TAF2_HUMAN
ID TAF2_HUMAN Reviewed; 1199 AA.
AC Q6P1X5; B2RE82; O43487; O43604; O60668; Q86WW7; Q8IWK4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcription initiation factor TFIID subunit 2;
DE AltName: Full=150 kDa cofactor of initiator function;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit B;
DE AltName: Full=TBP-associated factor 150 kDa;
DE AltName: Full=Transcription initiation factor TFIID 150 kDa subunit;
DE Short=TAF(II)150;
DE Short=TAFII-150;
DE Short=TAFII150;
GN Name=TAF2; Synonyms=CIF150, TAF2B;
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], VARIANT THR-447, FUNCTION, AND INTERACTION WITH
RP TAF2C1.
RX PubMed=9418870; DOI=10.1128/mcb.18.1.233;
RA Kaufmann J., Ahrens K., Koop R., Smale S.T., Muller R.;
RT "CIF150, a human cofactor for transcription factor IID-dependent initiator
RT function.";
RL Mol. Cell. Biol. 18:233-239(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-447, FUNCTION, SUBCELLULAR
RP LOCATION, IDENTIFICATION IN THE TFIID COMPLEX, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9774672; DOI=10.1128/mcb.18.11.6571;
RA Martinez E., Ge H., Tao Y., Yuan C.-X., Palhan V., Roeder R.G.;
RT "Novel cofactors and TFIIA mediate functional core promoter selectivity by
RT the human TAFII150-containing TFIID complex.";
RL Mol. Cell. Biol. 18:6571-6583(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-447.
RC TISSUE=Cervix carcinoma;
RA Guermah M., Roeder R.G.R.;
RT "Human TBP-associated factor (TAFII150).";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-604, AND VARIANT THR-447.
RC TISSUE=Duodenum, and Uterus;
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 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194; SER-1196 AND SER-1198,
RP AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-1188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1185 AND SER-1188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [11] {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:7EGH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 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).
RN [12]
RP VARIANT NEDFCF ARG-649.
RX PubMed=21937992; DOI=10.1038/nature10423;
RA Najmabadi H., Hu H., Garshasbi M., Zemojtel T., Abedini S.S., Chen W.,
RA Hosseini M., Behjati F., Haas S., Jamali P., Zecha A., Mohseni M.,
RA Puettmann L., Vahid L.N., Jensen C., Moheb L.A., Bienek M., Larti F.,
RA Mueller I., Weissmann R., Darvish H., Wrogemann K., Hadavi V.,
RA Lipkowitz B., Esmaeeli-Nieh S., Wieczorek D., Kariminejad R.,
RA Firouzabadi S.G., Cohen M., Fattahi Z., Rost I., Mojahedi F., Hertzberg C.,
RA Dehghan A., Rajab A., Banavandi M.J., Hoffer J., Falah M., Musante L.,
RA Kalscheuer V., Ullmann R., Kuss A.W., Tzschach A., Kahrizi K., Ropers H.H.;
RT "Deep sequencing reveals 50 novel genes for recessive cognitive
RT disorders.";
RL Nature 478:57-63(2011).
RN [13]
RP VARIANTS NEDFCF ARG-186 AND HIS-416.
RX PubMed=24084144; DOI=10.1016/j.pediatrneurol.2013.07.017;
RA Hellman-Aharony S., Smirin-Yosef P., Halevy A., Pasmanik-Chor M.,
RA Yeheskel A., Har-Zahav A., Maya I., Straussberg R., Dahary D., Haviv A.,
RA Shohat M., Basel-Vanagaite L.;
RT "Microcephaly thin corpus callosum intellectual disability syndrome caused
RT by mutated TAF2.";
RL Pediatr. Neurol. 49:411-417(2013).
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,
CC PubMed:9418870, PubMed:9774672). TAF2 forms a promoter DNA binding
CC subcomplex of TFIID, together with TAF7 and TAF1 (PubMed:9774672,
CC PubMed:33795473). {ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672}.
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 (PubMed:9774672,
CC PubMed:33795473). Interacts with TAF2C1 (PubMed:9418870). Component of
CC the TFTC-HAT complex (PubMed:12601814). {ECO:0000269|PubMed:12601814,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:9418870,
CC ECO:0000269|PubMed:9774672}.
CC -!- INTERACTION:
CC Q6P1X5; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-1560063, EBI-11529177;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9774672}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC {ECO:0000269|PubMed:9774672}.
CC -!- DISEASE: Neurodevelopmental disorder with feeding difficulties, thin
CC corpus callosum, and foot deformity (NEDFCF) [MIM:615599]: An autosomal
CC recessive disorder characterized by impaired intellectual development,
CC microcephaly, delayed psychomotor development, pyramidal signs, thin
CC corpus callosum, and foot deformity. {ECO:0000269|PubMed:21937992,
CC ECO:0000269|PubMed:24084144}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: PubMed:9418870 was unable to show an association between
CC TAF2 and TFIID.
