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Transcription initiation factor TFIID subunit 6 (RNA polymerase II TBP-associated factor subunit E) (Transcription initiation factor TFIID 70 kDa subunit) (TAF(II)70) (TAFII-70) (TAFII70) (Transcription initiation factor TFIID 80 kDa subunit) (TAF(II)80) (TAFII-80) (TAFII80)

 TAF6_HUMAN              Reviewed;         677 AA.
P49848; A4D2B2; A4D2B3; B4DT11; D6W5U2; Q6AI29;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 183.
RecName: Full=Transcription initiation factor TFIID subunit 6;
AltName: Full=RNA polymerase II TBP-associated factor subunit E;
AltName: Full=Transcription initiation factor TFIID 70 kDa subunit;
Short=TAF(II)70;
Short=TAFII-70;
Short=TAFII70;
AltName: Full=Transcription initiation factor TFIID 80 kDa subunit;
Short=TAF(II)80;
Short=TAFII-80;
Short=TAFII80;
Name=TAF6; Synonyms=TAF2E, TAFII70;
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 1 AND 2), PROTEIN SEQUENCE OF
78-95 AND 501-521, AND INTERACTION WITH TBP AND TAF1.
TISSUE=Cervix carcinoma;
PubMed=8262073;
Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.;
"Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal
conserved interactions with other subunits of TFIID.";
EMBO J. 12:5303-5309(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 78-103;
113-127; 368-383 AND 441-455, AND INTERACTION WITH TBP; TAF1; TAF9;
TAF12; GTF2F1 AND GTF2E1.
TISSUE=Placenta;
PubMed=7667268; DOI=10.1073/pnas.92.18.8195;
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M.,
Nakatani Y., Roeder R.G.;
"Evolutionary conservation of human TATA-binding-polypeptide-
associated factors TAFII31 and TAFII80 and interactions of TAFII80
with other TAFs and with general transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain cortex;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-36.
NIEHS SNPs program;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[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 1).
TISSUE=Pancreas;
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]
IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12601814; DOI=10.1002/pmic.200390030;
Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
"Novel subunits of the TATA binding protein free TAFII-containing
transcription complex identified by matrix-assisted laser
desorption/ionization-time of flight mass spectrometry following one-
dimensional gel electrophoresis.";
Proteomics 3:217-223(2003).
[10]
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).
[11]
INTERACTION WITH TAF9 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B,
AND DNA-BINDING.
PubMed=15601843; DOI=10.1128/MCB.25.1.206-219.2005;
Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S.,
Unger T., Dikstein R.;
"Core promoter binding by histone-like TAF complexes.";
Mol. Cell. Biol. 25:206-219(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND THR-660, 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]
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).
[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 THR-120; SER-634; SER-636;
SER-653 AND THR-660, 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-653 AND THR-660, 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]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-524, 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).
[21]
INVOLVEMENT IN ALYUS, AND VARIANT ALYUS THR-71.
PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y.,
Sogaty S., Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F.,
Alshahwan S.A., Seidahmed M.Z., Alhadid A.A., Aldhalaan H.,
AlQallaf F., Kurdi W., Alfadhel M., Babay Z., Alsogheer M., Kaya N.,
Al-Hassnan Z.N., Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F.,
El Khashab H.Y., Bohlega S., Jia X., Nguyen H.C., Hammami R., Adly N.,
Mohamed J.Y., Abdulwahab F., Ibrahim N., Naim E.A., Al-Younes B.,
Meyer B.F., Hashem M., Shaheen R., Xiong Y., Abouelhoda M.,
Aldeeri A.A., Monies D.M., Alkuraya F.S.;
"Accelerating novel candidate gene discovery in neurogenetic disorders
via whole-exome sequencing of prescreened multiplex consanguineous
families.";
Cell Rep. 10:148-161(2015).
[22]
INVOLVEMENT IN ALYUS, VARIANTS ALYUS CYS-46 AND THR-71, AND
CHARACTERIZATION OF VARIANTS ALYUS CYS-46 AND THR-71.
PubMed=25574841; DOI=10.1172/JCI77435;
Yuan B., Pehlivan D., Karaca E., Patel N., Charng W.L., Gambin T.,
Gonzaga-Jauregui C., Sutton V.R., Yesil G., Bozdogan S.T., Tos T.,
Koparir A., Koparir E., Beck C.R., Gu S., Aslan H., Yuregir O.O.,
Al Rubeaan K., Alnaqeb D., Alshammari M.J., Bayram Y., Atik M.M.,
Aydin H., Geckinli B.B., Seven M., Ulucan H., Fenercioglu E., Ozen M.,
Jhangiani S., Muzny D.M., Boerwinkle E., Tuysuz B., Alkuraya F.S.,
Gibbs R.A., Lupski J.R.;
"Global transcriptional disturbances underlie Cornelia de Lange
syndrome and related phenotypes.";
J. Clin. Invest. 125:636-651(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-196, 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: TAFs are components of the transcription factor IID
(TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII
complex (TFTC). TIIFD is multimeric protein complex that plays a
central role in mediating promoter responses to various activators
and repressors.
