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Transcription initiation factor TFIID subunit 7 (RNA polymerase II TBP-associated factor subunit F) (Transcription initiation factor TFIID 55 kDa subunit) (TAF(II)55) (TAFII-55) (TAFII55)

 TAF7_HUMAN              Reviewed;         349 AA.
Q15545; B2RBV9; Q13036;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Transcription initiation factor TFIID subunit 7;
AltName: Full=RNA polymerase II TBP-associated factor subunit F;
AltName: Full=Transcription initiation factor TFIID 55 kDa subunit;
Short=TAF(II)55;
Short=TAFII-55;
Short=TAFII55 {ECO:0000303|PubMed:11340078, ECO:0000303|PubMed:7824954, ECO:0000303|PubMed:8702684};
Name=TAF7; Synonyms=TAF2F, TAFII55;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=8702684; DOI=10.1074/jbc.271.33.19774;
Lavigne A.C., Mengus G., May M., Dubrowskaya V., Tora L., Davidson I.;
"Multiple interactions between hTAFII55 and other TFIID subunits.
Requirements for the formation of stable ternary complexes between
hTAFII55 and the TATA-binding protein.";
J. Biol. Chem. 271:19774-19780(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=7824954; DOI=10.1126/science.7824954;
Chiang C.-M., Roeder R.G.;
"Cloning of an intrinsic human TFIID subunit that interacts with
multiple transcriptional activators.";
Science 267:531-536(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11340078; DOI=10.1074/jbc.M102875200;
Zhou T., Chiang C.-M.;
"The intronless and TATA-less human TAFII55 gene contains a functional
initiator and a downstream promoter element.";
J. Biol. Chem. 276:25503-25511(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[7]
FUNCTION, AND SUBUNIT.
PubMed=10438527; DOI=10.1074/jbc.274.33.23480;
Wu S.Y., Thomas M.C., Hou S.Y., Likhite V., Chiang C.M.;
"Isolation of mouse TFIID and functional characterization of TBP and
TFIID in mediating estrogen receptor and chromatin transcription.";
J. Biol. Chem. 274:23480-23490(1999).
[8]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
MOTIF, AND MUTAGENESIS OF LYS-5.
PubMed=16415881; DOI=10.1038/nsmb1045;
Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
"Structural basis for the methylation site specificity of SET7/9.";
Nat. Struct. Mol. Biol. 13:140-146(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, AND
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, 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).
[16]
INTERACTION WITH TAF1, MISCELLANEOUS, PHOSPHORYLATION AT SER-264, AND
MUTAGENESIS OF SER-264.
PubMed=22711989; DOI=10.1128/MCB.00416-12;
Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.;
"Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene
transcription by TFIID subunits TAF1 and TAF7.";
Mol. Cell. Biol. 32:3358-3369(2012).
[17]
PHOSPHORYLATION BY CIITA.
PubMed=24036077; DOI=10.1016/j.bbagrm.2013.09.001;
Soe K.C., Devaiah B.N., Singer D.S.;
"Transcriptional coactivator CIITA, a functional homolog of TAF1, has
kinase activity.";
Biochim. Biophys. Acta 1829:1184-1190(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-200; SER-201;
SER-213 AND SER-264, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-264, 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).
[20]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TAF1.
PubMed=25412659; DOI=10.1038/cr.2014.148;
Wang H., Curran E.C., Hinds T.R., Wang E.H., Zheng N.;
"Crystal structure of a TAF1-TAF7 complex in human transcription
factor IID reveals a promoter binding module.";
Cell Res. 24:1433-1444(2014).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), AND SUBUNIT.
PubMed=27007846; DOI=10.1038/nature17394;
Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
"Structure of promoter-bound TFIID and model of human pre-initiation
complex assembly.";
Nature 531:604-609(2016).
