910; DOI=10.1089/10799900260442539;
RA De Andrea M., Zannetti C., Noris E., Gariglio M., Azzimonti B.,
RA Landolfo S.;
RT "The mouse interferon-inducible gene Ifi204 product interacts with the Tpr
RT protein, a component of the nuclear pore complex.";
RL J. Interferon Cytokine Res. 22:1113-1121(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259 AND SER-2223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259; SER-2141; THR-2184 AND
RP SER-2223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-551; LYS-787; LYS-822; LYS-829
RP AND LYS-1760, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2174; ARG-2179; ARG-2231;
RP ARG-2411; ARG-2413 AND ARG-2422, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs, plays a role
CC in the establishment of nuclear-peripheral chromatin
CC compartmentalization in interphase, and in the mitotic spindle
CC checkpoint signaling during mitosis. Involved in the quality control
CC and retention of unspliced mRNAs in the nucleus; in association with
CC NUP153, regulates the nuclear export of unspliced mRNA species bearing
CC constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent
CC manner. Negatively regulates both the association of CTE-containing
CC mRNA with large polyribosomes and translation initiation. Does not play
CC any role in Rev response element (RRE)-mediated export of unspliced
CC mRNAs. Implicated in nuclear export of mRNAs transcribed from heat
CC shock gene promoters; associates both with chromatin in the HSP70
CC promoter and with mRNAs transcribed from this promoter under stress-
CC induced conditions. Plays a limited role in the regulation of nuclear
CC protein export. Modulates the nucleocytoplasmic transport of activated
CC MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site for the
CC XPO1/CRM1-mediated nuclear export complex. Also plays a role as a
CC structural and functional element of the perinuclear chromatin
CC distribution; involved in the formation and/or maintenance of NPC-
CC associated perinuclear heterochromatin exclusion zones (HEZs). Finally,
CC acts as a spatial regulator of the spindle-assembly checkpoint (SAC)
CC response ensuring a timely and effective recruitment of spindle
CC checkpoint proteins like MAD1L1 and MAD2L1 to unattached kinetochore
CC during the metaphase-anaphase transition before chromosome congression.
CC Its N-terminus is involved in activation of oncogenic kinases (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC). Associates
CC with the XPO1/CRM1-mediated nuclear export complex, the Importin
CC alpha/Importin beta receptor and the dynein 1 complex. Interacts (via
CC C-terminal domain) with the KPNB1; the interaction occurs in a RanGTP-
CC dependent manner. Interacts (via C-terminal region and phosphorylated
CC form) with MAPK1/ERK2 (via phosphorylated form); the interaction
CC requires dimerization of MAPK1/ERK2 and increases following EGF
CC stimulation. Interacts with MAPK3/ERK1; the interaction increases
CC following EGF stimulation. Interacts (via coiled coil region) with
CC NUP153; the interaction is direct. Interacts with HSF1; the interaction
CC increases in a stress-responsive manner and stimulates export of
CC stress-induced HSP70 mRNA. Interacts with huntingtin/HTT; the
CC interaction is inhibited by aggregated huntingtin/HTT forms with
CC expanded polyglutamine stretch. Interacts with MAD1L1 (via N-terminal
CC region), MAD2L1, and TTK; the interactions occurs in a microtubule-
CC independent manner. Interacts (via middle region) with DYNLL1.
CC Interacts with DCTN1, dynein, NUP153 and tubulin. Interacts with MTA1
CC (By similarity). Interacts with IFI204 (via C-terminal region).
CC Interacts with IFI203. {ECO:0000250, ECO:0000269|PubMed:12513910}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus
CC membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P12270}. Nucleus envelope
CC {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:12513910}. Nucleus,
CC nuclear pore complex {ECO:0000250|UniProtKB:P12270,
CC ECO:0000269|PubMed:12513910}. Cytoplasm {ECO:0000250|UniProtKB:P12270}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}.
