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 27-MAR-2024, entry version 212. 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-BMAL1 heterodimer and promotes its transcriptional activator CC activity and binding to circadian target genes (PubMed:24043798). CC {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480, CC ECO:0000269|PubMed:22424773, ECO:0000269|PubMed:23525231, CC 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 BMAL1 (By CC 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="https://atlasgeneticsoncology.org/gene/42960/THRAP3"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 426. DR ComplexPortal; CPX-2653; SNIP1/SkIP associated RNA-processing complex. DR CORUM; Q9Y2W1; -. DR IntAct; Q9Y2W1; 141. DR MINT; Q9Y2W1; -. DR STRING; 9606.ENSP00000346634; -. DR ChEMBL; CHEMBL4105820; -. DR GlyCosmos; Q9Y2W1; 1 site, 1 glycan. DR GlyGen; Q9Y2W1; 8 sites, 1 O-linked glycan (8 sites). 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; 9606-ENSP00000346634; -. DR PeptideAtlas; Q9Y2W1; -. DR ProteomicsDB; 85914; -. DR Pumba; Q9Y2W1; -. DR TopDownProteomics; Q9Y2W1; -. DR Antibodypedia; 1852; 197 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 AGR; HGNC:22964; -. 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; 5323286at2759; -. 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 1173 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 183 other cell types or tissues. DR ExpressionAtlas; Q9Y2W1; baseline and differential. 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:0045893; P:positive regulation of DNA-templated transcription; IDA: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:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR InterPro; IPR029199; THRAP3_BCLAF1. DR PANTHER; PTHR15268; THRAP3/BCLAF1; 1. DR PANTHER; PTHR15268:SF16; THYROID HORMONE RECEPTOR-ASSOCIATED PROTEIN 3; 1. DR Pfam; PF15440; THRAP3_BCLAF1; 1. DR Genevisible; Q9Y2W1; HS. 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 //