-!- SUBUNIT: TFIID and PCAF are composed of TATA binding protein (TBP)
and a number of TBP-associated factors (TAFs). TBP is not part of
TFTC. Interacts directly with TBP, TAF1/TAFII250, TAF9/TAFII31 AND
TAF12/TAFII20. The TAF6/TAFII70-TAF9/TAFII31 heterodimer forms an
octamer complex with the TAF4B/TFII105-TAF12/TFIID20 heterodimer.
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. Also interacts with the GTFs, TFIIEalpha/GTF2E1
and TFIIFalpha/GTF2F1. Component of the TFTC-HAT complex.
{ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:15601843,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:7667268,
ECO:0000269|PubMed:8262073}.
-!- INTERACTION:
Q1K9H5:PB1 (xeno); NbExp=2; IntAct=EBI-1560206, EBI-6050669;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=P49848-1; Sequence=Displayed;
Name=2; Synonyms=Gamma;
IsoId=P49848-2; Sequence=VSP_037476;
Name=3;
IsoId=P49848-3; Sequence=VSP_043709;
Note=No experimental confirmation available.;
-!- DISEASE: Alazami-Yuan syndrome (ALYUS) [MIM:617126]: An autosomal
recessive syndrome reminiscent of Cornelia de Lange syndrome and
characterized by delayed psychomotor development with intellectual
disability, hypotonia, microcephaly, short stature, poor speech,
and dysmorphic features. {ECO:0000269|PubMed:25558065,
ECO:0000269|PubMed:25574841}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/taf6/";
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EMBL; L25444; AAA63643.1; -; mRNA.
EMBL; U31659; AAA84390.1; -; mRNA.
EMBL; AK300005; BAG61823.1; -; mRNA.
EMBL; CR627390; CAH10485.1; -; mRNA.
EMBL; AY149894; AAN10295.1; -; Genomic_DNA.
EMBL; CH236956; EAL23851.1; -; Genomic_DNA.
EMBL; CH236956; EAL23852.1; -; Genomic_DNA.
EMBL; CH471091; EAW76589.1; -; Genomic_DNA.
EMBL; CH471091; EAW76591.1; -; Genomic_DNA.
EMBL; CH471091; EAW76592.1; -; Genomic_DNA.
EMBL; BC018115; AAH18115.1; -; mRNA.
CCDS; CCDS55135.1; -. [P49848-3]
CCDS; CCDS5686.1; -. [P49848-1]
RefSeq; NP_001177344.1; NM_001190415.1. [P49848-3]
RefSeq; NP_005632.1; NM_005641.3. [P49848-1]
RefSeq; NP_647476.1; NM_139315.2. [P49848-1]
RefSeq; XP_006716163.1; XM_006716100.2. [P49848-1]
UniGene; Hs.489309; -.
PDB; 5FUR; EM; 8.50 A; J/K=1-677.
PDBsum; 5FUR; -.
ProteinModelPortal; P49848; -.
SMR; P49848; -.
BioGrid; 112741; 66.
CORUM; P49848; -.
DIP; DIP-773N; -.
IntAct; P49848; 25.
MINT; P49848; -.
STRING; 9606.ENSP00000399982; -.
iPTMnet; P49848; -.
PhosphoSitePlus; P49848; -.
BioMuta; TAF6; -.
DMDM; 1729810; -.
EPD; P49848; -.
MaxQB; P49848; -.
PaxDb; P49848; -.
PeptideAtlas; P49848; -.
PRIDE; P49848; -.
DNASU; 6878; -.
Ensembl; ENST00000344095; ENSP00000344537; ENSG00000106290. [P49848-1]
Ensembl; ENST00000437822; ENSP00000399982; ENSG00000106290. [P49848-3]
Ensembl; ENST00000452041; ENSP00000416396; ENSG00000106290. [P49848-1]
Ensembl; ENST00000453269; ENSP00000389575; ENSG00000106290. [P49848-1]
GeneID; 6878; -.
KEGG; hsa:6878; -.
UCSC; uc003uti.4; human. [P49848-1]
CTD; 6878; -.
DisGeNET; 6878; -.
EuPathDB; HostDB:ENSG00000106290.14; -.
GeneCards; TAF6; -.
HGNC; HGNC:11540; TAF6.
HPA; HPA006566; -.
