TR150_HUMAN
ID TR150_HUMAN Reviewed; 955 AA.
AC Q9Y2W1; D3DPS5; Q5VTK6;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Thyroid hormone receptor-associated protein 3;
DE AltName: Full=BCLAF1 and THRAP3 family member 2 {ECO:0000312|HGNC:HGNC:22964};
DE AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component;
DE Short=Trap150;
GN Name=THRAP3 {ECO:0000312|HGNC:HGNC:22964};
GN Synonyms=BCLAF2 {ECO:0000312|HGNC:HGNC:22964}, TRAP150;
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], PROTEIN SEQUENCE OF 490-500, TISSUE
RP SPECIFICITY, IDENTIFICATION IN TRAP COMPLEX, AND VARIANT VAL-201.
RC TISSUE=Cervix carcinoma;
RX PubMed=10198638; DOI=10.1016/s1097-2765(00)80463-3;
RA Ito M., Yuan C.-X., Malik S., Gu W., Fondell J.D., Yamamura S., Fu Z.-Y.,
RA Zhang X., Qin J., Roeder R.G.;
RT "Identity between TRAP and SMCC complexes indicates novel pathways for the
RT function of nuclear receptors and diverse mammalian activators.";
RL Mol. Cell 3:361-370(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-201.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-201.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 186-202; 216-245; 253-261; 314-333; 376-387; 443-451;
RP 468-481; 486-498; 573-591; 609-653; 678-687; 710-718; 792-802; 864-876;
RP 879-893 AND 927-944, METHYLATION AT ARG-17, PHOSPHORYLATION AT SER-243;
RP SER-320 AND SER-682, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S.,
RA von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; SER-248;
RP SER-253; SER-315; SER-320; SER-575; SER-672 AND SER-928, AND IDENTIFICATION
RP BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, 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 [10]
RP IDENTIFICATION BY 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 [11]
RP SUBUNIT.
RX PubMed=17095540; DOI=10.1261/rna.336807;
RA Merz C., Urlaub H., Will C.L., Luhrmann R.;
RT "Protein composition of human mRNPs spliced in vitro and differential
RT requirements for mRNP protein recruitment.";
RL RNA 13:116-128(2007).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION IN THE SNARP COMPLEX.
RX PubMed=18794151; DOI=10.1158/0008-5472.can-08-1217;
RA Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.;
RT "Regulation of cyclin D1 RNA stability by SNIP1.";
RL Cancer Res. 68:7621-7628(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248 AND SER-253, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-237; SER-240;
RP SER-243; SER-248; SER-253; SER-379; SER-406; SER-408; SER-575; SER-682;
RP THR-874; SER-928 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-874; SER-928 AND SER-939, AND
RP 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-455; LYS-519 AND
RP LYS-811, AND IDENTIFICATION BY MASS 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 [22]
RP FUNCTION, AND INTERACTION WITH SFPQ.
RX PubMed=20932480; DOI=10.1016/j.molcel.2010.09.013;
RA Heyd F., Lynch K.W.;
RT "Phosphorylation-dependent regulation of PSF by GSK3 controls CD45
RT alternative splicing.";
RL Mol. Cell 40:126-137(2010).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NXF1.
RX PubMed=20123736; DOI=10.1093/nar/gkq017;
RA Lee K.M., Hsu I.W., Tarn W.Y.;
RT "TRAP150 activates pre-mRNA splicing and promotes nuclear mRNA
RT degradation.";
RL Nucleic Acids Res. 38:3340-3350(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-243; SER-248;
RP SER-253; SER-257; SER-315; SER-320; SER-379; SER-408; SER-575; SER-622;
RP SER-682; SER-698; SER-928 AND SER-939, AND IDENTIFICATION BY MASS
RP 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 [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-253; SER-315;
RP SER-320; SER-339; SER-379; SER-406; SER-408; SER-535; SER-575; SER-622;
RP SER-682; SER-698; SER-928 AND SER-939, AND IDENTIFICATION BY MASS
RP 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 [27]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-406 AND SER-408.
