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Nucleoprotein TPR (Megator) (NPC-associated intranuclear protein) (Translocated promoter region protein)

 TPR_HUMAN               Reviewed;        2363 AA.
P12270; Q15624; Q15655; Q5SWY0; Q99968;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
20-JUN-2018, entry version 188.
RecName: Full=Nucleoprotein TPR;
AltName: Full=Megator;
AltName: Full=NPC-associated intranuclear protein;
AltName: Full=Translocated promoter region protein;
Name=TPR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1549355;
Mitchell P.J., Cooper C.S.;
"Nucleotide sequence analysis of human tpr cDNA clones.";
Oncogene 7:383-388(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1437155;
Mitchell P.J., Cooper C.S.;
"The human tpr gene encodes a protein of 2094 amino acids that has
extensive coiled-coil regions and an acidic C-terminal domain.";
Oncogene 7:2329-2333(1992).
[3]
SEQUENCE REVISION, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
PubMed=7798308; DOI=10.1083/jcb.127.6.1515;
Byrd D.A., Sweet D.J., Pante N., Konstantinov K.N., Guan T.,
Saphire A.C.S., Mitchell P.J., Cooper C.S., Aebi U., Gerace L.;
"Tpr, a large coiled coil protein whose amino terminus is involved in
activation of oncogenic kinases, is localized to the cytoplasmic
surface of the nuclear pore complex.";
J. Cell Biol. 127:1515-1526(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Embryonic brain;
PubMed=9024684; DOI=10.1083/jcb.136.3.515;
Cordes V.C., Reidenbach S., Rackwitz H.R., Franke W.W.;
"Identification of protein p270/Tpr as a constitutive component of the
nuclear pore complex-attached intranuclear filaments.";
J. Cell Biol. 136:515-529(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-191 (ISOFORM 1/2), AND CHROMOSOMAL
REARRANGEMENT WITH NTRK1.
PubMed=1532241;
Greco A., Pierotti M.A., Bongarzone I., Pagliardini S., Lanzi C.,
Della Porta G.;
"TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK genes
in human papillary thyroid carcinomas.";
Oncogene 7:237-242(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-142 (ISOFORM 1/2).
PubMed=3387099;
King H.W.S., Tempest P.R., Merrifield K.R., Rance A.J.;
"tpr homologues activate met and raf.";
Oncogene 2:617-619(1988).
[9]
PROTEIN SEQUENCE OF 2-11; 502-511; 1192-1201 AND 1421-1427, CLEAVAGE
OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Hepatoma, and Osteosarcoma;
Bienvenut W.V., Glen H., Brunton V.G., Frame M.C., Boldt K.,
von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[10]
CHROMOSOMAL REARRANGEMENT WITH MET.
PubMed=2300559; DOI=10.1073/pnas.87.2.738;
Soman N.R., Wogan G.N., Rhim J.S.;
"TPR-MET oncogenic rearrangement: detection by polymerase chain
reaction amplification of the transcript and expression in human tumor
cell lines.";
Proc. Natl. Acad. Sci. U.S.A. 87:738-742(1990).
[11]
SUBCELLULAR LOCATION, AND NPC-BINDING DOMAIN AND NUCLEAR IMPORT
DOMAIN.
PubMed=9828100; DOI=10.1006/excr.1998.4246;
Cordes V.C., Hase M.E., Muller L.;
"Molecular segments of protein Tpr that confer nuclear targeting and
association with the nuclear pore complex.";
Exp. Cell Res. 245:43-56(1998).
[12]
FUNCTION, NPC-BINDING DOMAIN AND NUCLEAR IMPORT DOMAIN, AND
SUBCELLULAR LOCATION.
PubMed=9864356; DOI=10.1083/jcb.143.7.1801;
Bangs P., Burke B., Powers C., Craig R., Purohit A., Doxsey S.;
"Functional analysis of Tpr: identification of nuclear pore complex
association and nuclear localization domains and a role in mRNA
export.";
J. Cell Biol. 143:1801-1812(1998).
[13]
HOMODIMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-458 AND
MET-489.