CC -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC68502.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH64830.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF026445; AAC02966.1; -; mRNA.
DR EMBL; AF040701; AAC68502.1; ALT_INIT; mRNA.
DR EMBL; AF057694; AAC13540.1; -; mRNA.
DR EMBL; AK316592; BAG38179.1; -; mRNA.
DR EMBL; AC107960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035673; AAH35673.1; -; mRNA.
DR EMBL; BC047732; AAH47732.1; -; mRNA.
DR EMBL; BC064830; AAH64830.1; ALT_SEQ; mRNA.
DR CCDS; CCDS34937.1; -.
DR RefSeq; NP_003175.1; NM_003184.3.
DR PDB; 5FUR; EM; 8.50 A; I=1-1199.
DR PDB; 6MZC; EM; 4.50 A; B=1-1199.
DR PDB; 6MZL; EM; 23.00 A; B=1-1199.
DR PDB; 6MZM; EM; 7.50 A; B=1-1199.
DR PDB; 7EDX; EM; 4.50 A; B=1-1199.
DR PDB; 7EG7; EM; 6.20 A; B=1-1199.
DR PDB; 7EG8; EM; 7.40 A; B=1-1199.
DR PDB; 7EG9; EM; 3.70 A; B=1-1199.
DR PDB; 7EGA; EM; 4.10 A; B=1-1199.
DR PDB; 7EGB; EM; 3.30 A; B=1-1199.
DR PDB; 7EGC; EM; 3.90 A; B=1-1199.
DR PDB; 7EGD; EM; 6.75 A; B=1-1199.
DR PDB; 7EGE; EM; 9.00 A; B=1-1199.
DR PDB; 7EGH; EM; 3.04 A; B=1-1199.
DR PDB; 7EGI; EM; 9.82 A; B=1-1199.
DR PDB; 7EGJ; EM; 8.64 A; B=1-1199.
DR PDB; 7ENA; EM; 4.07 A; DB=1-1199.
DR PDB; 7ENC; EM; 4.13 A; DB=1-1199.
DR PDBsum; 5FUR; -.
DR PDBsum; 6MZC; -.
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; 7EGH; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q6P1X5; -.
DR SMR; Q6P1X5; -.
DR BioGRID; 112736; 173.
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 CORUM; Q6P1X5; -.
DR DIP; DIP-38921N; -.
DR IntAct; Q6P1X5; 31.
DR MINT; Q6P1X5; -.
DR STRING; 9606.ENSP00000367406; -.
DR MEROPS; M01.972; -.
DR iPTMnet; Q6P1X5; -.
DR PhosphoSitePlus; Q6P1X5; -.
DR BioMuta; TAF2; -.
DR DMDM; 145559533; -.
DR EPD; Q6P1X5; -.
DR jPOST; Q6P1X5; -.
DR MassIVE; Q6P1X5; -.
DR MaxQB; Q6P1X5; -.
DR PaxDb; Q6P1X5; -.
DR PeptideAtlas; Q6P1X5; -.
DR PRIDE; Q6P1X5; -.
DR ProteomicsDB; 66877; -.
DR Antibodypedia; 26803; 164 antibodies from 22 providers.
DR DNASU; 6873; -.
DR Ensembl; ENST00000378164.7; ENSP00000367406.2; ENSG00000064313.13.
DR GeneID; 6873; -.
DR KEGG; hsa:6873; -.
DR MANE-Select; ENST00000378164.7; ENSP00000367406.2; NM_003184.4; NP_003175.2.
DR UCSC; uc003you.4; human.
DR CTD; 6873; -.
DR DisGeNET; 6873; -.
DR GeneCards; TAF2; -.
DR HGNC; HGNC:11536; TAF2.
DR HPA; ENSG00000064313; Low tissue specificity.
DR MalaCards; TAF2; -.
DR MIM; 604912; gene.
DR MIM; 615599; phenotype.
DR neXtProt; NX_Q6P1X5; -.
DR OpenTargets; ENSG00000064313; -.
DR Orphanet; 397951; Microcephaly-thin corpus callosum-intellectual disability syndrome.
DR PharmGKB; PA36311; -.
DR VEuPathDB; HostDB:ENSG00000064313; -.
DR eggNOG; KOG1932; Eukaryota.
DR GeneTree; ENSGT00390000000420; -.
DR HOGENOM; CLU_002317_0_0_1; -.
DR InParanoid; Q6P1X5; -.
DR OMA; GQESYEW; -.
DR OrthoDB; 142542at2759; -.
DR PhylomeDB; Q6P1X5; -.
DR TreeFam; TF315208; -.
DR PathwayCommons; Q6P1X5; -.
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-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 SignaLink; Q6P1X5; -.
DR SIGNOR; Q6P1X5; -.
DR BioGRID-ORCS; 6873; 534 hits in 1093 CRISPR screens.
DR ChiTaRS; TAF2; human.
DR GeneWiki; TAF2; -.
DR GenomeRNAi; 6873; -.