RX PubMed=22424773; DOI=10.1016/j.molcel.2012.01.026;
RA Beli P., Lukashchuk N., Wagner S.A., Weinert B.T., Olsen J.V., Baskcomb L.,
RA Mann M., Jackson S.P., Choudhary C.;
RT "Proteomic investigations reveal a role for RNA processing factor THRAP3 in
RT the DNA damage response.";
RL Mol. Cell 46:212-225(2012).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [29]
RP IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24100041; DOI=10.1074/jbc.m113.500397;
RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
RA Hamakubo T.;
RT "Identification of Wilms' tumor 1-associating protein complex and its role
RT in alternative splicing and the cell cycle.";
RL J. Biol. Chem. 288:33292-33302(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-232; SER-237;
RP SER-240; SER-243; SER-248; SER-253; SER-257; SER-315; SER-320; SER-323;
RP SER-326; SER-377; SER-379; THR-397; SER-406; SER-408; SER-444; SER-468;
RP SER-560; SER-562; SER-575; SER-619; SER-682; SER-698; THR-874; SER-928 AND
RP SER-939, AND 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 [31]
RP ADP-RIBOSYLATION.
RX PubMed=24055347; DOI=10.1016/j.molcel.2013.08.026;
RA Jungmichel S., Rosenthal F., Altmeyer M., Lukas J., Hottiger M.O.,
RA Nielsen M.L.;
RT "Proteome-wide identification of poly(ADP-Ribosyl)ation targets in
RT different genotoxic stress responses.";
RL Mol. Cell 52:272-285(2013).
RN [32]
RP FUNCTION, INTERACTION WITH HELZ2 AND PPARG, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [33]
RP FUNCTION.
RX PubMed=24043798; DOI=10.1073/pnas.1305980110;
RA Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.;
RT "A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the
RT basic transcriptional machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-253; SER-257;
RP SER-320; SER-377; SER-560; SER-575; SER-682 AND SER-684, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 [35]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-66; ARG-101; ARG-108 AND LYS-252,
RP AND IDENTIFICATION BY MASS 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 [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-451; LYS-467; LYS-470; LYS-486;
RP LYS-705; LYS-711; LYS-756 AND LYS-759, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-387 AND LYS-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-396; LYS-427; LYS-451; LYS-470;
RP LYS-486; LYS-527; LYS-697; LYS-705 AND LYS-711, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202; LYS-215; LYS-221; LYS-252;
RP LYS-333; LYS-346; LYS-353; LYS-375; LYS-387; LYS-389; LYS-396; LYS-401;
RP LYS-421; LYS-427; LYS-451; LYS-455; LYS-461; LYS-467; LYS-470; LYS-481;
RP LYS-486; LYS-527; LYS-551; LYS-558; LYS-602; LYS-697; LYS-705; LYS-709;
RP LYS-711; LYS-876 AND LYS-879, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Remains associated with
CC spliced mRNA after splicing which probably involves interactions with
CC the exon junction complex (EJC). Can trigger mRNA decay which seems to
CC be independent of nonsense-mediated decay involving premature stop
CC codons (PTC) recognition. May be involved in nuclear mRNA decay.
CC Involved in regulation of signal-induced alternative splicing. During
CC splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ
CC from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-
CC D1/CCND1 mRNA stability probably by acting as component of the SNARP
CC complex which associates with both the 3'end of the CCND1 gene and its
CC mRNA. Involved in response to DNA damage. Is excluced from DNA damage
CC sites in a manner that parallels transcription inhibition; the function
CC may involve the SNARP complex. Initially thought to play a role in
CC transcriptional coactivation through its association with the TRAP
CC complex; however, it is not regarded as a stable Mediator complex
CC subunit. Cooperatively with HELZ2, enhances the transcriptional
CC activation mediated by PPARG, maybe through the stabilization of the
CC PPARG binding to DNA in presence of ligand. May play a role in the
CC terminal stage of adipocyte differentiation. Plays a role in the
CC positive regulation of the circadian clock. Acts as a coactivator of
CC the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional
CC activator activity and binding to circadian target genes
CC (PubMed:24043798). {ECO:0000269|PubMed:20123736,
CC ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:22424773,
CC ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}.
