Full text data of TAF15
TAF15
(RBP56, TAF2N)
[Confidence: low (only semi-automatic identification from reviews)]
TATA-binding protein-associated factor 2N (68 kDa TATA-binding protein-associated factor; TAF(II)68; TAFII68; RNA-binding protein 56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TATA-binding protein-associated factor 2N (68 kDa TATA-binding protein-associated factor; TAF(II)68; TAFII68; RNA-binding protein 56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92804
ID RBP56_HUMAN Reviewed; 592 AA.
AC Q92804; B2R837; Q92751;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 147.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT binding 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
RP 282-297 AND 307-320.
RX PubMed=8890175;
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
RT pro-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.,
RA Munakata N., 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] (ISOFORM SHORT).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
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 [8]
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 MASS 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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, METHYLATION AT ARG-206 BY PRMT1, MASS SPECTROMETRY, AND
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-231, AND
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-438; SER-442;
RP SER-451 AND SER-554, 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).
CC -!- FUNCTION: RNA and ssDNA-binding protein that may play specific
CC roles during transcription initiation at distinct promoters. Can
CC enter the preinitiation complex together with the RNA polymerase
CC II (Pol II).
CC -!- SUBUNIT: Belongs to the RNA polymerase II (Pol II) transcriptional
CC multiprotein complex, together with the TATA-binding protein (TBP)
CC and other TBP-associated factors (TAF(II)s). Binds SF1.
CC -!- INTERACTION:
CC P35637:FUS; NbExp=5; IntAct=EBI-2255091, EBI-400434;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles from the
CC nucleus to the 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
CC dimethylarginine. The methylation may favor nuclear localization
CC and positive regulation of TAF15 transcriptional activity.
CC -!- DISEASE: Note=A chromosomal aberration involving TAF15/TAF2N is
CC found in a form of extraskeletal myxoid chondrosarcomas (EMC).
CC Translocation t(9;17)(q22;q11) with NR4A3.
CC -!- SIMILARITY: Belongs to the RRM TET family.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TAF2NID256.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf15/";
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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; AC015849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80124.1; -; Genomic_DNA.
DR PIR; S71954; S71954.
DR RefSeq; NP_003478.1; NM_003487.3.
DR RefSeq; NP_631961.1; NM_139215.2.
DR UniGene; Hs.402752; -.
DR ProteinModelPortal; Q92804; -.
DR SMR; Q92804; 232-319.
DR IntAct; Q92804; 20.
DR MINT; MINT-3049394; -.
DR STRING; 9606.ENSP00000309558; -.
DR PhosphoSite; Q92804; -.
DR DMDM; 8928305; -.
DR PaxDb; Q92804; -.
DR PRIDE; Q92804; -.
DR DNASU; 8148; -.
DR Ensembl; ENST00000311979; ENSP00000309558; ENSG00000172660.
DR Ensembl; ENST00000588240; ENSP00000466950; ENSG00000172660.
DR Ensembl; ENST00000604841; ENSP00000474609; ENSG00000270647.
DR Ensembl; ENST00000605844; ENSP00000474096; ENSG00000270647.
DR GeneID; 8148; -.
DR KEGG; hsa:8148; -.
DR UCSC; uc002hkd.4; human.
DR CTD; 8148; -.
DR GeneCards; GC17P034136; -.
DR HGNC; HGNC:11547; TAF15.
DR HPA; HPA052059; -.
DR MIM; 601574; gene.
DR neXtProt; NX_Q92804; -.
DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
DR PharmGKB; PA36322; -.
DR eggNOG; NOG240581; -.
DR HOGENOM; HOG000038010; -.
DR HOVERGEN; HBG005755; -.
DR InParanoid; Q92804; -.
DR KO; K14651; -.
DR OMA; QKQSSYS; -.
DR OrthoDB; EOG7DZ8N7; -.
DR PhylomeDB; Q92804; -.
DR ChiTaRS; TAF15; human.
DR GeneWiki; TAF15; -.
DR GenomeRNAi; 8148; -.
DR NextBio; 30819; -.
DR PMAP-CutDB; Q92804; -.
DR PRO; PR:Q92804; -.
DR ArrayExpress; Q92804; -.
DR Bgee; Q92804; -.
DR CleanEx; HS_TAF15; -.
DR Genevestigator; Q92804; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1060.10; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 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 Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1 592 TATA-binding protein-associated factor
FT 2N.
FT /FTId=PRO_0000081749.
FT DOMAIN 234 320 RRM.
FT REPEAT 407 413 1.
FT REPEAT 414 420 2.
