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TATA-binding protein-associated factor 2N (68 kDa TATA-binding protein-associated factor) (TAF(II)68) (TAFII68) (RNA-binding protein 56)

 RBP56_HUMAN             Reviewed;         592 AA.
Q92804; B2R837; Q86X94; Q92751;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-NOV-2018, entry version 193.
RecName: Full=TATA-binding protein-associated factor 2N;
AltName: Full=68 kDa TATA-binding protein-associated factor;
Short=TAF(II)68;
Short=TAFII68;
AltName: Full=RNA-binding protein 56;
Name=TAF15; Synonyms=RBP56, TAF2N;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
PubMed=8954779; DOI=10.1006/geno.1996.0591;
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND PROTEIN SEQUENCE OF
282-297 AND 307-320.
PubMed=8890175;
Bertolotti A., Lutz Y., Heard D.J., Chambon P., Tora L.;
"hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the
pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA
polymerase II.";
EMBO J. 15:5022-5031(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
PubMed=9795213; DOI=10.1016/S0378-1119(98)00463-6;
Morohoshi F., Ootsuka Y., Arai K., Ichikawa H., Mitani S.,
Munakata N., Ohki M.;
"Genomic structure of the human RBP56/hTAFII68 and FUS/TLS genes.";
Gene 221:191-198(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND LONG).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 75-101; 196-210; 284-306; 476-490 AND 563-576,
METHYLATION AT ARG-206; ARG-483 AND ARG-570, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[10]
INTERACTION WITH SF1.
PubMed=9660765; DOI=10.1074/jbc.273.29.18086;
Zhang D., Paley A.J., Childs G.;
"The transcriptional repressor ZFM1 interacts with and modulates the
ability of EWS to activate transcription.";
J. Biol. Chem. 273:18086-18091(1998).
[11]
CHROMOSOMAL TRANSLOCATION WITH NR4A3.
PubMed=10602519; DOI=10.1038/sj.onc.1203155;
Panagopoulos I., Mencinger M., Dietrich C.U., Bjerkehagen 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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
FUNCTION, METHYLATION AT ARG-206; ARG-528; ARG-535 AND ARG-570 BY
PRMT1, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=19124016; DOI=10.1016/j.yexcr.2008.12.008;
Jobert L., Argentini M., Tora L.;
"PRMT1 mediated methylation of TAF15 is required for its positive gene
regulatory function.";
Exp. Cell Res. 315:1273-1286(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-231, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-438; SER-442;
SER-451 AND SER-554, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-438, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
ADP-RIBOSYLATION.
PubMed=24055347; DOI=10.1016/j.molcel.2013.08.026;
Jungmichel S., Rosenthal F., Altmeyer M., Lukas J., Hottiger M.O.,
Nielsen M.L.;
"Proteome-wide identification of poly(ADP-Ribosyl)ation targets in
different genotoxic stress responses.";
Mol. Cell 52:272-285(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-206; ARG-431; ARG-459;
ARG-475 AND ARG-562, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-268, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: RNA and ssDNA-binding protein that may play specific
roles during transcription initiation at distinct promoters. Can
enter the preinitiation complex together with the RNA polymerase
II (Pol II). {ECO:0000269|PubMed:19124016}.
-!- SUBUNIT: Belongs to the RNA polymerase II (Pol II) transcriptional
multiprotein complex, together with the TATA-binding protein (TBP)
and other TBP-associated factors (TAF(II)s). Binds SF1.
-!- INTERACTION:
P35637:FUS; NbExp=5; IntAct=EBI-2255091, EBI-400434;
Q92993:KAT5; NbExp=2; IntAct=EBI-2255091, EBI-399080;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19124016}.
Cytoplasm {ECO:0000269|PubMed:19124016}. Note=Shuttles from the
nucleus to the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q92804-1; Sequence=Displayed;
Name=Short;
IsoId=Q92804-2; Sequence=VSP_005806;
-!- TISSUE SPECIFICITY: Ubiquitous. Observed in all fetal and adult
tissues.
-!- PTM: Dimethylated by PRMT1 at Arg-206 to asymmetric
dimethylarginine. The methylation may favor nuclear localization
and positive regulation of TAF15 transcriptional activity.
{ECO:0000269|PubMed:19124016, ECO:0000269|Ref.9}.
-!- PTM: ADP-ribosylated during genotoxic stress.
-!- DISEASE: Note=A chromosomal aberration involving TAF15/TAF2N is
found in a form of extraskeletal myxoid chondrosarcomas (EMC).
Translocation t(9;17)(q22;q11) with NR4A3.
{ECO:0000269|PubMed:10602519}.
-!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TAF2NID256.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/taf15/";
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EMBL; U51334; AAC50932.1; -; mRNA.
EMBL; X98893; CAA67398.1; -; mRNA.
EMBL; AB010067; BAA33811.1; -; Genomic_DNA.
EMBL; AB010067; BAA33812.1; -; Genomic_DNA.
EMBL; AY197697; AAO13485.1; -; Genomic_DNA.
EMBL; AK313223; BAG36034.1; -; mRNA.
EMBL; AK314194; BAG36873.1; -; mRNA.
EMBL; AC015849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471147; EAW80124.1; -; Genomic_DNA.
EMBL; CH471147; EAW80125.1; -; Genomic_DNA.
EMBL; BC046099; AAH46099.2; -; mRNA.
CCDS; CCDS32623.1; -. [Q92804-1]
CCDS; CCDS59279.1; -. [Q92804-2]
PIR; S71954; S71954.
RefSeq; NP_003478.1; NM_003487.3. [Q92804-2]
RefSeq; NP_631961.1; NM_139215.2. [Q92804-1]
UniGene; Hs.402752; -.
