TAF10_HUMAN
ID TAF10_HUMAN Reviewed; 218 AA.
AC Q12962; O00703; Q13175; Q6FH13;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Transcription initiation factor TFIID subunit 10;
DE AltName: Full=STAF28;
DE AltName: Full=Transcription initiation factor TFIID 30 kDa subunit;
DE Short=TAF(II)30;
DE Short=TAFII-30;
DE Short=TAFII30;
GN Name=TAF10; Synonyms=TAF2A, TAF2H, TAFII30;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7923369; DOI=10.1016/0092-8674(94)90404-9;
RA Jacq X., Brou C., Lutz Y., Davidson I., Chambon P., Tora L.;
RT "Human TAFII30 is present in a distinct TFIID complex and is required for
RT transcriptional activation by the estrogen receptor.";
RL Cell 79:107-117(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8530084; DOI=10.1006/geno.1995.1243;
RA Scheer E., Mattei M.-G., Jacq X., Chambon P., Tora L.;
RT "Organization and chromosomal localization of the gene (TAF2H) encoding the
RT human TBP-associated factor II 30 (TAFII30).";
RL Genomics 29:269-272(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-92.
RG NIEHS SNPs program;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 43-67, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2;
RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J.,
RA Howard B.H., Qin J., Nakatani Y.;
RT "Histone-like TAFs within the PCAF histone acetylase complex.";
RL Cell 94:35-44(1998).
RN [8]
RP INTERACTION WITH TAF12.
RX PubMed=7729427; DOI=10.1002/j.1460-2075.1995.tb07138.x;
RA Mengus G., May M., Jacq X., Staub A., Tora L., Chambon P., Davidson I.;
RT "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three
RT subunits of the human transcription factor TFIID.";
RL EMBO J. 14:1520-1531(1995).
RN [9]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
RP GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF12 AND TAF9, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [10]
RP IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H;
RP TAF6L; TAF12; TRRAP AND TAF9.
RX PubMed=9885574; DOI=10.1016/s1097-2765(00)80301-9;
RA Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J.,
RA Nakatani Y.;
RT "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the
RT ATM superfamily.";
RL Mol. Cell 2:869-875(1998).
RN [11]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H;
RP TAF2; TAF4; TAF5; TRRAP; GCN5L2 AND TAF10.
RX PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA Brand M., Yamamoto K., Staub A., Tora L.;
RT "Identification of TATA-binding protein-free TAFII-containing complex
RT subunits suggests a role in nucleosome acetylation and signal
RT transduction.";
RL J. Biol. Chem. 274:18285-18289(1999).
RN [12]
RP INTERACTION WITH TAF3.
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [13]
RP METHYLATION AT LYS-189, AND MUTAGENESIS OF LYS-189.
RX PubMed=15099517; DOI=10.1016/s1097-2765(04)00182-0;
RA Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.;
RT "Gene-specific modulation of TAF10 function by SET9-mediated methylation.";
RL Mol. Cell 14:175-182(2004).
RN [14]
RP MOTIF, AND METHYLATION AT LYS-189.
RX PubMed=16415881; DOI=10.1038/nsmb1045;
RA Couture J.-F., Collazo E., Hauk G., Trievel R.C.;
RT "Structural basis for the methylation site specificity of SET7/9.";
RL Nat. Struct. Mol. Biol. 13:140-146(2006).
RN [15]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12601814; DOI=10.1002/pmic.200390030;
RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
RT "Novel subunits of the TATA binding protein free TAFII-containing
RT transcription complex identified by matrix-assisted laser
RT desorption/ionization-time of flight mass spectrometry following one-
RT dimensional gel electrophoresis.";
RL Proteomics 3:217-223(2003).
RN [16]
RP IDENTIFICATION IN STAGA COMPLEX.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP INTERACTION WITH LOXL2, SUBCELLULAR LOCATION, METHYLATION AT LYS-189,
RP ALLYSINE AT LYS-189, MUTAGENESIS OF LYS-189, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=25959397; DOI=10.1016/j.molcel.2015.04.012;
RA Iturbide A., Pascual-Reguant L., Fargas L., Cebria J.P., Alsina B.,
RA Garcia de Herreros A., Peiro S.;
RT "LOXL2 oxidizes methylated TAF10 and controls TFIID-dependent genes during
RT neural progenitor differentiation.";
RL Mol. Cell 58:755-766(2015).