PubMed=11514627; DOI=10.1091/mbc.12.8.2433;
Hase M.E., Kuznetsov N.V., Cordes V.C.;
"Amino acid substitutions of coiled-coil protein Tpr abrogate
anchorage to the nuclear pore complex but not parallel, in-register
homodimerization.";
Mol. Biol. Cell 12:2433-2452(2001).
[14]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12424524; DOI=10.1007/s00412-002-0208-2;
Kuznetsov N.V., Sandblad L., Hase M.E., Hunziker A., Hergt M.,
Cordes V.C.;
"The evolutionarily conserved single-copy gene for murine Tpr encodes
one prevalent isoform in somatic cells and lacks paralogs in higher
eukaryotes.";
Chromosoma 111:236-255(2002).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11952838; DOI=10.1046/j.1365-2443.2002.00525.x;
Shibata S., Matsuoka Y., Yoneda Y.;
"Nucleocytoplasmic transport of proteins and poly(A)+ RNA in
reconstituted Tpr-less nuclei in living mammalian cells.";
Genes Cells 7:421-434(2002).
[16]
SUBCELLULAR LOCATION.
PubMed=11839768; DOI=10.1083/jcb.200106046;
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
"Tpr is localized within the nuclear basket of the pore complex and
has a role in nuclear protein export.";
J. Cell Biol. 156:617-630(2002).
[17]
ABSENCE OF FUNCTION IN ANCHORING NUCLEOPORINS, INTERACTION WITH
NUP153, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LEU-458 AND MET-489.
PubMed=12802065; DOI=10.1091/mbc.E02-09-0620;
Hase M.E., Cordes V.C.;
"Direct interaction with nup153 mediates binding of Tpr to the
periphery of the nuclear pore complex.";
Mol. Biol. Cell 14:1923-1940(2003).
[18]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE NUCLEAR PORE COMPLEX.
PubMed=15229283; DOI=10.1091/mbc.E04-03-0165;
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
"Nucleoporins as components of the nuclear pore complex core structure
and Tpr as the architectural element of the nuclear basket.";
Mol. Biol. Cell 15:4261-4277(2004).
[19]
FUNCTION IN NUCLEAR PROTEIN EXPORT, AND INTERACTION WITH HTT.
PubMed=15654337; DOI=10.1038/ng1503;
Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H.,
Li X.J.;
"Polyglutamine expansion of huntingtin impairs its nuclear export.";
Nat. Genet. 37:198-204(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2073, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
FUNCTION IN STRESS-INDUCED NUCLEAR MRNA EXPORT, AND INTERACTION WITH
HSF1.
PubMed=17897941; DOI=10.1074/jbc.M704054200;
Skaggs H.S., Xing H., Wilkerson D.C., Murphy L.A., Hong Y.,
Mayhew C.N., Sarge K.D.;
"HSF1-TPR interaction facilitates export of stress-induced HSP70
mRNA.";
J. Biol. Chem. 282:33902-33907(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2050, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[25]
INTERACTION WITH MAD2L1 AND MAD1L1, FUNCTION, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=18981471; DOI=10.1101/gad.1677208;
Lee S.H., Sterling H., Burlingame A., McCormick F.;
"Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-
Mad2-mediated mitotic spindle checkpoint.";
Genes Dev. 22:2926-2931(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2155, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[27]
FUNCTION IN PROTEIN IMPORT, INTERACTION WITH MAPK1, PHOSPHORYLATION BY
MAPK1, AND SUBCELLULAR LOCATION.
PubMed=18794356; DOI=10.1128/MCB.00925-08;
Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D.,
Parsons J.T., Weber M.J., Nandicoori V.K.;
"Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites
and docking domain on the nuclear pore complex protein Tpr
cooperatively regulate ERK2-Tpr interaction.";
Mol. Cell. Biol. 28:6954-6966(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; SER-2048
AND SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
ASSOCIATION WITH XPO1/CRM1 AND IMPORTIN ALPHA/IMPORTIN BETA RECEPTOR,
AND INTERACTION WITH KPNB1.
