TPR_HUMAN
ID TPR_HUMAN Reviewed; 2363 AA.
AC P12270; Q15624; Q15655; Q5SWY0; Q99968;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Nucleoprotein TPR;
DE AltName: Full=Megator;
DE AltName: Full=NPC-associated intranuclear protein;
DE AltName: Full=Translocated promoter region protein;
GN Name=TPR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1549355;
RA Mitchell P.J., Cooper C.S.;
RT "Nucleotide sequence analysis of human tpr cDNA clones.";
RL Oncogene 7:383-388(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1437155;
RA Mitchell P.J., Cooper C.S.;
RT "The human tpr gene encodes a protein of 2094 amino acids that has
RT extensive coiled-coil regions and an acidic C-terminal domain.";
RL Oncogene 7:2329-2333(1992).
RN [3]
RP SEQUENCE REVISION, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=7798308; DOI=10.1083/jcb.127.6.1515;
RA Byrd D.A., Sweet D.J., Pante N., Konstantinov K.N., Guan T.,
RA Saphire A.C.S., Mitchell P.J., Cooper C.S., Aebi U., Gerace L.;
RT "Tpr, a large coiled coil protein whose amino terminus is involved in
RT activation of oncogenic kinases, is localized to the cytoplasmic surface of
RT the nuclear pore complex.";
RL J. Cell Biol. 127:1515-1526(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=9024684; DOI=10.1083/jcb.136.3.515;
RA Cordes V.C., Reidenbach S., Rackwitz H.R., Franke W.W.;
RT "Identification of protein p270/Tpr as a constitutive component of the
RT nuclear pore complex-attached intranuclear filaments.";
RL J. Cell Biol. 136:515-529(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-191 (ISOFORM 1/2), AND CHROMOSOMAL
RP REARRANGEMENT WITH NTRK1.
RX PubMed=1532241;
RA Greco A., Pierotti M.A., Bongarzone I., Pagliardini S., Lanzi C.,
RA Della Porta G.;
RT "TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes in
RT human papillary thyroid carcinomas.";
RL Oncogene 7:237-242(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-142 (ISOFORM 1/2).
RX PubMed=3387099;
RA King H.W.S., Tempest P.R., Merrifield K.R., Rance A.J.;
RT "tpr homologues activate met and raf.";
RL Oncogene 2:617-619(1988).
RN [9]
RP PROTEIN SEQUENCE OF 2-11; 502-511; 1192-1201 AND 1421-1427, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma, and Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K.,
RA von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP CHROMOSOMAL REARRANGEMENT WITH MET.
RX PubMed=2300559; DOI=10.1073/pnas.87.2.738;
RA Soman N.R., Wogan G.N., Rhim J.S.;
RT "TPR-MET oncogenic rearrangement: detection by polymerase chain reaction
RT amplification of the transcript and expression in human tumor cell lines.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:738-742(1990).
RN [11]
RP SUBCELLULAR LOCATION, AND NPC-BINDING DOMAIN AND NUCLEAR IMPORT DOMAIN.
RX PubMed=9828100; DOI=10.1006/excr.1998.4246;
RA Cordes V.C., Hase M.E., Muller L.;
RT "Molecular segments of protein Tpr that confer nuclear targeting and
RT association with the nuclear pore complex.";
RL Exp. Cell Res. 245:43-56(1998).
RN [12]
RP FUNCTION, NPC-BINDING DOMAIN AND NUCLEAR IMPORT DOMAIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9864356; DOI=10.1083/jcb.143.7.1801;
RA Bangs P., Burke B., Powers C., Craig R., Purohit A., Doxsey S.;
RT "Functional analysis of Tpr: identification of nuclear pore complex
RT association and nuclear localization domains and a role in mRNA export.";
RL J. Cell Biol. 143:1801-1812(1998).
RN [13]
RP HOMODIMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-458 AND
RP MET-489.
RX PubMed=11514627; DOI=10.1091/mbc.12.8.2433;
RA Hase M.E., Kuznetsov N.V., Cordes V.C.;
RT "Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to
RT the nuclear pore complex but not parallel, in-register homodimerization.";
RL Mol. Biol. Cell 12:2433-2452(2001).