FT REPEAT 421 429 3.
FT REPEAT 430 439 4.
FT REPEAT 440 448 5.
FT REPEAT 449 457 6.
FT REPEAT 458 465 7.
FT REPEAT 466 473 8.
FT REPEAT 474 481 9.
FT REPEAT 482 488 10.
FT REPEAT 489 496 11.
FT REPEAT 497 503 12.
FT REPEAT 504 510 13.
FT REPEAT 511 517 14.
FT REPEAT 518 524 15.
FT REPEAT 525 533 16.
FT REPEAT 534 543 17.
FT REPEAT 544 551 18.
FT REPEAT 552 560 19.
FT REPEAT 561 568 20.
FT REPEAT 569 575 21.
FT ZN_FING 354 385 RanBP2-type.
FT REGION 407 575 21 X approximate tandem repeats of D-R-
FT [S,G](0,3)-G-G-Y-G-G.
FT COMPBIAS 1 208 Gln/Gly/Ser/Tyr-rich.
FT COMPBIAS 320 590 Arg/Gly-rich.
FT MOD_RES 206 206 Asymmetric dimethylarginine; by PRMT1.
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 268 268 N6-acetyllysine.
FT MOD_RES 423 423 Phosphoserine.
FT MOD_RES 438 438 Phosphoserine.
FT MOD_RES 442 442 Phosphoserine.
FT MOD_RES 451 451 Phosphoserine.
FT MOD_RES 483 483 Dimethylated arginine.
FT MOD_RES 528 528 Asymmetric dimethylarginine.
FT MOD_RES 535 535 Asymmetric dimethylarginine.
FT MOD_RES 554 554 Phosphoserine.
FT MOD_RES 570 570 Asymmetric dimethylarginine.
FT VAR_SEQ 60 62 Missing (in isoform Short).
FT /FTId=VSP_005806.
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
//
ID RBP56_HUMAN Reviewed; 592 AA.
AC Q92804; B2R837; Q92751;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1997, sequence version 1.
DT 22-JAN-2014, entry version 147.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT binding 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
RP 282-297 AND 307-320.
RX PubMed=8890175;
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
RT pro-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.,
RA Munakata N., 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] (ISOFORM SHORT).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
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 [8]
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 MASS 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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, METHYLATION AT ARG-206 BY PRMT1, MASS SPECTROMETRY, AND
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-231, AND
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-438; SER-442;
RP SER-451 AND SER-554, 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).
CC -!- FUNCTION: RNA and ssDNA-binding protein that may play specific
CC roles during transcription initiation at distinct promoters. Can
CC enter the preinitiation complex together with the RNA polymerase
CC II (Pol II).
CC -!- SUBUNIT: Belongs to the RNA polymerase II (Pol II) transcriptional
CC multiprotein complex, together with the TATA-binding protein (TBP)
CC and other TBP-associated factors (TAF(II)s). Binds SF1.
CC -!- INTERACTION:
CC P35637:FUS; NbExp=5; IntAct=EBI-2255091, EBI-400434;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles from the
CC nucleus to the 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
CC dimethylarginine. The methylation may favor nuclear localization
CC and positive regulation of TAF15 transcriptional activity.
CC -!- DISEASE: Note=A chromosomal aberration involving TAF15/TAF2N is
CC found in a form of extraskeletal myxoid chondrosarcomas (EMC).
CC Translocation t(9;17)(q22;q11) with NR4A3.
CC -!- SIMILARITY: Belongs to the RRM TET family.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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 -----------------------------------------------------------------------
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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; AC015849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80124.1; -; Genomic_DNA.
DR PIR; S71954; S71954.
DR RefSeq; NP_003478.1; NM_003487.3.
DR RefSeq; NP_631961.1; NM_139215.2.
DR UniGene; Hs.402752; -.
DR ProteinModelPortal; Q92804; -.
DR SMR; Q92804; 232-319.
DR IntAct; Q92804; 20.
DR MINT; MINT-3049394; -.
DR STRING; 9606.ENSP00000309558; -.
DR PhosphoSite; Q92804; -.
DR DMDM; 8928305; -.
DR PaxDb; Q92804; -.
DR PRIDE; Q92804; -.
DR DNASU; 8148; -.
DR Ensembl; ENST00000311979; ENSP00000309558; ENSG00000172660.
DR Ensembl; ENST00000588240; ENSP00000466950; ENSG00000172660.
DR Ensembl; ENST00000604841; ENSP00000474609; ENSG00000270647.
DR Ensembl; ENST00000605844; ENSP00000474096; ENSG00000270647.
