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 16-OCT-2013, entry version 129. DE RecName: Full=Thyroid hormone receptor-associated protein 3; DE AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component; DE Short=Trap150; GN Name=THRAP3; Synonyms=TRAP150; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Fu Z.-Y., Zhang X., Qin J., Roeder R.G.; RT "Identity between TRAP and SMCC complexes indicates novel pathways for RT the 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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; RP 443-451; 468-481; 486-498; 573-591; 609-653; 678-687; 710-718; RP 792-802; 864-876; 879-893 AND 927-944, METHYLATION AT ARG-17, RP PHOSPHORYLATION AT SER-243; SER-320 AND SER-682, AND MASS RP 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 [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 RT from human T cells using immobilized metal affinity chromatography and RT tandem mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [7] 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 MASS RP SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASS RP SPECTROMETRY. 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 RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] 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 RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [10] 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 [11] 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, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., 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 [12] 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., RA Perkins N.D.; RT "Regulation of cyclin D1 RNA stability by SNIP1."; RL Cancer Res. 68:7621-7628(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248 AND RP SER-253, AND MASS SPECTROMETRY. 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., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASS RP SPECTROMETRY. 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 RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASS RP SPECTROMETRY. 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [16] 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; RP SER-682; THR-874; SER-928 AND SER-939, AND MASS SPECTROMETRY. 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, AND MASS RP SPECTROMETRY. 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 RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [18] 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., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-874; SER-928 AND RP SER-939, AND MASS SPECTROMETRY. 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-455; LYS-519 AND RP LYS-811, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [21] 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 [22] 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 [23] 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; RP SER-622; SER-682; SER-698; SER-928 AND SER-939, AND MASS SPECTROMETRY. 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] 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., RA Buerckstuemmer T., 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 [25] 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; RP SER-622; SER-682; SER-698; SER-928 AND SER-939, AND MASS SPECTROMETRY. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] 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., RA Baskcomb L., Mann M., Jackson S.P., Choudhary C.; RT "Proteomic investigations reveal a role for RNA processing factor RT THRAP3 in the DNA damage response."; RL Mol. Cell 46:212-225(2012). CC -!- FUNCTION: Involved in pre-mRNA splicing. Remains associated with CC spliced mRNA after splicing which probably involves interactions CC with the exon junction complex (EJC). Can trigger mRNA decay which CC seems to be independent of nonsense-mediated decay involving CC premature stop codons (PTC) recognition. May be involved in CC nuclear mRNA decay. Involved in regulation of signal-induced CC alternative splicing. During splicing of PTPRC/CD45 is proposed to CC sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting CC T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by CC acting as component of the SNARP complex which associates with CC both the 3'end of the CCND1 gene and its mRNA. Involved in CC response to DNA damage. Is excluced from DNA damage sites in a CC manner that parallels transcription inhibition; the function may CC 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. CC -!- SUBUNIT: Associated with the large multiprotein complex TRAP CC (Mediator complex-like). Interacts with SFPQ; the interaction is CC dependent on SFPQ phosphorylation at 'Thr-687' and inhibits CC binding of SFPQ to an ESS1 exonic splicing silencer element- CC containing RNA. Interacts with NXF1. Component of the SNARP CC complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and CC PNN. Associated with spliced mRNP complexes. CC -!