RN [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11952838; DOI=10.1046/j.1365-2443.2002.00525.x;
RA Shibata S., Matsuoka Y., Yoneda Y.;
RT "Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted
RT Tpr-less nuclei in living mammalian cells.";
RL Genes Cells 7:421-434(2002).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [17]
RP ABSENCE OF FUNCTION IN ANCHORING NUCLEOPORINS, INTERACTION WITH NUP153,
RP HOMODIMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-458 AND
RP MET-489.
RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620;
RA Hase M.E., Cordes V.C.;
RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [18]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUCLEAR PORE COMPLEX.
RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165;
RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
RT "Nucleoporins as components of the nuclear pore complex core structure and
RT Tpr as the architectural element of the nuclear basket.";
RL Mol. Biol. Cell 15:4261-4277(2004).
RN [19]
RP FUNCTION IN NUCLEAR PROTEIN EXPORT, AND INTERACTION WITH HTT.
RX PubMed=15654337; DOI=10.1038/ng1503;
RA Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.;
RT "Polyglutamine expansion of huntingtin impairs its nuclear export.";
RL Nat. Genet. 37:198-204(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2073, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [22]
RP FUNCTION IN STRESS-INDUCED NUCLEAR MRNA EXPORT, AND INTERACTION WITH HSF1.
RX PubMed=17897941; DOI=10.1074/jbc.m704054200;
RA Skaggs H.S., Xing H., Wilkerson D.C., Murphy L.A., Hong Y., Mayhew C.N.,
RA Sarge K.D.;
RT "HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA.";
RL J. Biol. Chem. 282:33902-33907(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2050, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [25]
RP INTERACTION WITH MAD2L1 AND MAD1L1, FUNCTION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18981471; DOI=10.1101/gad.1677208;
RA Lee S.H., Sterling H., Burlingame A., McCormick F.;
RT "Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-
RT mediated mitotic spindle checkpoint.";
RL Genes Dev. 22:2926-2931(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [27]
RP FUNCTION IN PROTEIN IMPORT, INTERACTION WITH MAPK1, PHOSPHORYLATION BY
RP MAPK1, AND SUBCELLULAR LOCATION.
RX PubMed=18794356; DOI=10.1128/mcb.00925-08;
RA Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D., Parsons J.T.,
RA Weber M.J., Nandicoori V.K.;
RT "Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and
RT docking domain on the nuclear pore complex protein Tpr cooperatively
RT regulate ERK2-Tpr interaction.";
RL Mol. Cell. Biol. 28:6954-6966(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; SER-2048 AND
RP SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [30]
RP ASSOCIATION WITH XPO1/CRM1 AND IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR, AND
RP INTERACTION WITH KPNB1.
RX PubMed=19835572; DOI=10.1186/1471-2121-10-74;
RA Ben-Efraim I., Frosst P.D., Gerace L.;
RT "Karyopherin binding interactions and nuclear import mechanism of nuclear
RT pore complex protein Tpr.";
RL BMC Cell Biol. 10:74-74(2009).
RN [31]
RP FUNCTION, INTERACTION WITH MAD1L1; MAD2L1 AND TTK, AND SUBCELLULAR
RP 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185; SER-2050 AND SER-2155,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-312; LYS-345; LYS-428;
RP LYS-457; LYS-713; LYS-723; LYS-748 AND LYS-755, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [34]
RP FUNCTION, ORGANIZATION OF PERINUCLEAR CHROMATIN, SUBCELLULAR LOCATION, AND
RP PROTEOLYTIC PROCESSING.
RX PubMed=20407419; DOI=10.1038/emboj.2010.54;
RA Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H.,
RA Thyberg J., Cordes V.C.;
RT "Protein Tpr is required for establishing nuclear pore-associated zones of
RT heterochromatin exclusion.";
RL EMBO J. 29:1659-1673(2010).