DR GeneID; 8148; -.
DR KEGG; hsa:8148; -.
DR UCSC; uc002hkd.4; human.
DR CTD; 8148; -.
DR GeneCards; GC17P034136; -.
DR HGNC; HGNC:11547; TAF15.
DR HPA; HPA052059; -.
DR MIM; 601574; gene.
DR neXtProt; NX_Q92804; -.
DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
DR PharmGKB; PA36322; -.
DR eggNOG; NOG240581; -.
DR HOGENOM; HOG000038010; -.
DR HOVERGEN; HBG005755; -.
DR InParanoid; Q92804; -.
DR KO; K14651; -.
DR OMA; QKQSSYS; -.
DR OrthoDB; EOG7DZ8N7; -.
DR PhylomeDB; Q92804; -.
DR ChiTaRS; TAF15; human.
DR GeneWiki; TAF15; -.
DR GenomeRNAi; 8148; -.
DR NextBio; 30819; -.
DR PMAP-CutDB; Q92804; -.
DR PRO; PR:Q92804; -.
DR ArrayExpress; Q92804; -.
DR Bgee; Q92804; -.
DR CleanEx; HS_TAF15; -.
DR Genevestigator; Q92804; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; TAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1060.10; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 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 Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1 592 TATA-binding protein-associated factor
FT 2N.
FT /FTId=PRO_0000081749.
FT DOMAIN 234 320 RRM.
FT REPEAT 407 413 1.
FT REPEAT 414 420 2.
FT REPEAT 421 429 3.
FT REPEAT 430 439 4.
FT REPEAT 440 448 5.
FT REPEAT 449 457 6.
FT REPEAT 458 465 7.
FT REPEAT 466 473 8.
FT REPEAT 474 481 9.
FT REPEAT 482 488 10.
FT REPEAT 489 496 11.
FT REPEAT 497 503 12.
FT REPEAT 504 510 13.
FT REPEAT 511 517 14.
FT REPEAT 518 524 15.
FT REPEAT 525 533 16.
FT REPEAT 534 543 17.
FT REPEAT 544 551 18.
FT REPEAT 552 560 19.
FT REPEAT 561 568 20.
FT REPEAT 569 575 21.
FT ZN_FING 354 385 RanBP2-type.
FT REGION 407 575 21 X approximate tandem repeats of D-R-
FT [S,G](0,3)-G-G-Y-G-G.
FT COMPBIAS 1 208 Gln/Gly/Ser/Tyr-rich.
FT COMPBIAS 320 590 Arg/Gly-rich.
FT MOD_RES 206 206 Asymmetric dimethylarginine; by PRMT1.
FT MOD_RES 226 226 Phosphoserine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 268 268 N6-acetyllysine.
FT MOD_RES 423 423 Phosphoserine.
FT MOD_RES 438 438 Phosphoserine.
FT MOD_RES 442 442 Phosphoserine.
FT MOD_RES 451 451 Phosphoserine.
FT MOD_RES 483 483 Dimethylated arginine.
FT MOD_RES 528 528 Asymmetric dimethylarginine.
FT MOD_RES 535 535 Asymmetric dimethylarginine.
FT MOD_RES 554 554 Phosphoserine.
FT MOD_RES 570 570 Asymmetric dimethylarginine.
FT VAR_SEQ 60 62 Missing (in isoform Short).
FT /FTId=VSP_005806.
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
//
MIM
601574
*RECORD*
*FIELD* NO
601574
*FIELD* TI
*601574 TAF15 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR,
68-KD; TAF15
read more;;TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR 2N; TAF2N;;
TBP-ASSOCIATED FACTOR, RNA POLYMERASE II, 68-KD;;
RNA-BINDING PROTEIN 56; RBP56
RBP56/NR4A3 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
The EWS gene (EWSR1; 133450) was found at the chromosome breakpoints in
Ewing sarcoma (612219) and maps to chromosome 22; the FUS/TLS gene
(137070) was found at the breakpoints of myxoid liposarcoma and acute
myeloid leukemia and maps to chromosome 16. These genes encode proteins
that carry a highly homologous RNA binding domain. Fusion proteins made
between the N-terminal half of either gene and transcriptional
regulatory proteins, also derived from genes located at breakpoints,
appear to be involved in the pathogenesis of tumors. By PCR
amplification of human Namalwa cell cDNA using degenerate primers made
from the conserved amino acid sequences in the RNA binding domain of EWS
and FUS/TLS, Morohoshi et al. (1996) obtained a cDNA fragment,
designated RBP56. This fragment was predicted to encode an amino acid
sequence similar but not identical to those of EWS and FUS/TLS. Using
this fragment as a probe, they obtained 2 isoforms of cDNAs consisting
of 2,144 and 2,153 bp, respectively, which encoded proteins consisting
of 589 and 592 amino acid residues, respectively. The expression of
RBP56 mRNA was observed in all human fetal and adult tissues examined,
as was the expression of EWS and FUS/TLS mRNAs.