PubMed=19835572; DOI=10.1186/1471-2121-10-74;
Ben-Efraim I., Frosst P.D., Gerace L.;
"Karyopherin binding interactions and nuclear import mechanism of
nuclear pore complex protein Tpr.";
BMC Cell Biol. 10:74-74(2009).
[31]
FUNCTION, INTERACTION WITH MAD1L1; MAD2L1 AND TTK, AND SUBCELLULAR
LOCATION.
PubMed=19273613; DOI=10.1083/jcb.200811012;
Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E.,
Tavares A., Johansen J., Johansen K.M., Maiato H.;
"Spatiotemporal control of mitosis by the conserved spindle matrix
protein Megator.";
J. Cell Biol. 184:647-657(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185; SER-2050 AND
SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-312; LYS-345;
LYS-428; LYS-457; LYS-713; LYS-723; LYS-748 AND LYS-755, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[34]
FUNCTION, ORGANIZATION OF PERINUCLEAR CHROMATIN, SUBCELLULAR LOCATION,
AND PROTEOLYTIC PROCESSING.
PubMed=20407419; DOI=10.1038/emboj.2010.54;
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H.,
Thyberg J., Cordes V.C.;
"Protein Tpr is required for establishing nuclear pore-associated
zones of heterochromatin exclusion.";
EMBO J. 29:1659-1673(2010).
[35]
FUNCTION, INTERACTION WITH DCTN1; DYNEIN; DYNLL1; MAD2L1; NUP153 AND
TUBULIN, AND SUBCELLULAR LOCATION.
PubMed=20133940; DOI=10.1074/jbc.M110.105890;
Nakano H., Funasaka T., Hashizume C., Wong R.W.;
"Nucleoporin translocated promoter region (Tpr) associates with dynein
complex, preventing chromosome lagging formation during mitosis.";
J. Biol. Chem. 285:10841-10849(2010).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; THR-1692
AND SER-2155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
FUNCTION IN UNSPLICED RNA EXPORT.
PubMed=21613532; DOI=10.1261/rna.2616111;
Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.;
"The Tpr protein regulates export of mRNAs with retained introns that
traffic through the Nxf1 pathway.";
RNA 17:1344-1356(2011).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-2073, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[40]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[41]
FUNCTION IN UNSPLICED RNA EXPORT, INTERACTION WITH MAPK1, AND
SUBCELLULAR LOCATION.
PubMed=22253824; DOI=10.1371/journal.pone.0029921;
Rajanala K., Nandicoori V.K.;
"Localization of nucleoporin Tpr to the nuclear pore complex is
essential for Tpr mediated regulation of the export of unspliced
RNA.";
PLoS ONE 7:E29921-E29921(2012).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-1185; THR-1692;
SER-2034; SER-2037; SER-2048; SER-2050; THR-2137 AND SER-2155, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-522; SER-523;
SER-632; SER-1893 AND SER-2155, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[45]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2111, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[46]
SUBCELLULAR LOCATION, AND INTERACTION WITH MTA1.
PubMed=24970816;
Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
"The subcellular distribution and function of MTA1 in cancer
differentiation.";
Oncotarget 5:5153-5164(2014).
-!- 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. 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. According to some authors, plays a limited role in the
regulation of nuclear protein export (PubMed:22253824 and
PubMed:11952838). Plays also 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.
{ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:15654337,
ECO:0000269|PubMed:17897941, ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613,
ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:20407419,
ECO:0000269|PubMed:21613532, ECO:0000269|PubMed:22253824,
ECO:0000269|PubMed:9864356}.
-!- SUBUNIT: Interacts with IFI204 (via C-terminal region). Interacts
with IFI203 (By similarity). Homodimer. Part of the nuclear pore
complex (NPC). Associates with the XPO1/CRM1-mediated nuclear
export complex, the Importin alpha/Importin beta receptor and the
dynein 1 complex. Interacts (via C-terminal domain) with the
KPNB1; the interaction occurs in a RanGTP-dependent manner.