RN [35]
RP FUNCTION, INTERACTION WITH DCTN1; DYNEIN; DYNLL1; MAD2L1; NUP153 AND
RP TUBULIN, AND SUBCELLULAR LOCATION.
RX PubMed=20133940; DOI=10.1074/jbc.m110.105890;
RA Nakano H., Funasaka T., Hashizume C., Wong R.W.;
RT "Nucleoporin translocated promoter region (Tpr) associates with dynein
RT complex, preventing chromosome lagging formation during mitosis.";
RL J. Biol. Chem. 285:10841-10849(2010).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; THR-1692 AND
RP SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [38]
RP FUNCTION IN UNSPLICED RNA EXPORT.
RX PubMed=21613532; DOI=10.1261/rna.2616111;
RA Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.;
RT "The Tpr protein regulates export of mRNAs with retained introns that
RT traffic through the Nxf1 pathway.";
RL RNA 17:1344-1356(2011).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-2073, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [41]
RP FUNCTION IN UNSPLICED RNA EXPORT, INTERACTION WITH MAPK1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22253824; DOI=10.1371/journal.pone.0029921;
RA Rajanala K., Nandicoori V.K.;
RT "Localization of nucleoporin Tpr to the nuclear pore complex is essential
RT for Tpr mediated regulation of the export of unspliced RNA.";
RL PLoS ONE 7:E29921-E29921(2012).
RN [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; THR-1692;
RP SER-2034; SER-2037; SER-2048; SER-2050; THR-2137 AND SER-2155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-522; SER-523;
RP SER-632; SER-1893 AND SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [45]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [46]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
RX PubMed=24970816; DOI=10.18632/oncotarget.2095;
RA Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
RA Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
RT "The subcellular distribution and function of MTA1 in cancer
RT differentiation.";
RL Oncotarget 5:5153-5164(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. Modulates the nucleocytoplasmic transport of
CC activated MAPK1/ERK2 and huntingtin/HTT and may serve as a docking site
CC for the XPO1/CRM1-mediated nuclear export complex. According to some
CC authors, plays a limited role in the regulation of nuclear protein
CC export (PubMed:22253824 and PubMed:11952838). 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.
CC {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337,
CC ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356,
CC ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613,
CC ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419,
CC ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824,
CC ECO:0000269|PubMed:9864356}.
CC -!- SUBUNIT: Interacts with IFI204 (via C-terminal region). Interacts with
CC IFI203 (By similarity). Homodimer. Part of the nuclear pore complex
CC (NPC). Associates with the XPO1/CRM1-mediated nuclear export complex,
CC the Importin alpha/Importin beta receptor and the dynein 1 complex.
CC Interacts (via C-terminal domain) with the KPNB1; the interaction
CC occurs in a RanGTP-dependent manner. Interacts (via C-terminal
CC regionand phosphorylated form) with MAPK1/ERK2 (via phosphorylated
CC form); the interaction requires dimerization of MAPK1/ERK2 and
CC increases following EGF stimulation. Interacts with MAPK3/ERK1; the
CC interaction increases following EGF stimulation. Interacts (via coiled
CC coil region) with NUP153; the interaction is direct. Interacts with
CC HSF1; the interaction increases in a stress-responsive manner and
CC stimulates export of stress-induced HSP70 mRNA. Interacts with
CC huntingtin/HTT; the interaction is inhibited by aggregated
CC huntingtin/HTT forms with expanded polyglutamine stretch. Interacts
CC with MAD1L1 (via N-terminal region), MAD2L1, and TTK; the interactions
CC occurs in a microtubule-independent manner. Interacts (via middle
CC region) with DYNLL1. Interacts with DCTN1, dynein, NUP153 and tubulin.
CC Interacts with MTA1. {ECO:0000250, ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15654337,
CC ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356,
CC ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613,
CC ECO:0000269|PubMed:19835572, ECO:0000269|PubMed:20133940,
CC ECO:0000269|PubMed:22253824, ECO:0000269|PubMed:24970816}.