RN [22] {ECO:0007744|PDB:4J7F}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 186-195.
RA Horowitz S., Dirk L.M.A., Yesselman J.D., Nimtz J.S., Del Rizzo P.A.,
RA Vander Meulen K.A., Butcher S.E., Mehl R.A., Houtz R.L., Al-Hashimi H.M.,
RA Trievel R.C.;
RT "Methyl CH O Hydrogen Bonds Orchestrate AdoMet-Dependent Methylation.";
RL Submitted (FEB-2013) to the PDB data bank.
RN [23] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGF}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.77 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE TFIID COMPLEX, AND SUBUNIT.
RX PubMed=33795473; DOI=10.1126/science.aba8490;
RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z.,
RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.;
RT "Structural insights into preinitiation complex assembly on core
RT promoters.";
RL Science 372:0-0(2021).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription (PubMed:33795473). TFIID recognizes and binds promoters
CC with or without a TATA box via its subunit TBP, a TATA-box-binding
CC protein, and promotes assembly of the pre-initiation complex (PIC)
CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF10 is
CC also component of the PCAF histone acetylase complex, the TATA-binding
CC protein-free TAF complex (TFTC) and the STAGA transcription
CC coactivator-HAT complex (PubMed:18206972, PubMed:11564863,
CC PubMed:9885574, PubMed:10373431, PubMed:12601814). May regulate cyclin
CC E expression (By similarity). {ECO:0000250|UniProtKB:Q8K0H5,
CC ECO:0000269|PubMed:10373431, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:18206972,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:9885574}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13
CC (PubMed:33795473). Component of the TATA-binding protein-free TAF
CC complex (TFTC), the PCAF histone acetylase complex and the STAGA
CC transcription coactivator-HAT complex (PubMed:11564863, PubMed:9885574,
CC PubMed:10373431, PubMed:12601814, PubMed:18206972). The PCAF complex
CC consists at least of TADA2L/ADA2, TADA3L/ADA3, SUPT3H, TAF5L TAF6L,
CC TAF9, TAF10, TAF12 and TRRAP (PubMed:9885574). The TFTC-HAT complex
CC consists at least of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5,
CC GCN5L2/GCN5, TAF10 and TRRAP (PubMed:10373431, PubMed:12601814). The
CC STAGA transcription coactivator-HAT complex consists at least of
CC SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12,
CC TRRAP and TAF9 (PubMed:11564863, PubMed:18206972). The STAGA core
CC complex is associated with a subcomplex required for histone
CC deubiquitination composed of ATXN7L3, ENY2 and USP22 (PubMed:18206972).
CC Interacts with TAF3 (PubMed:11438666). Interacts with LOXL2
CC (PubMed:25959397). Interacts with TAF12 isoform TAFII20; the
CC interaction is direct (PubMed:7729427). {ECO:0000269|PubMed:10373431,
CC ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:18206972,
CC ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:7729427, ECO:0000269|PubMed:9885574}.
CC -!- INTERACTION:
CC Q12962; O15265: ATXN7; NbExp=7; IntAct=EBI-708376, EBI-708350;
CC Q12962; Q8WTS6: SETD7; NbExp=4; IntAct=EBI-708376, EBI-1268586;
CC Q12962; Q7Z7C8-2: TAF8; NbExp=6; IntAct=EBI-708376, EBI-9089028;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:9674425}.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase. {ECO:0000269|PubMed:16415881}.
CC -!- PTM: Monomethylated at Lys-189 by SETD7, leading to increased affinity
CC for RNA polymerase II. {ECO:0000269|PubMed:15099517,
CC ECO:0000269|PubMed:16415881}.
CC -!- PTM: Lysine deamination at Lys-189 to form allysine is mediated by
CC LOXL2. Allysine formation by LOXL2 results in release of TAF10 from
CC promoters, leading to inhibition of TFIID-dependent transcription.
CC {ECO:0000269|PubMed:25959397}.
CC -!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf10/";
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DR EMBL; U13991; AAA62230.1; -; mRNA.
DR EMBL; U25816; AAB61242.1; -; Genomic_DNA.
DR EMBL; AF498312; AAM14627.1; -; Genomic_DNA.