Interacts (via C-terminal regionand phosphorylated form) with
MAPK1/ERK2 (via phosphorylated form); the interaction requires
dimerization of MAPK1/ERK2 and increases following EGF
stimulation. Interacts with MAPK3/ERK1; the interaction increases
following EGF stimulation. Interacts (via coiled coil region) with
NUP153; the interaction is direct. Interacts with HSF1; the
interaction increases in a stress-responsive manner and stimulates
export of stress-induced HSP70 mRNA. Interacts with
huntingtin/HTT; the interaction is inhibited by aggregated
huntingtin/HTT forms with expanded polyglutamine stretch.
Interacts with MAD1L1 (via N-terminal region), MAD2L1, and TTK;
the interactions occurs in a microtubule-independent manner.
Interacts (via middle region) with DYNLL1. Interacts with DCTN1,
dynein, NUP153 and tubulin. Interacts with MTA1. {ECO:0000250,
ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:17897941,
ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:18981471,
ECO:0000269|PubMed:19273613, ECO:0000269|PubMed:19835572,
ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:22253824,
ECO:0000269|PubMed:24970816}.
-!- INTERACTION:
Q9Y6D9:MAD1L1; NbExp=2; IntAct=EBI-1048528, EBI-742610;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12802065}.
Nucleus membrane {ECO:0000269|PubMed:11514627,
ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100,
ECO:0000269|PubMed:9864356}; Peripheral membrane protein
{ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:9024684,
ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356};
Nucleoplasmic side {ECO:0000269|PubMed:11514627,
ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100,
ECO:0000269|PubMed:9864356}. Nucleus envelope
{ECO:0000269|PubMed:12424524, ECO:0000269|PubMed:7798308}.
Nucleus, nuclear pore complex {ECO:0000269|PubMed:11514627,
ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:18981471,
ECO:0000269|PubMed:7798308, ECO:0000269|PubMed:9024684,
ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}. Cytoplasm
{ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:12802065}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19273613}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18981471}.
Nucleus membrane {ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308};
Peripheral membrane protein {ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308};
Cytoplasmic side {ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:7798308}.
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 (PubMed:7798308). 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 (PubMed:18981471).
Colocalizes with MAD2L1 in the spindle matrix but not at
kinetochore (PubMed:19273613). Colocalizes with dynein, dynactin,
tubulin at kinetochore during the metaphase-anaphase transition.
Colocalizes with DYNLL1 at the mitotic spindle. {ECO:0000250,
ECO:0000269|PubMed:18981471, ECO:0000269|PubMed:19273613,
ECO:0000269|PubMed:7798308}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P12270-1; Sequence=Displayed;
Name=2;
IsoId=P12270-2; Sequence=VSP_057406, VSP_057407;
-!- TISSUE SPECIFICITY: Expressed in esophagus, ovary, liver, skin,
smooth muscles, cerebrum and fetal cerebellum (at protein level).
Highest in testis, lung, thymus, spleen and brain, lower levels in
heart, liver and kidney. {ECO:0000269|PubMed:12424524,
ECO:0000269|PubMed:9024684}.
-!- DOMAIN: The N-terminal domain mediates intranuclear attachment to
the nuclear pore complex. The C-terminal domain mediates its
nuclear import.
-!- PTM: Phosphorylated. Phosphorylation occurs on serine and
threonine residues (comprised in the C-terminal region) by
MAPK1/ERK2 and stabilizes the interaction between these two
proteins. {ECO:0000269|PubMed:18794356}.
-!- PTM: Proteolytically degraded after poliovirus (PV) infection;
degradation is restricted to its unfolded C-terminal tail domain
whereas its coiled-coil domain containing NCP- and NUP153-binding
domains withstand degradation.
-!- DISEASE: Note=A chromosomal aberration involving TPR has been
found in papillary thyroid carcinomas (PTCs). Intrachromosomal
rearrangement that links the 5'-end of the TPR gene to the protein
kinase domain of NTRK1 forms the fusion protein TRK-T1. TRK-T1 is
a 55 kDa protein reacting with antibodies against the carboxy
terminus of the NTRK1 protein. {ECO:0000269|PubMed:1532241}.
-!- DISEASE: Note=Involved in tumorigenic rearrangements with the MET.