CC -!- INTERACTION:
CC P12270; Q9Y6D9: MAD1L1; NbExp=2; IntAct=EBI-1048528, EBI-742610;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12802065}. Nucleus
CC membrane {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:11952838,
CC ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:9024684,
CC ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11514627,
CC ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100,
CC ECO:0000269|PubMed:9864356}; Nucleoplasmic side
CC {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:9024684,
CC ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}. Nucleus
CC envelope {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:7798308}.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:11514627,
CC ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:18981471,
CC ECO:0000269|PubMed:7798308, ECO:0000269|PubMed:9024684,
CC ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}. Cytoplasm
CC {ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:12802065}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:19273613}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:18981471}. Nucleus membrane
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:7798308}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:7798308}; Cytoplasmic side
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:7798308}. 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 (PubMed:7798308). 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 (PubMed:18981471). Colocalizes with
CC MAD2L1 in the spindle matrix but not at kinetochore (PubMed:19273613).
CC Colocalizes with dynein, dynactin, tubulin at kinetochore during the
CC metaphase-anaphase transition. Colocalizes with DYNLL1 at the mitotic
CC spindle. {ECO:0000250, ECO:0000269|PubMed:18981471,
CC ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:7798308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12270-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12270-2; Sequence=VSP_057406, VSP_057407;
CC -!- TISSUE SPECIFICITY: Expressed in esophagus, ovary, liver, skin, smooth
CC muscles, cerebrum and fetal cerebellum (at protein level). Highest in
CC testis, lung, thymus, spleen and brain, lower levels in heart, liver
CC and kidney. {ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:9024684}.
CC -!- DOMAIN: The N-terminal domain mediates intranuclear attachment to the
CC nuclear pore complex. The C-terminal domain mediates its nuclear
CC import.
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.
CC {ECO:0000269|PubMed:18794356}.
CC -!- PTM: Proteolytically degraded after poliovirus (PV) infection;
CC degradation is restricted to its unfolded C-terminal tail domain
CC whereas its coiled-coil domain containing NCP- and NUP153-binding
CC domains withstand degradation.
CC -!- DISEASE: Note=A chromosomal aberration involving TPR has been found in
CC papillary thyroid carcinomas (PTCs). Intrachromosomal rearrangement
CC that links the 5'-end of the TPR gene to the protein kinase domain of
CC NTRK1 forms the fusion protein TRK-T1. TRK-T1 is a 55 kDa protein
CC reacting with antibodies against the carboxy terminus of the NTRK1
CC protein. {ECO:0000269|PubMed:1532241}.
CC -!- DISEASE: Note=Involved in tumorigenic rearrangements with the MET.
CC {ECO:0000269|PubMed:2300559}.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TPRID282.html";
CC ---------------------------------------------------------------------------
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DR EMBL; X63105; CAA44819.1; -; mRNA.
DR EMBL; X66397; CAA47021.1; -; mRNA.
DR EMBL; U69668; AAB48030.1; -; mRNA.
DR EMBL; AL596220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91205.1; -; Genomic_DNA.
DR EMBL; X62947; CAA44719.1; ALT_TERM; mRNA.
DR EMBL; Y00672; CAA68681.1; -; mRNA.
DR CCDS; CCDS41446.1; -. [P12270-1]
DR PIR; S23741; S23741.
DR RefSeq; NP_003283.2; NM_003292.2. [P12270-1]
DR PDB; 5TO5; X-ray; 2.50 A; A/B=2-142.
DR PDB; 5TO6; X-ray; 2.70 A; A/B/C/D=2-142.
DR PDB; 5TO7; X-ray; 2.60 A; A/B/C/D=2-142.
DR PDB; 5TVB; X-ray; 2.75 A; A/B=2-142.
DR PDBsum; 5TO5; -.
DR PDBsum; 5TO6; -.
DR PDBsum; 5TO7; -.
DR PDBsum; 5TVB; -.
DR AlphaFoldDB; P12270; -.
DR SMR; P12270; -.
DR BioGRID; 113028; 151.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-50405N; -.
DR IntAct; P12270; 61.
DR MINT; P12270; -.