CC -!- SUBUNIT: Associated with the large multiprotein complex TRAP (Mediator
CC complex-like). Interacts with SFPQ; the interaction is dependent on
CC SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an
CC ESS1 exonic splicing silencer element-containing RNA. Interacts with
CC NXF1. Component of the SNARP complex which consists at least of SNIP1,
CC SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes.
CC Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1
CC (By similarity). Component of a MACOM-like complex, named WTAP complex,
CC composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3.
CC {ECO:0000250|UniProtKB:Q569Z6, ECO:0000269|PubMed:10198638,
CC ECO:0000269|PubMed:17095540, ECO:0000269|PubMed:18794151,
CC ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480,
CC ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24100041}.
CC -!- INTERACTION:
CC Q9Y2W1; P68400: CSNK2A1; NbExp=2; IntAct=EBI-352039, EBI-347804;
CC Q9Y2W1; P38919: EIF4A3; NbExp=2; IntAct=EBI-352039, EBI-299104;
CC Q9Y2W1; Q9UBU9: NXF1; NbExp=4; IntAct=EBI-352039, EBI-398874;
CC Q9Y2W1; P23246: SFPQ; NbExp=6; IntAct=EBI-352039, EBI-355453;
CC Q9Y2W1; Q13573: SNW1; NbExp=4; IntAct=EBI-352039, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20123736,
CC ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24100041}. Nucleus speckle
CC {ECO:0000269|PubMed:24100041}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10198638}.
CC -!- PTM: ADP-ribosylation during genotoxic stress promotes accumulation in
CC nuclear speckles.
CC -!- SIMILARITY: Belongs to the BCLAF1/THRAP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37554.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/THRAP3ID42960ch1p34.html";
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DR EMBL; AF117756; AAD22034.1; -; mRNA.
DR EMBL; AL591845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07379.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07380.1; -; Genomic_DNA.
DR EMBL; BC037554; AAH37554.1; ALT_SEQ; mRNA.
DR EMBL; BC112330; AAI12331.1; -; mRNA.
DR EMBL; BC112350; AAI12351.1; -; mRNA.
DR CCDS; CCDS405.1; -.
DR RefSeq; NP_001308400.1; NM_001321471.1.
DR RefSeq; NP_001308402.1; NM_001321473.1.
DR RefSeq; NP_005110.2; NM_005119.3.
DR AlphaFoldDB; Q9Y2W1; -.
DR BioGRID; 115292; 292.
DR CORUM; Q9Y2W1; -.
DR IntAct; Q9Y2W1; 129.
DR MINT; Q9Y2W1; -.
DR STRING; 9606.ENSP00000346634; -.
DR ChEMBL; CHEMBL4105820; -.
DR GlyGen; Q9Y2W1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2W1; -.
DR MetOSite; Q9Y2W1; -.
DR PhosphoSitePlus; Q9Y2W1; -.
DR SwissPalm; Q9Y2W1; -.
DR BioMuta; THRAP3; -.
DR DMDM; 97537467; -.
DR EPD; Q9Y2W1; -.
DR jPOST; Q9Y2W1; -.
DR MassIVE; Q9Y2W1; -.
DR MaxQB; Q9Y2W1; -.
DR PaxDb; Q9Y2W1; -.
DR PeptideAtlas; Q9Y2W1; -.
DR PRIDE; Q9Y2W1; -.
DR ProteomicsDB; 85914; -.
DR TopDownProteomics; Q9Y2W1; -.
DR Antibodypedia; 1852; 171 antibodies from 31 providers.
DR DNASU; 9967; -.
DR Ensembl; ENST00000354618.10; ENSP00000346634.5; ENSG00000054118.15.
DR Ensembl; ENST00000469141.6; ENSP00000433825.1; ENSG00000054118.15.
DR GeneID; 9967; -.
DR KEGG; hsa:9967; -.