CC Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P12270}. Note=Detected as discrete intranuclear
CC foci with IFI204 (By similarity). In interphase, localizes to the
CC nucleoplasmic side of the nuclear pore complex (NPC) core structure,
CC forming a fibrous structure called the nuclear basket. Detected
CC exclusively to the cytoplasmic margin of NPC (By similarity). Docking
CC to the inner nucleoplasmic side of the NPC is mediated through binding
CC to nucleoporins. Anchored by NUP153 to the NPC. The assembly of the NPC
CC is a stepwise process in which Trp-containing peripheral structures
CC assemble after other components, including p62. Detected as filaments
CC that emanate from the nuclear basket of the NPC and extend to the
CC nucleolus to delineate a chromatin-free network extending from the
CC nuclear envelope to the perinucleolar region. Detected in diffuse and
CC discrete spheroidal intranuclear foci. Nucleocytoplasmic shuttling
CC protein imported into the nucleus in a XPO1/CRM1- and Importin
CC alpha/Importin beta receptor-dependent manner. Remains localized to the
CC nuclear membrane after poliovirus (PV) infection. During mitosis,
CC remains associated with the nuclear envelope until prometaphase.
CC Associated with the mitotic spindle from late prometaphase until
CC anaphase. Reorganized during mitosis in a viscous and dynamic nuclear-
CC derived spindle matrix that embeds the microtubule spindle apparatus
CC from pole to pole in a microtubule-independent manner. Recruited to the
CC reforming nuclear envelope during telophase and cytokinesis. Detected
CC at kinetochores during prometaphase. Colocalizes with MAD2L1 in the
CC spindle matrix but not at kinetochore. Colocalizes with dynein,
CC dynactin, tubulin at kinetochore during the metaphase-anaphase
CC transition. Colocalizes with DYNLL1 at the mitotic spindle (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12270}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart, liver, kidney, spleen, lung
CC and skeletal muscles. {ECO:0000269|PubMed:12424524}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at the mid two-cell stage and in the embryo at 7, 11, 15 and
CC 17 dpc. {ECO:0000269|PubMed:12424524}.
CC -!- DOMAIN: The N-terminal domain mediates intranuclear attachment to the
CC nuclear pore complex. The C-terminal domain mediates its nuclear import
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs on serine and threonine
CC residues (comprised in the C-terminal region) by MAPK1/ERK2 and
CC stabilizes the interaction between these two proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
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DR EMBL; AC161432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466520; EDL39478.1; -; Genomic_DNA.
DR EMBL; AJ298076; CAC40701.1; -; Genomic_DNA.
DR EMBL; AF490392; AAM03151.1; -; mRNA.
DR CCDS; CCDS35734.2; -.
DR RefSeq; NP_598541.3; NM_133780.3.
DR AlphaFoldDB; F6ZDS4; -.
DR SMR; F6ZDS4; -.
DR BioGRID; 224509; 35.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; F6ZDS4; 2.
DR STRING; 10090.ENSMUSP00000117616; -.
DR BindingDB; F6ZDS4; -.
DR iPTMnet; F6ZDS4; -.
DR PhosphoSitePlus; F6ZDS4; -.
DR EPD; F6ZDS4; -.
DR jPOST; F6ZDS4; -.
DR MaxQB; F6ZDS4; -.
DR PaxDb; F6ZDS4; -.
DR PeptideAtlas; F6ZDS4; -.
DR PRIDE; F6ZDS4; -.
DR ProteomicsDB; 259073; -.
DR Antibodypedia; 11198; 224 antibodies from 30 providers.
DR DNASU; 108989; -.
DR Ensembl; ENSMUST00000124973; ENSMUSP00000117616; ENSMUSG00000006005.
DR GeneID; 108989; -.
DR KEGG; mmu:108989; -.
DR UCSC; uc007cyb.2; mouse.
DR CTD; 7175; -.
DR MGI; MGI:1922066; Tpr.
DR VEuPathDB; HostDB:ENSMUSG00000006005; -.