DR STRING; 9606.ENSP00000356448; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyConnect; 2850; 1 O-Linked glycan (1 site).
DR GlyGen; P12270; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; P12270; -.
DR MetOSite; P12270; -.
DR PhosphoSitePlus; P12270; -.
DR SwissPalm; P12270; -.
DR BioMuta; TPR; -.
DR DMDM; 215274208; -.
DR EPD; P12270; -.
DR jPOST; P12270; -.
DR MassIVE; P12270; -.
DR MaxQB; P12270; -.
DR PaxDb; P12270; -.
DR PeptideAtlas; P12270; -.
DR PRIDE; P12270; -.
DR ProteomicsDB; 52840; -. [P12270-1]
DR Antibodypedia; 11198; 224 antibodies from 30 providers.
DR DNASU; 7175; -.
DR Ensembl; ENST00000367478.9; ENSP00000356448.3; ENSG00000047410.14. [P12270-1]
DR Ensembl; ENST00000613151.1; ENSP00000483425.1; ENSG00000047410.14. [P12270-2]
DR GeneID; 7175; -.
DR KEGG; hsa:7175; -.
DR MANE-Select; ENST00000367478.9; ENSP00000356448.3; NM_003292.3; NP_003283.2.
DR UCSC; uc001grv.4; human. [P12270-1]
DR UCSC; uc057nyz.1; human.
DR CTD; 7175; -.
DR DisGeNET; 7175; -.
DR GeneCards; TPR; -.
DR HGNC; HGNC:12017; TPR.
DR HPA; ENSG00000047410; Low tissue specificity.
DR MalaCards; TPR; -.
DR MIM; 189940; gene.
DR neXtProt; NX_P12270; -.
DR OpenTargets; ENSG00000047410; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA36696; -.
DR VEuPathDB; HostDB:ENSG00000047410; -.
DR eggNOG; KOG4674; Eukaryota.
DR GeneTree; ENSGT00730000111014; -.
DR HOGENOM; CLU_001059_0_0_1; -.
DR InParanoid; P12270; -.
DR OMA; KYDRVDP; -.
DR OrthoDB; 20957at2759; -.
DR PhylomeDB; P12270; -.
DR TreeFam; TF350364; -.
DR PathwayCommons; P12270; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P12270; -.
DR SIGNOR; P12270; -.
DR BioGRID-ORCS; 7175; 697 hits in 1086 CRISPR screens.
DR ChiTaRS; TPR; human.
DR GenomeRNAi; 7175; -.
DR Pharos; P12270; Tbio.
DR PRO; PR:P12270; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P12270; protein.
DR Bgee; ENSG00000047410; Expressed in tendon of biceps brachii and 211 other tissues.
DR ExpressionAtlas; P12270; baseline and differential.
DR Genevisible; P12270; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; 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: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:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP: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; IDA:UniProtKB.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; IMP:UniProtKB.
DR GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; 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:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0010965; P:regulation of mitotic sister chromatid separation; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0070849; P:response to epidermal growth factor; IDA:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0006404; P:RNA import into nucleus; IDA:UniProtKB.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosomal rearrangement; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinetochore; Membrane;
KW Methylation; Mitosis; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Proto-oncogene; Reference proteome;
KW Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..2363
FT /note="Nucleoprotein TPR"
FT /id="PRO_0000204920"
FT REGION 3..13
FT /note="Sufficient for interaction with TPR"
FT REGION 14..117
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000269|PubMed:17897941"
FT REGION 437..513
FT /note="Necessary for association to the NPC"
FT REGION 912..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1320
FT /note="Necessary for interaction with HSF1"
FT /evidence="ECO:0000269|PubMed:17897941"
FT REGION 1454..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1619..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..2134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1812..1867
FT /note="Sufficient and essential for mediating its nuclear
FT import"
FT REGION 2227..2363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..370
FT /evidence="ECO:0000255"
FT COILED 423..602
FT /evidence="ECO:0000255"
FT COILED 661..1173
FT /evidence="ECO:0000255"
FT COILED 1215..1630
FT /evidence="ECO:0000255"
FT COMPBIAS 912..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2000..2014
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2090
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2227..2260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2296..2325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 191
FT /note="Breakpoint for translocation to form TRK-T1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 312
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 428
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 477
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 723
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 748
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 755
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1690
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 1692
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2037
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 2073
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2106
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2163
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2343
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2345
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT MOD_RES 2354
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:F6ZDS4"
FT VAR_SEQ 726
FT /note="E -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1549355"
FT /id="VSP_057406"
FT VAR_SEQ 727..2363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1549355"
FT /id="VSP_057407"
FT VARIANT 960
FT /note="S -> N (in dbSNP:rs3753565)"
FT /id="VAR_020429"
FT VARIANT 1428
FT /note="V -> G (in dbSNP:rs35550453)"
FT /id="VAR_047289"
FT VARIANT 1707
FT /note="T -> A (in dbSNP:rs35766045)"
FT /id="VAR_047290"
FT MUTAGEN 458
FT /note="L->P: Diminishes association to NPC but not
FT homodimerization. Inhibits association to NPC, interaction
FT with NUP153 and nuclear membrane localization but not
FT homodimerization; when associated with P-489."