-!- FUNCTION: Functions as a component of the DNA-binding general
transcription factor complex TFIID, a multimeric protein complex
that plays a central role in mediating promoter responses to
various activators and repressors. Present in both of the
previously described TFIID species which either lack or contain
TAFII30 (TFIID alpha and TFIID beta respectively).
{ECO:0000269|PubMed:10438527}.
-!- SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a
number of TBP-associated factors (TAFs) (PubMed:27007846,
PubMed:10438527). Part of a TFIID-containing RNA polymerase II
pre-initiation complex that is composed of TBP and at least
GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4,
GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5,
TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13
(PubMed:27007846). Interacts with TAF1; the interaction is direct
(PubMed:25412659). Interacts with TAFII250, TAFII100, TAFII28,
TAFII20, and TAFII18, but not with TAFII30 or TBP (PubMed:8702684,
PubMed:10438527). Component of some MLL1/MLL complex, at least
composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1,
WDR5 and RBBP5, as well as the facultative components BAP18, CHD8,
E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF,
PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3,
TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). Binds to
CIITA and TAF1 and inhibits their acetyltransferase activity,
thereby repressing activated transcription and behaving as a
repressor at these promoters. {ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:22711989, ECO:0000269|PubMed:25412659,
ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:7824954,
ECO:0000269|PubMed:8702684}.
-!- INTERACTION:
Q80UV9-1:Taf1 (xeno); NbExp=2; IntAct=EBI-1560194, EBI-15563115;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9R1C0}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the
SETD7 methyltransferase, which methylates Lys-5 in vitro.
{ECO:0000250}.
-!- PTM: Phosphorylated by CIITA. Phosphorylation at Ser-264 by TAF1
in early G1 phase disrupts binding to TAF1.
{ECO:0000269|PubMed:22711989, ECO:0000269|PubMed:24036077}.
-!- MISCELLANEOUS: Overexpression of TAF7 in HeLa cells inhibits
cyclin D1 and cyclin A gene transcription and causes the cells to
accumulate in early S phase. In contrast, depletion of TAF7 from
TFIID complexes by siRNAs increases histone H3 acetylation at both
cyclin promoters and stimulates cyclins CCND1 and CCNA gene
transcription.
-!- SIMILARITY: Belongs to the TAF7 family. {ECO:0000305}.
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EMBL; X97999; CAA66636.1; -; mRNA.
EMBL; U18062; AAB60347.1; -; mRNA.
EMBL; AF349038; AAK30585.1; -; Genomic_DNA.
EMBL; AK314837; BAG37356.1; -; mRNA.
EMBL; CH471062; EAW61966.1; -; Genomic_DNA.
EMBL; BC032737; AAH32737.1; -; mRNA.
CCDS; CCDS4259.1; -.
PIR; I38904; I38904.
RefSeq; NP_005633.2; NM_005642.2.
UniGene; Hs.438838; -.
PDB; 4RGW; X-ray; 2.30 A; B=1-349.
PDB; 5FUR; EM; 8.50 A; H=1-349.
PDBsum; 4RGW; -.
PDBsum; 5FUR; -.
ProteinModelPortal; Q15545; -.
SMR; Q15545; -.
BioGrid; 112742; 45.
CORUM; Q15545; -.
DIP; DIP-29047N; -.
IntAct; Q15545; 19.
MINT; MINT-3031780; -.
STRING; 9606.ENSP00000312709; -.
iPTMnet; Q15545; -.
PhosphoSitePlus; Q15545; -.
BioMuta; TAF7; -.
DMDM; 3024690; -.
EPD; Q15545; -.
MaxQB; Q15545; -.
PaxDb; Q15545; -.
PeptideAtlas; Q15545; -.
PRIDE; Q15545; -.
DNASU; 6879; -.
Ensembl; ENST00000313368; ENSP00000312709; ENSG00000178913.
GeneID; 6879; -.
KEGG; hsa:6879; -.
UCSC; uc003ljg.4; human.
CTD; 6879; -.