PDB; 2MMY; NMR; -; A=231-323.
PDBsum; 2MMY; -.
ProteinModelPortal; Q92804; -.
SMR; Q92804; -.
BioGrid; 113807; 141.
CORUM; Q92804; -.
DIP; DIP-52760N; -.
IntAct; Q92804; 37.
MINT; Q92804; -.
STRING; 9606.ENSP00000466950; -.
iPTMnet; Q92804; -.
PhosphoSitePlus; Q92804; -.
SwissPalm; Q92804; -.
BioMuta; TAF15; -.
DMDM; 8928305; -.
EPD; Q92804; -.
MaxQB; Q92804; -.
PaxDb; Q92804; -.
PeptideAtlas; Q92804; -.
PRIDE; Q92804; -.
ProteomicsDB; 75488; -.
ProteomicsDB; 75489; -. [Q92804-2]
DNASU; 8148; -.
Ensembl; ENST00000604841; ENSP00000474609; ENSG00000270647. [Q92804-2]
Ensembl; ENST00000605844; ENSP00000474096; ENSG00000270647. [Q92804-1]
Ensembl; ENST00000617382; ENSP00000480040; ENSG00000276833. [Q92804-1]
Ensembl; ENST00000631482; ENSP00000488684; ENSG00000276833. [Q92804-2]
GeneID; 8148; -.
KEGG; hsa:8148; -.
UCSC; uc002hkc.5; human. [Q92804-1]
CTD; 8148; -.
DisGeNET; 8148; -.
EuPathDB; HostDB:ENSG00000270647.5; -.
GeneCards; TAF15; -.
HGNC; HGNC:11547; TAF15.
HPA; HPA052059; -.
HPA; HPA063647; -.
MalaCards; TAF15; -.
MIM; 601574; gene.
neXtProt; NX_Q92804; -.
OpenTargets; ENSG00000270647; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
PharmGKB; PA36322; -.
eggNOG; ENOG410IP57; Eukaryota.
eggNOG; ENOG4111P4G; LUCA.
GeneTree; ENSGT00530000063105; -.
HOGENOM; HOG000038010; -.
HOVERGEN; HBG005755; -.
InParanoid; Q92804; -.
KO; K14651; -.
OMA; YGGMNDR; -.
OrthoDB; EOG091G0U8W; -.
PhylomeDB; Q92804; -.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNOR; Q92804; -.
ChiTaRS; TAF15; human.
GeneWiki; TAF15; -.
GenomeRNAi; 8148; -.
PMAP-CutDB; Q92804; -.
PRO; PR:Q92804; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000270647; Expressed in 230 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_TAF15; -.
ExpressionAtlas; Q92804; baseline and differential.
Genevisible; Q92804; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034875; TAF15.
InterPro; IPR034870; TET_fam.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
PANTHER; PTHR23238; PTHR23238; 2.
PANTHER; PTHR23238:SF25; PTHR23238:SF25; 2.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00641; zf-RanBP; 1.
SMART; SM00360; RRM; 1.
SMART; SM00547; ZnF_RBZ; 1.
SUPFAM; SSF54928; SSF54928; 1.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 592 TATA-binding protein-associated factor
2N.
/FTId=PRO_0000081749.
DOMAIN 234 320 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 407 413 1.
REPEAT 414 420 2.
REPEAT 421 429 3.
REPEAT 430 439 4.
REPEAT 440 448 5.
REPEAT 449 457 6.
REPEAT 458 465 7.
REPEAT 466 473 8.
REPEAT 474 481 9.
REPEAT 482 488 10.
REPEAT 489 496 11.
REPEAT 497 503 12.
REPEAT 504 510 13.
REPEAT 511 517 14.
REPEAT 518 524 15.
REPEAT 525 533 16.
REPEAT 534 543 17.
REPEAT 544 551 18.
REPEAT 552 560 19.
REPEAT 561 568 20.
REPEAT 569 575 21.
ZN_FING 354 385 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
REGION 407 575 21 X approximate tandem repeats of D-R-
[S,G](0,3)-G-G-Y-G-G.
COMPBIAS 1 208 Gln/Gly/Ser/Tyr-rich.
COMPBIAS 320 590 Arg/Gly-rich.
MOD_RES 206 206 Asymmetric dimethylarginine; by PRMT1;
alternate. {ECO:0000269|PubMed:19124016,
ECO:0000269|Ref.9}.
MOD_RES 206 206 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 268 268 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 431 431 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 442 442 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 459 459 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 475 475 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 483 483 Dimethylated arginine.
{ECO:0000269|Ref.9}.
MOD_RES 528 528 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19124016}.
MOD_RES 535 535 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19124016}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 562 562 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 570 570 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:19124016,
ECO:0000269|Ref.9}.
MOD_RES 570 570 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:19124016,
ECO:0000269|Ref.9}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 268 268 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 60 62 Missing (in isoform Short).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8890175,
ECO:0000303|PubMed:8954779}.
/FTId=VSP_005806.
STRAND 236 240 {ECO:0000244|PDB:2MMY}.
HELIX 250 255 {ECO:0000244|PDB:2MMY}.
TURN 264 266 {ECO:0000244|PDB:2MMY}.
STRAND 272 274 {ECO:0000244|PDB:2MMY}.
TURN 277 279 {ECO:0000244|PDB:2MMY}.
STRAND 285 288 {ECO:0000244|PDB:2MMY}.
HELIX 293 301 {ECO:0000244|PDB:2MMY}.
STRAND 304 308 {ECO:0000244|PDB:2MMY}.
STRAND 314 316 {ECO:0000244|PDB:2MMY}.
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


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