RBP56_HUMAN
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 03-AUG-2022, entry version 218.
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 AlphaFoldDB; Q92804; -.
DR BMRB; Q92804; -.
DR SMR; Q92804; -.
DR BioGRID; 113807; 339.
DR CORUM; Q92804; -.
DR DIP; DIP-52760N; -.
DR IntAct; Q92804; 66.
DR MINT; Q92804; -.
DR STRING; 9606.ENSP00000474096; -.
DR GlyGen; Q92804; 1 site, 1 O-linked glycan (1 site).
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; 331 antibodies from 36 providers.
DR DNASU; 8148; -.
DR Ensembl; ENST00000604841.5; ENSP00000474609.1; ENSG00000270647.7. [Q92804-2]
DR Ensembl; ENST00000605844.6; ENSP00000474096.1; ENSG00000270647.7. [Q92804-1]
DR Ensembl; ENST00000617382.2; ENSP00000480040.1; ENSG00000276833.2. [Q92804-1]
DR Ensembl; ENST00000631482.1; ENSP00000488684.1; ENSG00000276833.2. [Q92804-2]
DR GeneID; 8148; -.
DR KEGG; hsa:8148; -.
DR MANE-Select; ENST00000605844.6; ENSP00000474096.1; NM_139215.3; NP_631961.1.
DR UCSC; uc002hkc.5; human. [Q92804-1]
DR CTD; 8148; -.
DR DisGeNET; 8148; -.
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 VEuPathDB; HostDB:ENSG00000270647; -.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00940000156438; -.
DR HOGENOM; CLU_025609_2_2_1; -.
DR InParanoid; Q92804; -.
DR OMA; NDFRNDQ; -.
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 SignaLink; Q92804; -.
DR SIGNOR; Q92804; -.
DR BioGRID-ORCS; 8148; 31 hits in 1081 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 endometrium and 101 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:0008380; P:RNA splicing; IEA:Ensembl.
DR DisProt; DP02345; -.
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 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:24129315"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 268
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 431
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 459
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 475
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|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:0007744|PubMed:21406692"
FT MOD_RES 562
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|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:0007744|PubMed:28112733"
FT CROSSLNK 268
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|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:0007829|PDB:2MMY"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:2MMY"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:2MMY"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:2MMY"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:2MMY"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2MMY"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:2MMY"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2MMY"
FT STRAND 314..316
FT /evidence="ECO:0007829|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