EuPathDB; HostDB:ENSG00000178913.7; -.
GeneCards; TAF7; -.
HGNC; HGNC:11541; TAF7.
HPA; HPA006429; -.
MIM; 600573; gene.
neXtProt; NX_Q15545; -.
OpenTargets; ENSG00000178913; -.
PharmGKB; PA36316; -.
eggNOG; KOG4011; Eukaryota.
eggNOG; COG5414; LUCA.
GeneTree; ENSGT00390000010815; -.
HOGENOM; HOG000035121; -.
HOVERGEN; HBG013606; -.
InParanoid; Q15545; -.
KO; K03132; -.
OMA; CQMLVCT; -.
OrthoDB; EOG091G0S3N; -.
PhylomeDB; Q15545; -.
TreeFam; TF313044; -.
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.
SignaLink; Q15545; -.
ChiTaRS; TAF7; human.
GeneWiki; TAF7; -.
GenomeRNAi; 6879; -.
PRO; PR:Q15545; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000178913; -.
CleanEx; HS_TAF7; -.
ExpressionAtlas; Q15545; baseline and differential.
Genevisible; Q15545; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IPI:ParkinsonsUK-UCL.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; IPI:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0035067; P:negative regulation of histone acetylation; IDA:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0060260; P:regulation of transcription initiation from RNA polymerase II promoter; NAS:ParkinsonsUK-UCL.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
GO; GO:0000296; P:spermine transport; ISS:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
CDD; cd08047; TAF7; 1.
InterPro; IPR006751; TAFII55_prot_cons_reg.
Pfam; PF04658; TAFII55_N; 1.
SMART; SM01370; TAFII55_N; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 349 Transcription initiation factor TFIID
subunit 7.
/FTId=PRO_0000118881.
COILED 244 349 {ECO:0000255}.
MOTIF 3 5 [KR]-[STA]-K motif.
COMPBIAS 227 230 Poly-Ser.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:22711989}.
VARIANT 178 178 S -> R.
/FTId=VAR_005629.
MUTAGEN 5 5 K->R: Abolishes methylation in vitro.
{ECO:0000269|PubMed:16415881}.
MUTAGEN 264 264 S->A: Reduced H3 acetylation and
transcription at target promoters.
{ECO:0000269|PubMed:22711989}.
MUTAGEN 264 264 S->D: 50% reduction in TAF1-binding,
reduced incorporation of TAF7 into TFIID
complexes. {ECO:0000269|PubMed:22711989}.
CONFLICT 283 283 K -> N (in Ref. 2; AAB60347).
{ECO:0000305}.
STRAND 14 19 {ECO:0000244|PDB:4RGW}.
HELIX 22 34 {ECO:0000244|PDB:4RGW}.
HELIX 39 42 {ECO:0000244|PDB:4RGW}.
STRAND 43 47 {ECO:0000244|PDB:4RGW}.
STRAND 51 58 {ECO:0000244|PDB:4RGW}.
STRAND 61 101 {ECO:0000244|PDB:4RGW}.
HELIX 138 140 {ECO:0000244|PDB:4RGW}.
HELIX 143 146 {ECO:0000244|PDB:4RGW}.
SEQUENCE 349 AA; 40259 MW; 0AAFD3E33E3CCD6E CRC64;
MSKSKDDAPH ELESQFILRL PPEYASTVRR AVQSGHVNLK DRLTIELHPD GRHGIVRVDR
VPLASKLVDL PCVMESLKTI DKKTFYKTAD ICQMLVSTVD GDLYPPVEEP VASTDPKASK
KKDKDKEKKF IWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR
WEIIAEDETK EAENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEDETQHQD
EEDINIIDTE EDLERQLQDK LNESDEQHQE NEGTNQLVMG IQKQIDNMKG KLQETQDRAK
RQEDLIMKVE NLALKNRFQA VLDELKQKED REKEQLSSLQ EELESLLEK


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