{ECO:0000269|PubMed:2300559}.
-!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TPRID282.html";
-----------------------------------------------------------------------
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EMBL; X63105; CAA44819.1; -; mRNA.
EMBL; X66397; CAA47021.1; -; mRNA.
EMBL; U69668; AAB48030.1; -; mRNA.
EMBL; AL596220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91205.1; -; Genomic_DNA.
EMBL; X62947; CAA44719.1; ALT_TERM; mRNA.
EMBL; Y00672; CAA68681.1; -; mRNA.
CCDS; CCDS41446.1; -. [P12270-1]
PIR; S23741; S23741.
RefSeq; NP_003283.2; NM_003292.2. [P12270-1]
UniGene; Hs.279640; -.
PDB; 5TO5; X-ray; 2.50 A; A/B=2-142.
PDB; 5TO6; X-ray; 2.70 A; A/B/C/D=2-142.
PDB; 5TO7; X-ray; 2.60 A; A/B/C/D=2-142.
PDB; 5TVB; X-ray; 2.75 A; A/B=2-142.
PDBsum; 5TO5; -.
PDBsum; 5TO6; -.
PDBsum; 5TO7; -.
PDBsum; 5TVB; -.
ProteinModelPortal; P12270; -.
SMR; P12270; -.
BioGrid; 113028; 92.
CORUM; P12270; -.
DIP; DIP-50405N; -.
IntAct; P12270; 35.
MINT; P12270; -.
STRING; 9606.ENSP00000356448; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P12270; -.
PhosphoSitePlus; P12270; -.
BioMuta; TPR; -.
DMDM; 215274208; -.
EPD; P12270; -.
MaxQB; P12270; -.
PaxDb; P12270; -.
PeptideAtlas; P12270; -.
PRIDE; P12270; -.
ProteomicsDB; 52840; -.
Ensembl; ENST00000367478; ENSP00000356448; ENSG00000047410. [P12270-1]
Ensembl; ENST00000613151; ENSP00000483425; ENSG00000047410. [P12270-2]
GeneID; 7175; -.
KEGG; hsa:7175; -.
UCSC; uc001grv.4; human. [P12270-1]
UCSC; uc057nyz.1; human.
CTD; 7175; -.
DisGeNET; 7175; -.
EuPathDB; HostDB:ENSG00000047410.13; -.
GeneCards; TPR; -.
HGNC; HGNC:12017; TPR.
HPA; HPA019661; -.
HPA; HPA019663; -.
HPA; HPA024336; -.
MalaCards; TPR; -.
MIM; 189940; gene.
neXtProt; NX_P12270; -.
OpenTargets; ENSG00000047410; -.
Orphanet; 146; Papillary or follicular thyroid carcinoma.
PharmGKB; PA36696; -.
eggNOG; KOG4674; Eukaryota.
eggNOG; ENOG410XSA1; LUCA.
GeneTree; ENSGT00730000111014; -.
HOGENOM; HOG000139431; -.
HOVERGEN; HBG009158; -.
InParanoid; P12270; -.
KO; K09291; -.
OMA; SENTRFR; -.
OrthoDB; EOG091G006U; -.
PhylomeDB; P12270; -.
TreeFam; TF350364; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
SIGNOR; P12270; -.
ChiTaRS; TPR; human.
GenomeRNAi; 7175; -.
PMAP-CutDB; P12270; -.
PRO; PR:P12270; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000047410; -.
CleanEx; HS_TPR; -.
ExpressionAtlas; P12270; baseline and differential.
Genevisible; P12270; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IDA:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IDA:UniProtKB.
GO; GO:0046832; P:negative regulation of RNA export from nucleus; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; IMP:UniProtKB.
GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB.
GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:UniProtKB.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; TAS:ProtInc.
GO; GO:0010965; P:regulation of mitotic sister chromatid separation; IMP:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0070849; P:response to epidermal growth factor; IDA:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; IMP:UniProtKB.
GO; GO:0006404; P:RNA import into nucleus; IDA:UniProtKB.
GO; GO:0016032; P:viral process; TAS:Reactome.