DR EMBL; CR541943; CAG46741.1; -; mRNA.
DR EMBL; CH471064; EAW68687.1; -; Genomic_DNA.
DR EMBL; BC012088; AAH12088.1; -; mRNA.
DR CCDS; CCDS7769.1; -.
DR PIR; A57694; A57694.
DR RefSeq; NP_006275.1; NM_006284.3.
DR PDB; 2F69; X-ray; 1.30 A; B=186-195.
DR PDB; 3M53; X-ray; 1.85 A; B=186-195.
DR PDB; 3M54; X-ray; 1.60 A; B=186-195.
DR PDB; 3M55; X-ray; 1.55 A; B=186-195.
DR PDB; 3M56; X-ray; 1.65 A; B=186-195.
DR PDB; 3M57; X-ray; 1.70 A; B=186-195.
DR PDB; 3M58; X-ray; 1.40 A; B=186-195.
DR PDB; 3M59; X-ray; 1.70 A; B=186-195.
DR PDB; 3M5A; X-ray; 1.75 A; B=186-195.
DR PDB; 4J7F; X-ray; 1.59 A; B=186-195.
DR PDB; 4J7I; X-ray; 2.56 A; B=186-195.
DR PDB; 4J83; X-ray; 1.70 A; B=186-195.
DR PDB; 4J8O; X-ray; 1.63 A; B=186-195.
DR PDB; 4WV4; X-ray; 1.91 A; A=112-212.
DR PDB; 5EG2; X-ray; 1.55 A; B=186-195.
DR PDB; 6MZC; EM; 4.50 A; O=1-218.
DR PDB; 6MZD; EM; 9.80 A; N=1-218.
DR PDB; 6MZL; EM; 23.00 A; N/O=1-218.
DR PDB; 6MZM; EM; 7.50 A; O=1-218.
DR PDB; 7EDX; EM; 4.50 A; J/j=1-218.
DR PDB; 7EG7; EM; 6.20 A; J/j=1-218.
DR PDB; 7EG8; EM; 7.40 A; J/j=1-218.
DR PDB; 7EG9; EM; 3.70 A; J/j=1-218.
DR PDB; 7EGA; EM; 4.10 A; J/j=1-218.
DR PDB; 7EGB; EM; 3.30 A; J/j=1-218.
DR PDB; 7EGC; EM; 3.90 A; J/j=1-218.
DR PDB; 7EGD; EM; 6.75 A; J/j=1-218.
DR PDB; 7EGE; EM; 9.00 A; J/j=1-218.
DR PDB; 7EGF; EM; 3.16 A; j=1-218.
DR PDB; 7EGG; EM; 2.77 A; J=1-218.
DR PDB; 7EGI; EM; 9.82 A; J/j=1-218.
DR PDB; 7EGJ; EM; 8.64 A; J/j=1-218.
DR PDB; 7ENA; EM; 4.07 A; DJ/Dj=1-218.
DR PDB; 7ENC; EM; 4.13 A; DJ/Dj=1-218.
DR PDB; 7KTR; EM; 2.93 A; H=1-218.
DR PDB; 7KTS; EM; 19.09 A; H=1-218.
DR PDBsum; 2F69; -.
DR PDBsum; 3M53; -.
DR PDBsum; 3M54; -.
DR PDBsum; 3M55; -.
DR PDBsum; 3M56; -.
DR PDBsum; 3M57; -.
DR PDBsum; 3M58; -.
DR PDBsum; 3M59; -.
DR PDBsum; 3M5A; -.
DR PDBsum; 4J7F; -.
DR PDBsum; 4J7I; -.
DR PDBsum; 4J83; -.
DR PDBsum; 4J8O; -.
DR PDBsum; 4WV4; -.
DR PDBsum; 5EG2; -.
DR PDBsum; 6MZC; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 6MZM; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGE; -.
DR PDBsum; 7EGF; -.
DR PDBsum; 7EGG; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; Q12962; -.
DR SMR; Q12962; -.
DR BioGRID; 112744; 105.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; Q12962; -.
DR DIP; DIP-297N; -.
DR IntAct; Q12962; 33.
DR MINT; Q12962; -.
DR STRING; 9606.ENSP00000299424; -.
DR GlyGen; Q12962; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12962; -.