GENE STRUCTURE
By genomic sequence analysis, Morohoshi et al. (1998) determined that
the RBP56 gene spans about 37 kb and contains 16 exons ranging in size
from 33 bp to 562 bp. The longest, exon 15, encodes a C-terminal region
with 19 repeats. The authors noted that the conservation of the overall
exon number and structure of RBP56, FUS/TLS, and EWS indicates that they
probably originated from the same ancestor gene.
MAPPING
Morohoshi et al. (1996) mapped the TAF15 (RBP56) gene to chromosome 17
by Southern blot analysis of mouse/human somatic cell hybrids and
localized it to 17q11.2-q12 by FISH. By PCR analysis using genomic DNA
from human/rodent somatic cell hybrid panels harboring part of human
chromosome 17, they further localized the gene to 17q11.1-q11.2.
CYTOGENETICS
- RBP56/NR4A3 Fusion Gene
Although most extraskeletal myxoid chondrosarcomas (EMC; 612237) are
characterized by the translocation t(9;22)(q22;q12), another subset
carries a t(9;17)(q22;q11). The t(9;22) is known to result in fusion of
the EWS gene on 22q12 with the NR4A3 gene (600542) on 9q11, creating a
chimeric EWS/NR4A3 gene. Panagopoulos et al. (1999) examined 2
extraskeletal myxoid chondrosarcomas with t(9;17)(q22;q11) and found
that the NR4A3 gene, which they designated CHN, was combined with the
RBP56 gene from 17q11 to generate a chimeric RBP56/NR4A3 gene. RBP56 had
not previously been implicated in tumorigenesis, but it encodes a
putative RNA-binding protein similar to the EWS and FUS genes known to
play a pathogenetic role in sarcomas. The presence of the RBP56/NR4A3
chimeric gene in extraskeletal myxoid chondrosarcomas showed that the
N-terminal parts of EWS and RBP56 have similar oncogenic potential,
making them pathogenetically equivalent in oncoproteins arising from
fusions with certain transcription factors.
*FIELD* RF
1. Morohoshi, F.; Arai, K.; Takahashi, E.; Tanigami, A.; Ohki, M.
: Cloning and mapping of a human RBP56 gene encoding a putative RNA
binding protein similar to FUS/TLS and EWS proteins. Genomics 38:
51-57, 1996.
2. Morohoshi, F.; Ootsuka, Y.; Arai, K.; Ichikawa, H.; Mitani, S.;
Munakata, N.; Ohki, M.: Genomic structure of the human RBP56/hTAF(II)68
and FUS/TLS genes. Gene 221: 191-198, 1998.
3. Panagopoulos, I.; Mencinger, M.; Dietrich, C. U.; Bjerkehagan,
B.; Saeter, G.; Mertens, F.; Mandahl, N.; Heim, S.: Fusion of the
RBP56 and CHN genes in extraskeletal myxoid chondrosarcomas with translocation
t(9;17)(q22;q11). Oncogene 18: 7594-7598, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/14/2008
Paul J. Converse - updated: 7/14/2000
Victor A. McKusick - updated: 1/24/2000
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
carol: 08/20/2008
ckniffin: 8/14/2008
carol: 8/5/2008
carol: 12/21/2001
joanna: 12/5/2001
mgross: 7/14/2000
carol: 1/30/2000
terry: 1/24/2000
alopez: 3/9/1999
mark: 2/11/1998
terry: 2/4/1998
jenny: 12/20/1996
mark: 12/16/1996
*RECORD*
*FIELD* NO
601574
*FIELD* TI
*601574 TAF15 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR,
68-KD; TAF15
read more;;TATA BOX-BINDING PROTEIN-ASSOCIATED FACTOR 2N; TAF2N;;
TBP-ASSOCIATED FACTOR, RNA POLYMERASE II, 68-KD;;
RNA-BINDING PROTEIN 56; RBP56
RBP56/NR4A3 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
The EWS gene (EWSR1; 133450) was found at the chromosome breakpoints in
Ewing sarcoma (612219) and maps to chromosome 22; the FUS/TLS gene
(137070) was found at the breakpoints of myxoid liposarcoma and acute
myeloid leukemia and maps to chromosome 16. These genes encode proteins
that carry a highly homologous RNA binding domain. Fusion proteins made
between the N-terminal half of either gene and transcriptional
regulatory proteins, also derived from genes located at breakpoints,
appear to be involved in the pathogenesis of tumors. By PCR
amplification of human Namalwa cell cDNA using degenerate primers made
from the conserved amino acid sequences in the RNA binding domain of EWS
and FUS/TLS, Morohoshi et al. (1996) obtained a cDNA fragment,
designated RBP56. This fragment was predicted to encode an amino acid
sequence similar but not identical to those of EWS and FUS/TLS. Using
this fragment as a probe, they obtained 2 isoforms of cDNAs consisting
of 2,144 and 2,153 bp, respectively, which encoded proteins consisting
of 589 and 592 amino acid residues, respectively. The expression of
RBP56 mRNA was observed in all human fetal and adult tissues examined,
as was the expression of EWS and FUS/TLS mRNAs.