InterPro; IPR012929; TPR/MLP1.
Pfam; PF07926; TPR_MLP1_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Centromere; Chromosomal rearrangement; Chromosome;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Kinetochore; Membrane; Methylation;
Mitosis; mRNA transport; Nuclear pore complex; Nucleus;
Phosphoprotein; Polymorphism; Protein transport; Proto-oncogene;
Reference proteome; Translocation; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
CHAIN 2 2363 Nucleoprotein TPR.
/FTId=PRO_0000204920.
REGION 3 13 Sufficient for interaction with TPR.
REGION 14 117 Necessary for interaction with HSF1.
{ECO:0000269|PubMed:17897941}.
REGION 437 513 Necessary for association to the NPC.
REGION 1218 1320 Necessary for interaction with HSF1.
{ECO:0000269|PubMed:17897941}.
REGION 1812 1867 Sufficient and essential for mediating
its nuclear import.
COILED 29 370 {ECO:0000255}.
COILED 423 602 {ECO:0000255}.
COILED 661 1173 {ECO:0000255}.
COILED 1215 1630 {ECO:0000255}.
COMPBIAS 527 530 Poly-Ser.
COMPBIAS 1833 1836 Poly-Glu.
COMPBIAS 1971 1978 Poly-Asp.
COMPBIAS 2309 2312 Poly-Ser.
SITE 191 191 Breakpoint for translocation to form TRK-
T1.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 312 312 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 345 345 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 379 379 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 428 428 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 457 457 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 477 477 N6-acetyllysine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 713 713 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 723 723 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 748 748 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 755 755 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1185 1185 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1690 1690 N6-acetyllysine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 1692 1692 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1893 1893 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2034 2034 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2037 2037 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2048 2048 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2050 2050 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2073 2073 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692}.
MOD_RES 2106 2106 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 2111 2111 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2116 2116 Phosphothreonine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 2137 2137 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2155 2155 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2163 2163 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 2343 2343 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 2345 2345 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:F6ZDS4}.
MOD_RES 2354 2354 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:F6ZDS4}.
VAR_SEQ 726 726 E -> L (in isoform 2).
{ECO:0000303|PubMed:1549355}.
/FTId=VSP_057406.
VAR_SEQ 727 2363 Missing (in isoform 2).
{ECO:0000303|PubMed:1549355}.
/FTId=VSP_057407.
VARIANT 960 960 S -> N (in dbSNP:rs3753565).
/FTId=VAR_020429.
VARIANT 1428 1428 V -> G (in dbSNP:rs35550453).
/FTId=VAR_047289.
VARIANT 1707 1707 T -> A (in dbSNP:rs35766045).
/FTId=VAR_047290.
MUTAGEN 458 458 L->P: Diminishes association to NPC but
not homodimerization. Inhibits
association to NPC, interaction with
NUP153 and nuclear membrane localization
but not homodimerization; when associated
with P-489. {ECO:0000269|PubMed:11514627,
ECO:0000269|PubMed:12802065}.
MUTAGEN 489 489 M->P: Diminishes association to NPC but
not homodimerization. Inhibits
association to NPC, interaction with
NUP153 and nuclear membrane localization
but not homodimerization; when associated
with P-458. {ECO:0000269|PubMed:11514627,
ECO:0000269|PubMed:12802065}.
CONFLICT 32 32 Q -> R (in Ref. 5; CAA44719 and 6;
CAA68681). {ECO:0000305}.
CONFLICT 779 779 V -> I (in Ref. 4; AAB48030).
{ECO:0000305}.
CONFLICT 906 906 Q -> R (in Ref. 4; AAB48030).
{ECO:0000305}.
CONFLICT 1239 1239 Q -> E (in Ref. 3; CAA47021).
{ECO:0000305}.
CONFLICT 1952 1965 Missing (in Ref. 3; CAA47021).
{ECO:0000305}.
HELIX 5 8 {ECO:0000244|PDB:5TO5}.
HELIX 11 14 {ECO:0000244|PDB:5TO5}.
HELIX 19 140 {ECO:0000244|PDB:5TO5}.
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


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