MalaCards; TAF6; -.
MIM; 602955; gene.
MIM; 617126; phenotype.
neXtProt; NX_P49848; -.
OpenTargets; ENSG00000106290; -.
PharmGKB; PA36315; -.
eggNOG; KOG2549; Eukaryota.
eggNOG; COG5095; LUCA.
GeneTree; ENSGT00640000091486; -.
HOGENOM; HOG000253001; -.
HOVERGEN; HBG012489; -.
InParanoid; P49848; -.
KO; K03131; -.
PhylomeDB; P49848; -.
TreeFam; TF313632; -.
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-6807505; RNA polymerase II transcribes snRNA genes.
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.
ChiTaRS; TAF6; human.
GeneWiki; TAF6; -.
GenomeRNAi; 6878; -.
PRO; PR:P49848; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106290; -.
CleanEx; HS_TAF6; -.
ExpressionAtlas; P49848; baseline and differential.
Genevisible; P49848; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
GO; GO:0000124; C:SAGA complex; IEA:InterPro.
GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; IEA:InterPro.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR009072; Histone-fold.
InterPro; IPR037796; TAF6.
InterPro; IPR011442; TAF6_C.
InterPro; IPR004823; TAF_TATA-bd.
PANTHER; PTHR10221; PTHR10221; 1.
Pfam; PF02969; TAF; 1.
Pfam; PF07571; TAF6_C; 1.
SMART; SM00803; TAF; 1.
SUPFAM; SSF47113; SSF47113; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Isopeptide bond;
Mental retardation; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 677 Transcription initiation factor TFIID
subunit 6.
/FTId=PRO_0000118873.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 248 248 Phosphothreonine.
{ECO:0000250|UniProtKB:Q63801}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q63801}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000250|UniProtKB:Q63801}.
MOD_RES 524 524 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000250|UniProtKB:Q62311}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 660 660 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 196 196 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MTKRRLQTITACLQLREGSPSLHRGLHPSREEKRDS
RM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043709.
VAR_SEQ 477 486 Missing (in isoform 2).
{ECO:0000303|PubMed:8262073}.
/FTId=VSP_037476.
VARIANT 36 36 C -> S (in dbSNP:rs4134897).
{ECO:0000269|Ref.5}.
/FTId=VAR_014349.
VARIANT 46 46 R -> C (in ALYUS; decreased interaction
with TAF1 and TBP shown by functional
expression studies in a Drosophila cell
line; dbSNP:rs727503778).
{ECO:0000269|PubMed:25574841}.
/FTId=VAR_077840.
VARIANT 71 71 I -> T (in ALYUS; decreased interaction
with TAF1, TAF9 and TBP shown by
functional expression studies in a
Drosophila cell line; dbSNP:rs374993554).
{ECO:0000269|PubMed:25558065,
ECO:0000269|PubMed:25574841}.
/FTId=VAR_077841.
CONFLICT 196 196 K -> E (in Ref. 4; CAH10485).
{ECO:0000305}.
CONFLICT 417 417 R -> W (in Ref. 4; CAH10485).
{ECO:0000305}.
SEQUENCE 677 AA; 72668 MW; 06C6BFA563580823 CRC64;
MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM
GKRQKLTTSD IDYALKLKNV EPLYGFHAQE FIPFRFASGG GRELYFYEEK EVDLSDIINT
PLPRVPLDVC LKAHWLSIEG CQPAIPENPP PAPKEQQKAE ATEPLKSAKP GQEEDGPLKG
KGQGATTADG KGKEKKAPPL LEGAPLRLKP RSIHELSVEQ QLYYKEITEA CVGSCEAKRA
EALQSIATDP GLYQMLPRFS TFISEGVRVN VVQNNLALLI YLMRMVKALM DNPTLYLEKY
VHELIPAVMT CIVSRQLCLR PDVDNHWALR DFAARLVAQI CKHFSTTTNN IQSRITKTFT
KSWVDEKTPW TTRYGSIAGL AELGHDVIKT LILPRLQQEG ERIRSVLDGP VLSNIDRIGA
DHVQSLLLKH CAPVLAKLRP PPDNQDAYRA EFGSLGPLLC SQVVKARAQA ALQAQQVNRT
TLTITQPRPT LTLSQAPQPG PRTPGLLKVP GSIALPVQTL VSARAAAPPQ PSPPPTKFIV
MSSSSSAPST QQVLSLSTSA PGSGSTTTSP VTTTVPSVQP IVKLVSTATT APPSTAPSGP
GSVQKYIVVS LPPTGEGKGG PTSHPSPVPP PASSPSPLSG SALCGGKQEA GDSPPPAPGT
PKANGSQPNS GSPQPAP


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