- INTERACTION: CC P38919:EIF4A3; NbExp=2; IntAct=EBI-352039, EBI-299104; CC Q9UBU9:NXF1; NbExp=4; IntAct=EBI-352039, EBI-398874; CC P23246:SFPQ; NbExp=6; IntAct=EBI-352039, EBI-355453; CC Q13573:SNW1; NbExp=4; IntAct=EBI-352039, EBI-632715; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SEQUENCE CAUTION: CC Sequence=AAH37554.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/THRAP3ID42960ch1p34.html"; 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; CAH71859.1; -; 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 IPI; IPI00104050; -. DR RefSeq; NP_005110.2; NM_005119.3. DR UniGene; Hs.744057; -. DR ProteinModelPortal; Q9Y2W1; -. DR IntAct; Q9Y2W1; 38. DR MINT; MINT-1684118; -. DR STRING; 9606.ENSP00000346634; -. DR PhosphoSite; Q9Y2W1; -. DR DMDM; 97537467; -. DR PaxDb; Q9Y2W1; -. DR PeptideAtlas; Q9Y2W1; -. DR PRIDE; Q9Y2W1; -. DR DNASU; 9967; -. DR Ensembl; ENST00000354618; ENSP00000346634; ENSG00000054118. DR Ensembl; ENST00000469141; ENSP00000433825; ENSG00000054118. DR GeneID; 9967; -. DR KEGG; hsa:9967; -. DR UCSC; uc001cae.4; human. DR CTD; 9967; -. DR GeneCards; GC01P036690; -. DR HGNC; HGNC:22964; THRAP3. DR HPA; CAB017472; -. DR HPA; HPA012041; -. DR MIM; 603809; gene. DR neXtProt; NX_Q9Y2W1; -. DR PharmGKB; PA134893249; -. DR eggNOG; NOG43306; -. DR HOGENOM; HOG000231570; -. DR HOVERGEN; HBG054554; -. DR InParanoid; Q9Y2W1; -. DR KO; K13112; -. DR OMA; RSTEKTE; -. DR OrthoDB; EOG4NKBVJ; -. DR PhylomeDB; Q9Y2W1; -. DR SignaLink; Q9Y2W1; -. DR ChiTaRS; THRAP3; human. DR GeneWiki; THRAP3; -. DR GenomeRNAi; 9967; -. DR NextBio; 37614; -. DR PRO; PR:Q9Y2W1; -. DR ArrayExpress; Q9Y2W1; -. DR Bgee; Q9Y2W1; -. DR CleanEx; HS_THRAP3; -. DR Genevestigator; Q9Y2W1; -. DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; NAS:UniProtKB. DR GO; GO:0051219; F:phosphoprotein binding; IDA:UniProtKB. DR GO; GO:0004872; F:receptor activity; IDA:UniProtKB. DR GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IDA:UniProtKB. DR GO; GO:0046966; F:thyroid hormone receptor binding; IDA:UniProtKB. DR GO; GO:0042809; F:vitamin D receptor binding; NAS:UniProtKB. DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB. 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:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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 GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB. DR InterPro; IPR026667; THRAP3. DR PANTHER; PTHR15268:SF7; PTHR15268:SF7; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; ATP-binding; Complete proteome; KW Direct protein sequencing; Methylation; mRNA processing; KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Receptor; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 955 Thyroid hormone receptor-associated FT protein 3. FT /FTId=PRO_0000065583. FT NP_BIND 552 559 ATP (Potential). FT REGION 1 190 Required for mRNA splicing activation. FT REGION 359 955 Required for mRNA decay activity. FT COMPBIAS 7 339 Ser-rich. FT COMPBIAS 12 161 Arg-rich. FT MOD_RES 17 17 Dimethylated arginine. FT MOD_RES 51 51 Phosphoserine (By similarity). FT MOD_RES 53 53 Phosphoserine (By similarity). FT MOD_RES 55 55 Phosphoserine (By similarity). FT MOD_RES 119 119 Phosphoserine (By similarity). FT MOD_RES 134 134 Phosphoserine (By similarity). FT MOD_RES 221 221 N6-acetyllysine. FT MOD_RES 232 232 Phosphoserine. FT MOD_RES 237 237 Phosphoserine. FT MOD_RES 240 240 Phosphoserine. FT MOD_RES 243 243 Phosphoserine. FT MOD_RES 248 248 Phosphoserine. FT MOD_RES 253 253 Phosphoserine. FT MOD_RES 257 257 Phosphoserine. FT MOD_RES 264 264 Phosphoserine (By similarity). FT MOD_RES 268 268 Phosphoserine (By similarity). FT MOD_RES 315 315 Phosphoserine. FT MOD_RES 320 320 Phosphoserine. FT MOD_RES 324 324 Phosphothreonine (By similarity). FT MOD_RES 339 339 Phosphoserine. FT MOD_RES 379 379 Phosphoserine. FT MOD_RES 406 406 Phosphoserine. FT MOD_RES 408 408 Phosphoserine. FT MOD_RES 455 455 N6-acetyllysine. FT MOD_RES 519 519 N6-acetyllysine. FT MOD_RES 535 535 Phosphoserine. FT MOD_RES 575 575 Phosphoserine. FT MOD_RES 622 622 Phosphoserine. FT MOD_RES 672 672 Phosphoserine. FT MOD_RES 682 682 Phosphoserine. FT MOD_RES 698 698 Phosphoserine. FT MOD_RES 811 811 N6-acetyllysine. FT MOD_RES 874 874 Phosphothreonine. FT MOD_RES 928 928 Phosphoserine. FT MOD_RES 939 939 Phosphoserine. FT MOD_RES 941 941 Phosphothreonine (By similarity). FT VARIANT 201 201 A -> V (in dbSNP:rs6425977). FT /FTId=VAR_024552. FT MUTAGEN 406 406 S->A: Reduces phosphorylation upon DNA FT damage; when associated with A-408. FT MUTAGEN 408 408 S->A: Reduces phosphorylation upon DNA FT damage; when associated with A-406. 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 //