GENE STRUCTURE
By genomic sequence analysis, Morohoshi et al. (1998) determined that
the RBP56 gene spans about 37 kb and contains 16 exons ranging in size
from 33 bp to 562 bp. The longest, exon 15, encodes a C-terminal region
with 19 repeats. The authors noted that the conservation of the overall
exon number and structure of RBP56, FUS/TLS, and EWS indicates that they
probably originated from the same ancestor gene.
MAPPING
Morohoshi et al. (1996) mapped the TAF15 (RBP56) gene to chromosome 17
by Southern blot analysis of mouse/human somatic cell hybrids and
localized it to 17q11.2-q12 by FISH. By PCR analysis using genomic DNA
from human/rodent somatic cell hybrid panels harboring part of human
chromosome 17, they further localized the gene to 17q11.1-q11.2.
CYTOGENETICS
- RBP56/NR4A3 Fusion Gene
Although most extraskeletal myxoid chondrosarcomas (EMC; 612237) are
characterized by the translocation t(9;22)(q22;q12), another subset
carries a t(9;17)(q22;q11). The t(9;22) is known to result in fusion of
the EWS gene on 22q12 with the NR4A3 gene (600542) on 9q11, creating a
chimeric EWS/NR4A3 gene. Panagopoulos et al. (1999) examined 2
extraskeletal myxoid chondrosarcomas with t(9;17)(q22;q11) and found
that the NR4A3 gene, which they designated CHN, was combined with the
RBP56 gene from 17q11 to generate a chimeric RBP56/NR4A3 gene. RBP56 had
not previously been implicated in tumorigenesis, but it encodes a
putative RNA-binding protein similar to the EWS and FUS genes known to
play a pathogenetic role in sarcomas. The presence of the RBP56/NR4A3
chimeric gene in extraskeletal myxoid chondrosarcomas showed that the
N-terminal parts of EWS and RBP56 have similar oncogenic potential,
making them pathogenetically equivalent in oncoproteins arising from
fusions with certain transcription factors.
*FIELD* RF
1. Morohoshi, F.; Arai, K.; Takahashi, E.; Tanigami, A.; Ohki, M.
: Cloning and mapping of a human RBP56 gene encoding a putative RNA
binding protein similar to FUS/TLS and EWS proteins. Genomics 38:
51-57, 1996.
2. Morohoshi, F.; Ootsuka, Y.; Arai, K.; Ichikawa, H.; Mitani, S.;
Munakata, N.; Ohki, M.: Genomic structure of the human RBP56/hTAF(II)68
and FUS/TLS genes. Gene 221: 191-198, 1998.
3. Panagopoulos, I.; Mencinger, M.; Dietrich, C. U.; Bjerkehagan,
B.; Saeter, G.; Mertens, F.; Mandahl, N.; Heim, S.: Fusion of the
RBP56 and CHN genes in extraskeletal myxoid chondrosarcomas with translocation
t(9;17)(q22;q11). Oncogene 18: 7594-7598, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/14/2008
Paul J. Converse - updated: 7/14/2000
Victor A. McKusick - updated: 1/24/2000
*FIELD* CD
Victor A. McKusick: 12/13/1996
*FIELD* ED
carol: 08/20/2008
ckniffin: 8/14/2008
carol: 8/5/2008
carol: 12/21/2001
joanna: 12/5/2001
mgross: 7/14/2000
carol: 1/30/2000
terry: 1/24/2000
alopez: 3/9/1999
mark: 2/11/1998
terry: 2/4/1998
jenny: 12/20/1996
mark: 12/16/1996