FT /evidence="ECO:0000269|PubMed:11514627,
FT ECO:0000269|PubMed:12802065"
FT MUTAGEN 489
FT /note="M->P: Diminishes association to NPC but not
FT homodimerization. Inhibits association to NPC, interaction
FT with NUP153 and nuclear membrane localization but not
FT homodimerization; when associated with P-458."
FT /evidence="ECO:0000269|PubMed:11514627,
FT ECO:0000269|PubMed:12802065"
FT CONFLICT 32
FT /note="Q -> R (in Ref. 5; CAA44719 and 6; CAA68681)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="V -> I (in Ref. 4; AAB48030)"
FT /evidence="ECO:0000305"
FT CONFLICT 906
FT /note="Q -> R (in Ref. 4; AAB48030)"
FT /evidence="ECO:0000305"
FT CONFLICT 1239
FT /note="Q -> E (in Ref. 3; CAA47021)"
FT /evidence="ECO:0000305"
FT CONFLICT 1952..1965
FT /note="Missing (in Ref. 3; CAA47021)"
FT /evidence="ECO:0000305"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:5TO5"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:5TO5"
FT HELIX 19..140
FT /evidence="ECO:0007829|PDB:5TO5"
SQ SEQUENCE 2363 AA; 267293 MW; 01E669CBDC496772 CRC64;
MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES EQQYFEIEKR
LSHSQERLVN ETRECQSLRL ELEKLNNQLK ALTEKNKELE IAQDRNIAIQ SQFTRTKEEL
EAEKRDLIRT NERLSQELEY LTEDVKRLNE KLKESNTTKG ELQLKLDELQ ASDVSVKYRE
KRLEQEKELL HSQNTWLNTE LKTKTDELLA LGREKGNEIL ELKCNLENKK EEVSRLEEQM
NGLKTSNEHL QKHVEDLLTK LKEAKEQQAS MEEKFHNELN AHIKLSNLYK SAADDSEAKS
NELTRAVEEL HKLLKEAGEA NKAIQDHLLE VEQSKDQMEK EMLEKIGRLE KELENANDLL
SATKRKGAIL SEEELAAMSP TAAAVAKIVK PGMKLTELYN AYVETQDQLL LEKLENKRIN
KYLDEIVKEV EAKAPILKRQ REEYERAQKA VASLSVKLEQ AMKEIQRLQE DTDKANKQSS
VLERDNRRME IQVKDLSQQI RVLLMELEEA RGNHVIRDEE VSSADISSSS EVISQHLVSY
RNIEELQQQN QRLLVALREL GETREREEQE TTSSKITELQ LKLESALTEL EQLRKSRQHQ
MQLVDSIVRQ RDMYRILLSQ TTGVAIPLHA SSLDDVSLAS TPKRPSTSQT VSTPAPVPVI
ESTEAIEAKA ALKQLQEIFE NYKKEKAENE KIQNEQLEKL QEQVTDLRSQ NTKISTQLDF