DR eggNOG; KOG4674; Eukaryota.
DR GeneTree; ENSGT00730000111014; -.
DR InParanoid; F6ZDS4; -.
DR OMA; KYDRVDP; -.
DR OrthoDB; 20957at2759; -.
DR PhylomeDB; F6ZDS4; -.
DR TreeFam; TF350364; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 108989; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Tpr; mouse.
DR PRO; PR:F6ZDS4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; F6ZDS4; protein.
DR Bgee; ENSMUSG00000006005; Expressed in undifferentiated genital tubercle and 269 other tissues.
DR ExpressionAtlas; F6ZDS4; baseline and differential.
DR Genevisible; F6ZDS4; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; ISS:UniProtKB.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006999; P:nuclear pore organization; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0010965; P:regulation of mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006404; P:RNA import into nucleus; ISS:UniProtKB.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Membrane; Methylation;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Proto-oncogene; Reference proteome; Translocation;
KW Transport.
FT CHAIN 1..2431
FT /note="Nucleoprotein TPR"
FT /id="PRO_0000422100"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..87
FT /note="Sufficient for interaction with TPR"
FT /evidence="ECO:0000250"
FT REGION 88..191
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000250"
FT REGION 511..587
FT /note="Necessary for association to the NPC"
FT /evidence="ECO:0000250"
FT REGION 989..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1394
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000250"
FT REGION 1689..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..2193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1937
FT /note="Sufficient and essential for mediating its nuclear
FT import"
FT /evidence="ECO:0000250"
FT REGION 2295..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..444
FT /evidence="ECO:0000255"
FT COILED 486..678
FT /evidence="ECO:0000255"
FT COILED 736..1246
FT /evidence="ECO:0000255"
FT COILED 1289..1494
FT /evidence="ECO:0000255"
FT COILED 1547..1700
FT /evidence="ECO:0000255"
FT COMPBIAS 1689..1706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1975..2007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2053
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2082
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2096..2138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2139..2158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2295..2327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2364..2393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 419
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 502
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 531
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 787
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 797
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 822
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 829
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1760
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1762
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 1963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2174
