ID RBP56_HUMAN Reviewed; 592 AA. AC Q92804; B2R837; Q86X94; Q92751; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 12-AUG-2020, entry version 209. DE RecName: Full=TATA-binding protein-associated factor 2N; DE AltName: Full=68 kDa TATA-binding protein-associated factor; DE Short=TAF(II)68; DE Short=TAFII68; DE AltName: Full=RNA-binding protein 56; GN Name=TAF15; Synonyms=RBP56, TAF2N; 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] (ISOFORMS LONG AND SHORT). RX PubMed=8954779; DOI=10.1006/geno.1996.0591; RA Morohoshi F., Arai K., Takahashi E., Tanigami A., Ohki M.; RT "Cloning and mapping of a human RBP56 gene encoding a putative RNA binding RT protein similar to FUS/TLS and EWS proteins."; RL Genomics 38:51-57(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND PROTEIN SEQUENCE OF 282-297 RP AND 307-320. RX PubMed=8890175; DOI=10.1002/j.1460-2075.1996.tb00882.x; RA Bertolotti A., Lutz Y., Heard D.J., Chambon P., Tora L.; RT "hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro- RT oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA RT polymerase II."; RL EMBO J. 15:5022-5031(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT). RX PubMed=9795213; DOI=10.1016/s0378-1119(98)00463-6; RA Morohoshi F., Ootsuka Y., Arai K., Ichikawa H., Mitani S., Munakata N., RA Ohki M.; RT "Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes."; RL Gene 221:191-198(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND LONG). RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Testis; 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 [9] RP PROTEIN SEQUENCE OF 75-101; 196-210; 284-306; 476-490 AND 563-576, RP METHYLATION AT ARG-206; ARG-483 AND ARG-570, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP INTERACTION WITH SF1. RX PubMed=9660765; DOI=10.1074/jbc.273.29.18086; RA Zhang D., Paley A.J., Childs G.; RT "The transcriptional repressor ZFM1 interacts with and modulates the RT ability of EWS to activate transcription."; RL J. Biol. Chem. 273:18086-18091(1998). RN [11] RP CHROMOSOMAL TRANSLOCATION WITH NR4A3. RX PubMed=10602519; DOI=10.1038/sj.onc.1203155; RA Panagopoulos I., Mencinger M., Dietrich C.U., Bjerkehagen B., Saeter G., RA Mertens F., Mandahl N., Heim S.; RT "Fusion of the RBP56 and CHN genes in extraskeletal myxoid chondrosarcomas RT with translocation t(9;17)(q22;q11)."; RL Oncogene 18:7594-7598(1999). 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP FUNCTION, METHYLATION AT ARG-206; ARG-528; ARG-535 AND ARG-570 BY PRMT1, RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=19124016; DOI=10.1016/j.yexcr.2008.12.008; RA Jobert L., Argentini M., Tora L.; RT "PRMT1 mediated methylation of TAF15 is required for its positive gene RT regulatory function."; RL Exp. Cell Res. 315:1273-1286(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-231, 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-438; SER-442; RP SER-451 AND SER-554, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-438, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY RP 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 [22] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206; ARG-431; ARG-459; ARG-475 RP AND ARG-562, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-268, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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: RNA and ssDNA-binding protein that may play specific roles CC during transcription initiation at distinct promoters. Can enter the CC preinitiation complex together with the RNA polymerase II (Pol II). CC {ECO:0000269|PubMed:19124016}. CC -!- SUBUNIT: Belongs to the RNA polymerase II (Pol II) transcriptional CC multiprotein complex, together with the TATA-binding protein (TBP) and CC other TBP-associated factors (TAF(II)s). Binds SF1. CC -!- INTERACTION: CC Q92804; P35637: FUS; NbExp=7; IntAct=EBI-2255091, EBI-400434; CC Q92804; Q92993: KAT5; NbExp=2; IntAct=EBI-2255091, EBI-399080; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19124016}. Cytoplasm CC {ECO:0000269|PubMed:19124016}. Note=Shuttles from the nucleus to the CC cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q92804-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q92804-2; Sequence=VSP_005806; CC -!- TISSUE SPECIFICITY: Ubiquitous. Observed in all fetal and adult CC tissues. CC -!