DR PhosphoSitePlus; Q12962; -.
DR BioMuta; TAF10; -.
DR DMDM; 3024688; -.
DR EPD; Q12962; -.
DR jPOST; Q12962; -.
DR MassIVE; Q12962; -.
DR MaxQB; Q12962; -.
DR PaxDb; Q12962; -.
DR PeptideAtlas; Q12962; -.
DR PRIDE; Q12962; -.
DR ProteomicsDB; 59056; -.
DR Antibodypedia; 1301; 151 antibodies from 27 providers.
DR DNASU; 6881; -.
DR Ensembl; ENST00000299424.9; ENSP00000299424.4; ENSG00000166337.11.
DR GeneID; 6881; -.
DR KEGG; hsa:6881; -.
DR MANE-Select; ENST00000299424.9; ENSP00000299424.4; NM_006284.4; NP_006275.1.
DR UCSC; uc001mej.3; human.
DR CTD; 6881; -.
DR DisGeNET; 6881; -.
DR GeneCards; TAF10; -.
DR HGNC; HGNC:11543; TAF10.
DR HPA; ENSG00000166337; Low tissue specificity.
DR MIM; 600475; gene.
DR neXtProt; NX_Q12962; -.
DR OpenTargets; ENSG00000166337; -.
DR PharmGKB; PA36318; -.
DR VEuPathDB; HostDB:ENSG00000166337; -.
DR eggNOG; KOG3423; Eukaryota.
DR GeneTree; ENSGT00390000009368; -.
DR HOGENOM; CLU_064104_1_0_1; -.
DR InParanoid; Q12962; -.
DR OMA; TGPMSCS; -.
DR OrthoDB; 1478962at2759; -.
DR PhylomeDB; Q12962; -.
DR TreeFam; TF313156; -.
DR PathwayCommons; Q12962; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SABIO-RK; Q12962; -.
DR SignaLink; Q12962; -.
DR SIGNOR; Q12962; -.
DR BioGRID-ORCS; 6881; 631 hits in 1081 CRISPR screens.
DR ChiTaRS; TAF10; human.
DR GeneWiki; TAF10; -.
DR GenomeRNAi; 6881; -.
DR Pharos; Q12962; Tbio.
DR PRO; PR:Q12962; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q12962; protein.
DR Bgee; ENSG00000166337; Expressed in right testis and 100 other tissues.
DR ExpressionAtlas; Q12962; baseline and differential.
DR Genevisible; Q12962; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:UniProtKB.
DR GO; GO:1905069; P:allantois development; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0048371; P:lateral mesodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051101; P:regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0036285; P:SAGA complex assembly; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IC:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd07982; TAF10; 1.
DR IDEAL; IID00465; -.
DR InterPro; IPR003923; TFIID_30kDa.
DR PANTHER; PTHR21242; PTHR21242; 1.
DR Pfam; PF03540; TFIID_30kDa; 1.
DR PIRSF; PIRSF017246; TFIID_TAF10; 1.
DR PRINTS; PR01443; TFIID30KDSUB.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..218
FT /note="Transcription initiation factor TFIID subunit 10"
FT /id="PRO_0000118897"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..189
FT /note="[KR]-[STA]-K motif"
FT /evidence="ECO:0000305|PubMed:16415881"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 189
FT /note="Allysine; alternate"
FT /evidence="ECO:0000269|PubMed:25959397"
FT MOD_RES 189
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15099517,
FT ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:25959397"
FT VARIANT 92
FT /note="I -> T (in dbSNP:rs3176311)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013706"
FT MUTAGEN 189
FT /note="K->Q: Abolishes methylation. Does not affect
FT interaction with LOXL2 but greatly reduces deamination by
FT LOXL2."
FT /evidence="ECO:0000269|PubMed:15099517,
FT ECO:0000269|PubMed:25959397"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 149..174
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:4WV4"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:7EGG"
SQ SEQUENCE 218 AA; 21711 MW; 032ED5CA97EBE411 CRC64;
MSCSGSGADP EAAPASAASA PGPAPPVSAP AALPSSTAAE NKASPAGTAG GPGAGAAAGG
TGPLAARAGE PAERRGAAPV SAGGAAPPEG AISNGVYVLP SAANGDVKPV VSSTPLVDFL
MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA
SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT