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2179
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2184
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12270"
FT MOD_RES 2223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2231
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2411
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2413
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2422
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 2431 AA; 273990 MW; D21CEA4F9C2C27C5 CRC64;
MTSGGSASRS GHRGVPMTSR GFDGSRRGSL RRAGARETAS EAADGAAPAA GLRASPCSLA
SPSAAAAVAA IPADMAAVLQ QVLERPELNK LPKSTQNKLE KFLAEQQSEI DCLKGRHEKF
KVESEQQYFE IEKRLSQSQE RLVTETRECQ NLRLELEKLN NQVKVLTEKT KELETAQDRN
LGIQSQFTRA KEELEAEKRD LIRTNERLSQ EVEYLTEDVK RLNEKLKESN TTKGELQLKL
DELQASDVAV KYREKRLEQE KELLHNQNSW LNTELKTKTD ELLALGREKG NEILELKCNL
ENKKEEVLRL EEQMNGLKTS NEHLQKHVED LLTKLKEAKE QQASMEEKFH NELNAHIKLS
NLYKSAADDS EAKSNELTRA VDELHKLLKE AGEANKTIQD HLLQVEESKD QMEKEMLEKI
GKLEKELENA NDLLSATKRK GAILSEEELA AMSPTAAAVA KIVKPGMKLT ELYNAYVETQ
DQLLLEKQEN KRINKYLDEI VKEVEAKAPI LKRQREEYER AQKAVASLSA KLEQAMKEIQ
RLQEDTDKAN KHSSVLERDN QRMEIQIKDL SQQIRVLLME LEEARGNHVI RDEEVSSADI
SSSSEVISQH LVSYRNIEEL QQQNQRLLFA LRELGETRER EEQETTSSKI AELQHKLENS
LAELEQLRES RQHQMQLVDS IVRQRDMYRI LLSQTTGMAI PLQASSLDDI SLLSTPKRSS
TSQTVSTPAP EPVIDSTEAI EAKAALKQLQ EIFENYKKEK IDSEKLQNEQ LEKLQEQVTD
LRSQNTKIST QLDFASKRYE MLQDNVEGYR REITSLQERN QKLTATTQKQ EQIINTMTQD
LRGANEKLAV AEVRAENLKK EKEMLKLSEV RLSQQRESLL AEQRGQNLLL TNLQTIQGIL
ERSETETKQR LNSQIEKLEH EISHLKKKLE NEVEQRHTLT RNLDVQLLDT KRQLDTEINL
HLNTKELLKN AQKDIATLKQ HLNNMEAQLA SQSTQRTGKG QPGDRDDVDD LKSQLRQAEE
QVNDLKERLK TSTSNVEQYR AMVTSLEDSL NKEKQVTEEV HKNIEVRLKE SAEFQTQLEK
KLMEVEKEKQ ELQDDKRKAI ESMEQQLSEL KKTLSTVQNE VQEALQRAST ALSNEQQARR
DCQEQAKIAV EAQNKYEREL MLHAADVEAL QAAKEQVSKM TSIRQHLEET TQKAESQLLE
CKASWEERER VLKDEVSKSV SRCEDLEKQN RLLHDQIEKL SDKVVTSMKD AVQAPLNVSL
NEEGKSQEQI LEILRFIRRE KEIAETRFEV AQVESLRYRQ RVELLERELQ ELQDSLNVER
EKVQVTAKTM AQHEELMKKT ETMNVVMETN KMLREEKERL EQNLQQMQAK VRKLELDILP
LQEANAELSE KSGMLQAEKK LLEEDVKRWK ARNQQLINQQ KDPDTEEYRK LLSEKEIHTK
RIQQLNEEVG RLKAEIARSN ASLTNNQNLI QSLREDLSKA RTEKEGIQKD LDAKIIDIQE
KVKTITQVKK IGRRYKTQFE ELKAQQNKAM ETSTQSSGDH QEQHISVQEM QELKDTLSQS
ETKTKSLEGQ VENLQKTLSE KETEARSLQE QTVQLQSELS RLRQDLQDKT TEEQLRQQMN
EKTWKTLALA KSKITHLSGV KDQLTKEIEE LKQRNGALDQ QKDELDVRMT ALKSQYEGRI
SRLERELREH QERHLEQRDE PQEPTNKAPE QQRQITLKTT PASGERGIAS TSDPPTANIK
PTPVVSTPSK VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ
SEGPVEHVPV FGNASGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPTN
QELSPNIVEV VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTM EAGDQVSEDT
VEMPLPKKLK MVTPVGTEEE VMAEESTDGE AETQAYNQDS QDSIGEGVTQ GDYTPMEDSE
ETSQSLQIDL GPLQSDQQTT SSQDGQGKGD DVIVIDSDDE DDDEENDGEH EDYEEDEDDD
DDEEDDTGMG DEGEDSNEGT GSADGNDGYE ADDAEGGDGT DPGTETEESM GGAESHQRAA
DSQNSGEGNT SAAESSFSQE VAREQQPTSA SERQTPQAPQ SPRRPPHPLP PRLTIHAPPQ
ELGPPVQRIQ MTRRQSVGRG LQLTPGIGGM QQHFFDDEDR TVPSTPTLVV PHRTDGFAEA
IHSPQVAGVP RFRFGPPEDM PQTSSSHSDL GQLASQGGLG MYETPLFLAH EEESGGRSVP
TTPLQVAAPV TVFTESTTSD ASEHASQSVP MVTTSTGTLS TTNETAAGDD GDEVFVEAES
EGISSEAGLE IDSQQEEEPV QASDESDLPS TSQDPPSSSS VDTSSSQPKP FRRVRLQTTL
RQGVRGRQFN RQRGISHAMG GRGGINRGNI N