ASKRYEMLQD NVEGYRREIT SLHERNQKLT ATTQKQEQII NTMTQDLRGA NEKLAVAEVR
AENLKKEKEM LKLSEVRLSQ QRESLLAEQR GQNLLLTNLQ TIQGILERSE TETKQRLSSQ
IEKLEHEISH LKKKLENEVE QRHTLTRNLD VQLLDTKRQL DTETNLHLNT KELLKNAQKE
IATLKQHLSN MEVQVASQSS QRTGKGQPSN KEDVDDLVSQ LRQTEEQVND LKERLKTSTS
NVEQYQAMVT SLEESLNKEK QVTEEVRKNI EVRLKESAEF QTQLEKKLME VEKEKQELQD
DKRRAIESME QQLSELKKTL SSVQNEVQEA LQRASTALSN EQQARRDCQE QAKIAVEAQN
KYERELMLHA ADVEALQAAK EQVSKMASVR QHLEETTQKA ESQLLECKAS WEERERMLKD
EVSKCVCRCE DLEKQNRLLH DQIEKLSDKV VASVKEGVQG PLNVSLSEEG KSQEQILEIL
RFIRREKEIA ETRFEVAQVE SLRYRQRVEL LERELQELQD SLNAEREKVQ VTAKTMAQHE
ELMKKTETMN VVMETNKMLR EEKERLEQDL QQMQAKVRKL ELDILPLQEA NAELSEKSGM
LQAEKKLLEE DVKRWKARNQ HLVSQQKDPD TEEYRKLLSE KEVHTKRIQQ LTEEIGRLKA
EIARSNASLT NNQNLIQSLK EDLNKVRTEK ETIQKDLDAK IIDIQEKVKT ITQVKKIGRR
YKTQYEELKA QQDKVMETSA QSSGDHQEQH VSVQEMQELK ETLNQAETKS KSLESQVENL
QKTLSEKETE ARNLQEQTVQ LQSELSRLRQ DLQDRTTQEE QLRQQITEKE EKTRKAIVAA
KSKIAHLAGV KDQLTKENEE LKQRNGALDQ QKDELDVRIT ALKSQYEGRI SRLERELREH
QERHLEQRDE PQEPSNKVPE QQRQITLKTT PASGERGIAS TSDPPTANIK PTPVVSTPSK
VTAAAMAGNK STPRASIRPM VTPATVTNPT TTPTATVMPT TQVESQEAMQ SEGPVEHVPV
FGSTSGSVRS TSPNVQPSIS QPILTVQQQT QATAFVQPTQ QSHPQIEPAN QELSSNIVEV
VQSSPVERPS TSTAVFGTVS ATPSSSLPKR TREEEEDSTI EASDQVSDDT VEMPLPKKLK
SVTPVGTEEE VMAEESTDGE VETQVYNQDS QDSIGEGVTQ GDYTPMEDSE ETSQSLQIDL
GPLQSDQQTT TSSQDGQGKG DDVIVIDSDD EEEDDDENDG EHEDYEEDEE DDDDDEDDTG
MGDEGEDSNE GTGSADGNDG YEADDAEGGD GTDPGTETEE SMGGGEGNHR AADSQNSGEG
NTGAAESSFS QEVSREQQPS SASERQAPRA PQSPRRPPHP LPPRLTIHAP PQELGPPVQR
IQMTRRQSVG RGLQLTPGIG GMQQHFFDDE DRTVPSTPTL VVPHRTDGFA EAIHSPQVAG
VPRFRFGPPE DMPQTSSSHS DLGQLASQGG LGMYETPLFL AHEEESGGRS VPTTPLQVAA
PVTVFTESTT SDASEHASQS VPMVTTSTGT LSTTNETATG DDGDEVFVEA ESEGISSEAG
LEIDSQQEEE PVQASDESDL PSTSQDPPSS SSVDTSSSQP KPFRRVRLQT TLRQGVRGRQ
FNRQRGVSHA MGGRGGINRG NIN