DR MANE-Select; ENST00000354618.10; ENSP00000346634.5; NM_005119.4; NP_005110.2.
DR UCSC; uc001cae.5; human.
DR CTD; 9967; -.
DR DisGeNET; 9967; -.
DR GeneCards; THRAP3; -.
DR HGNC; HGNC:22964; THRAP3.
DR HPA; ENSG00000054118; Low tissue specificity.
DR MIM; 603809; gene.
DR neXtProt; NX_Q9Y2W1; -.
DR OpenTargets; ENSG00000054118; -.
DR PharmGKB; PA134893249; -.
DR VEuPathDB; HostDB:ENSG00000054118; -.
DR eggNOG; ENOG502QR38; Eukaryota.
DR GeneTree; ENSGT00950000183163; -.
DR HOGENOM; CLU_014485_1_0_1; -.
DR InParanoid; Q9Y2W1; -.
DR OMA; SHSYKVE; -.
DR OrthoDB; 380969at2759; -.
DR PhylomeDB; Q9Y2W1; -.
DR TreeFam; TF335939; -.
DR PathwayCommons; Q9Y2W1; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9Y2W1; -.
DR SIGNOR; Q9Y2W1; -.
DR BioGRID-ORCS; 9967; 50 hits in 1093 CRISPR screens.
DR ChiTaRS; THRAP3; human.
DR GeneWiki; THRAP3; -.
DR GenomeRNAi; 9967; -.
DR Pharos; Q9Y2W1; Tbio.
DR PRO; PR:Q9Y2W1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y2W1; protein.
DR Bgee; ENSG00000054118; Expressed in gastrocnemius and 181 other tissues.
DR ExpressionAtlas; Q9Y2W1; baseline and differential.
DR Genevisible; Q9Y2W1; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; NAS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; NAS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR026667; THRAP3.
DR InterPro; IPR029199; THRAP3_BCLAF1.
DR PANTHER; PTHR15268; PTHR15268; 1.
DR PANTHER; PTHR15268:SF16; PTHR15268:SF16; 1.
DR Pfam; PF15440; THRAP3_BCLAF1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ADP-ribosylation; ATP-binding; Biological rhythms;
KW Direct protein sequencing; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..955
FT /note="Thyroid hormone receptor-associated protein 3"
FT /id="PRO_0000065583"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..190
FT /note="Required for mRNA splicing activation"
FT REGION 117..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..955
FT /note="Required for mRNA decay activity"
FT REGION 663..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..776
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 552..559
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|Ref.5"
FT MOD_RES 66
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 101
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 252
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 346
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 481
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 519
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 527
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 558
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 811
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 845
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q569Z6"
FT MOD_RES 874
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 451
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 451
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 705
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 711
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 756
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 759
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 876
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 201
FT /note="A -> V (in dbSNP:rs6425977)"
FT /evidence="ECO:0000269|PubMed:10198638,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_024552"
FT MUTAGEN 406
FT /note="S->A: Reduces phosphorylation upon DNA damage; when
FT associated with A-408."
FT /evidence="ECO:0000269|PubMed:22424773"
FT MUTAGEN 408
FT /note="S->A: Reduces phosphorylation upon DNA damage; when
FT associated with A-406."
FT /evidence="ECO:0000269|PubMed:22424773"
SQ SEQUENCE 955 AA; 108666 MW; 01131D2479B8C0F4 CRC64;
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR SRSYSPAHNR
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS
ELSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE EQKTENGKDK
EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE KPFRGSQSPK RYKLRDDFEK
KMADFHKEEM DDQDKDKAKG RKESEFDDEP KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG
KEKQRKTEEL EEESFPERSK KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK
TSESRDKLGA KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL HERFTKYLKR
GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR EPGYKAEGKY KDDPVDLRLD
IERRKKHKER DLKRGKSRES VDSRDSSHSR ERSAEKTEKT HKGSKKQKKH RRARDRSRSS
SSSSQSSHSY KAEEYTEETE EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG
RGWGRGNYSG NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI QPTTE