- PTM: Dimethylated by PRMT1 at Arg-206 to asymmetric dimethylarginine. CC The methylation may favor nuclear localization and positive regulation CC of TAF15 transcriptional activity. {ECO:0000269|PubMed:19124016, CC ECO:0000269|Ref.9}. CC -!- PTM: ADP-ribosylated during genotoxic stress. CC -!- DISEASE: Note=A chromosomal aberration involving TAF15/TAF2N is found CC in a form of extraskeletal myxoid chondrosarcomas (EMC). Translocation CC t(9;17)(q22;q11) with NR4A3. {ECO:0000269|PubMed:10602519}. CC -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/TAF2NID256.html"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/taf15/"; 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; U51334; AAC50932.1; -; mRNA. DR EMBL; X98893; CAA67398.1; -; mRNA. DR EMBL; AB010067; BAA33811.1; -; Genomic_DNA. DR EMBL; AB010067; BAA33812.1; -; Genomic_DNA. DR EMBL; AY197697; AAO13485.1; -; Genomic_DNA. DR EMBL; AK313223; BAG36034.1; -; mRNA. DR EMBL; AK314194; BAG36873.1; -; mRNA. DR EMBL; AC015849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471147; EAW80124.1; -; Genomic_DNA. DR EMBL; CH471147; EAW80125.1; -; Genomic_DNA. DR EMBL; BC046099; AAH46099.2; -; mRNA. DR CCDS; CCDS32623.1; -. [Q92804-1] DR CCDS; CCDS59279.1; -. [Q92804-2] DR PIR; S71954; S71954. DR RefSeq; NP_003478.1; NM_003487.3. [Q92804-2] DR RefSeq; NP_631961.1; NM_139215.2. [Q92804-1] DR PDB; 2MMY; NMR; -; A=231-323. DR PDBsum; 2MMY; -. DR SMR; Q92804; -. DR BioGRID; 113807; 310. DR CORUM; Q92804; -. DR DIP; DIP-52760N; -. DR IntAct; Q92804; 59. DR MINT; Q92804; -. DR STRING; 9606.ENSP00000474096; -. DR iPTMnet; Q92804; -. DR PhosphoSitePlus; Q92804; -. DR SwissPalm; Q92804; -. DR BioMuta; TAF15; -. DR DMDM; 8928305; -. DR EPD; Q92804; -. DR jPOST; Q92804; -. DR MassIVE; Q92804; -. DR MaxQB; Q92804; -. DR PaxDb; Q92804; -. DR PeptideAtlas; Q92804; -. DR PRIDE; Q92804; -. DR ProteomicsDB; 75488; -. [Q92804-1] DR ProteomicsDB; 75489; -. [Q92804-2] DR Antibodypedia; 74808; 305 antibodies. DR DNASU; 8148; -. DR Ensembl; ENST00000604841; ENSP00000474609; ENSG00000270647. [Q92804-2] DR Ensembl; ENST00000605844; ENSP00000474096; ENSG00000270647. [Q92804-1] DR Ensembl; ENST00000617382; ENSP00000480040; ENSG00000276833. [Q92804-1] DR Ensembl; ENST00000631482; ENSP00000488684; ENSG00000276833. [Q92804-2] DR GeneID; 8148; -. DR KEGG; hsa:8148; -. DR UCSC; uc002hkc.5; human. [Q92804-1] DR CTD; 8148; -. DR DisGeNET; 8148; -. DR EuPathDB; HostDB:ENSG00000270647.5; -. DR GeneCards; TAF15; -. DR HGNC; HGNC:11547; TAF15. DR HPA; ENSG00000270647; Low tissue specificity. DR MalaCards; TAF15; -. DR MIM; 601574; gene. DR neXtProt; NX_Q92804; -. DR OpenTargets; ENSG00000270647; -. DR Orphanet; 803; Amyotrophic lateral sclerosis. DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma. DR PharmGKB; PA36322; -. DR eggNOG; KOG1995; Eukaryota. DR GeneTree; ENSGT00940000156438; -. DR HOGENOM; CLU_025609_2_2_1; -. DR InParanoid; Q92804; -. DR KO; K14651; -. DR OMA; HQSSYDQ; -. DR OrthoDB; 1539664at2759; -. DR PhylomeDB; Q92804; -. DR PathwayCommons; Q92804; -. DR Reactome; R-HSA-167161; HIV Transcription Initiation. DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape. DR Reactome; R-HSA-167172; Transcription of the HIV genome. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR SIGNOR; Q92804; -. DR BioGRID-ORCS; 8148; 19 hits in 877 CRISPR screens. DR ChiTaRS; TAF15; human. DR GeneWiki; TAF15; -. DR GenomeRNAi; 8148; -. DR Pharos; Q92804; Tbio. DR PRO; PR:Q92804; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q92804; protein. DR Bgee; ENSG00000270647; Expressed in tendon of biceps brachii and 242 other tissues. DR ExpressionAtlas; Q92804; baseline and differential. DR Genevisible; Q92804; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0048255; P:mRNA stabilization; IDA:MGI. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR GO; GO:0008380; P:RNA splicing; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR034875; TAF15. DR InterPro; IPR034870; TET_fam. DR InterPro; IPR001876; Znf_RanBP2. DR InterPro; IPR036443; Znf_RanBP2_sf. DR PANTHER; PTHR23238; PTHR23238; 1. DR PANTHER; PTHR23238:SF25; PTHR23238:SF25; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF00641; zf-RanBP; 1. DR SMART; SM00360; RRM; 1. DR SMART; SM00547; ZnF_RBZ; 1. DR SUPFAM; SSF54928; SSF54928; 1. DR SUPFAM; SSF90209; SSF90209; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS01358; ZF_RANBP2_1; 1. DR PROSITE; PS50199; ZF_RANBP2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; KW Chromosomal rearrangement; Cytoplasm; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus; KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; RNA-binding; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..592 FT /note="TATA-binding protein-associated factor 2N" FT /id="PRO_0000081749" FT DOMAIN 234..320 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REPEAT 407..413 FT /note="1" FT REPEAT 414..420 FT /note="2" FT REPEAT 421..429 FT /note="3" FT REPEAT 430..439 FT /note="4" FT REPEAT 440..448 FT /note="5" FT REPEAT 449..457 FT /note="6" FT REPEAT 458..465 FT /note="7" FT REPEAT 466..473 FT /note="8" FT REPEAT 474..481 FT /note="9" FT REPEAT 482..488 FT /note="10" FT REPEAT 489..496 FT /note="11" FT REPEAT 497..503 FT /note="12" FT REPEAT 504..510 FT /note="13" FT REPEAT 511..517 FT /note="14" FT REPEAT 518..524 FT /note="15" FT REPEAT 525..533 FT /note="16" FT REPEAT 534..543 FT /note="17" FT REPEAT 544..551 FT /note="18" FT REPEAT 552..560 FT /note="19" FT REPEAT 561..568 FT /note="20" FT REPEAT 569..575 FT /note="21" FT ZN_FING 354..385 FT /note="RanBP2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322" FT REGION 407..575 FT /note="21 X approximate tandem repeats of D-R-[S,G](0,3)-G- FT G-Y-G-G" FT COMPBIAS 1..208 FT /note="Gln/Gly/Ser/Tyr-rich" FT COMPBIAS 320..590 FT /note="Arg/Gly-rich" FT MOD_RES 206 FT /note="Asymmetric dimethylarginine; by PRMT1; alternate" FT /evidence="ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9" FT MOD_RES 206 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 226 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19690332" FT MOD_RES 231 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19690332" FT MOD_RES 268 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692" FT MOD_RES 431 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163" FT MOD_RES 442 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692" FT MOD_RES 459 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 475 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 483 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|Ref.9" FT MOD_RES 528 FT /note="Asymmetric dimethylarginine; by PRMT1" FT /evidence="ECO:0000269|PubMed:19124016" FT MOD_RES 535 FT /note="Asymmetric dimethylarginine; by PRMT1" FT /evidence="ECO:0000269|PubMed:19124016" FT MOD_RES 554 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:21406692" FT MOD_RES 562 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 570 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9" FT MOD_RES 570 FT /note="Asymmetric dimethylarginine; by PRMT1" FT /evidence="ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9" FT CROSSLNK 265 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 268 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000244|PubMed:28112733" FT VAR_SEQ 60..62 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:8890175, ECO:0000303|PubMed:8954779" FT /id="VSP_005806" FT STRAND 236..240 FT /evidence="ECO:0000244|PDB:2MMY" FT HELIX 250..255 FT /evidence="ECO:0000244|PDB:2MMY" FT TURN 264..266 FT /evidence="ECO:0000244|PDB:2MMY" FT STRAND 272..274 FT /evidence="ECO:0000244|PDB:2MMY" FT TURN 277..279 FT /evidence="ECO:0000244|PDB:2MMY" FT STRAND 285..288 FT /evidence="ECO:0000244|PDB:2MMY" FT HELIX 293..301 FT /evidence="ECO:0000244|PDB:2MMY" FT STRAND 304..308 FT /evidence="ECO:0000244|PDB:2MMY" FT STRAND 314..316 FT /evidence="ECO:0000244|PDB:2MMY" SQ SEQUENCE 592 AA; 61830 MW; 73D37C171E1E2BCA CRC64; MSDSGSYGQS GGEQQSYSTY GNPGSQGYGQ ASQSYSGYGQ TTDSSYGQNY SGYSSYGQSQ SGYSQSYGGY ENQKQSSYSQ QPYNNQGQQQ NMESSGSQGG RAPSYDQPDY GQQDSYDQQS GYDQHQGSYD EQSNYDQQHD SYSQNQQSYH SQRENYSHHT QDDRRDVSRY GEDNRGYGGS QGGGRGRGGY DKDGRGPMTG SSGGDRGGFK NFGGHRDYGP RTDADSESDN SDNNTIFVQG LGEGVSTDQV GEFFKQIGII KTNKKTGKPM INLYTDKDTG KPKGEATVSF DDPPSAKAAI DWFDGKEFHG NIIKVSFATR RPEFMRGGGS GGGRRGRGGY RGRGGFQGRG GDPKSGDWVC PNPSCGNMNF ARRNSCNQCN EPRPEDSRPS GGDFRGRGYG GERGYRGRGG RGGDRGGYGG DRSGGGYGGD RSSGGGYSGD RSGGGYGGDR SGGGYGGDRG GGYGGDRGGG YGGDRGGGYG GDRGGYGGDR GGGYGGDRGG YGGDRGGYGG DRGGYGGDRG GYGGDRSRGG YGGDRGGGSG YGGDRSGGYG GDRSGGGYGG DRGGGYGGDR GGYGGKMGGR NDYRNDQRNR PY //