DR Pharos; Q6P1X5; Tbio.
DR PRO; PR:Q6P1X5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6P1X5; protein.
DR Bgee; ENSG00000064313; Expressed in adrenal tissue and 207 other tissues.
DR ExpressionAtlas; Q6P1X5; baseline and differential.
DR Genevisible; Q6P1X5; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
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: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:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; PTHR15137; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Intellectual disability; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1199
FT /note="Transcription initiation factor TFIID subunit 2"
FT /id="PRO_0000252424"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1172
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 8
FT /note="P -> L (in dbSNP:rs17818842)"
FT /id="VAR_027854"
FT VARIANT 186
FT /note="T -> R (in NEDFCF; unknown pathological
FT significance; dbSNP:rs398124656)"
FT /evidence="ECO:0000269|PubMed:24084144"
FT /id="VAR_070945"
FT VARIANT 416
FT /note="P -> H (in NEDFCF; unknown pathological
FT significance; dbSNP:rs398124655)"
FT /evidence="ECO:0000269|PubMed:24084144"
FT /id="VAR_070946"
FT VARIANT 447
FT /note="S -> T (in dbSNP:rs9297605)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9418870, ECO:0000269|PubMed:9774672,
FT ECO:0000269|Ref.3"
FT /id="VAR_027855"
FT VARIANT 649
FT /note="W -> R (in NEDFCF; dbSNP:rs398124645)"
FT /id="VAR_070947"
FT VARIANT 686
FT /note="E -> K (in dbSNP:rs34154779)"
FT /id="VAR_057263"
FT VARIANT 1122
FT /note="S -> N (in dbSNP:rs956749)"
FT /id="VAR_027856"
FT VARIANT 1139
FT /note="T -> A (in dbSNP:rs956748)"
FT /id="VAR_027857"
FT CONFLICT 1
FT /note="M -> R (in Ref. 2; AAC68502)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> H (in Ref. 1; AAC02966)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="P -> L (in Ref. 6; AAH47732)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> C (in Ref. 6; AAH64830)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="I -> K (in Ref. 6; AAH35673/AAH47732)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="R -> G (in Ref. 2; AAC68502)"
FT /evidence="ECO:0000305"
FT STRAND 23..39
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 44..58
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 229..242
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 367..408
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 443..463
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 466..483
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 528..538
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 543..550
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 675..685
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 692..708
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 709..712
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 720..727
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 746..757
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 769..780
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 785..789
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 792..804
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 824..842
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 849..863
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 872..877
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 884..900
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 904..915
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 920..932
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 947..958
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 962..964
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 967..979
FT /evidence="ECO:0007829|PDB:7EGH"
SQ SEQUENCE 1199 AA; 136971 MW; 169DA4A3878CFD59 CRC64;
MPLTGVEPAR MNRKKGDKGF ESPRPYKLTH QVVCINNINF QRKSVVGFVE LTIFPTVANL
NRIKLNSKQC RIYRVRINDL EAAFIYNDPT LEVCHSESKQ RNLNYFSNAY AAAVSAVDPD
AGNGELCIKV PSELWKHVDE LKVLKIHINF SLDQPKGGLH FVVPSVEGSM AERGAHVFSC
GYQNSTRFWF PCVDSYSELC TWKLEFTVDA AMVAVSNGDL VETVYTHDMR KKTFHYMLTI
PTAASNISLA IGPFEILVDP YMHEVTHFCL PQLLPLLKHT TSYLHEVFEF YEEILTCRYP
YSCFKTVFID EAYVEVAAYA SMSIFSTNLL HSAMIIDETP LTRRCLAQSL AQQFFGCFIS
RMSWSDEWVL KGISGYIYGL WMKKTFGVNE YRHWIKEELD KIVAYELKTG GVLLHPIFGG
GKEKDNPASH LHFSIKHPHT LSWEYYSMFQ CKAHLVMRLI ENRISMEFML QVFNKLLSLA
STASSQKFQS HMWSQMLVST SGFLKSISNV SGKDIQPLIK QWVDQSGVVK FYGSFAFNRK
RNVLELEIKQ DYTSPGTQKY VGPLKVTVQE LDGSFNHTLQ IEENSLKHDI PCHSKSRRNK
KKKIPLMNGE EVDMDLSAMD ADSPLLWIRI DPDMSVLRKV EFEQADFMWQ YQLRYERDVV
AQQESILALE KFPTPASRLA LTDILEQEQC FYRVRMSACF CLAKIANSMV STWTGPPAMK
SLFTRMFCCK SCPNIVKTNN FMSFQSYFLQ KTMPVAMALL RDVHNLCPKE VLTFILDLIK
YNDNRKNKFS DNYYRAEMID ALANSVTPAV SVNNEVRTLD NLNPDVRLIL EEITRFLNME
KLLPSYRHTI TVSCLRAIRV LQKNGHVPSD PALFKSYAEY GHFVDIRIAA LEAVVDYTKV
DRSYEELQWL LNMIQNDPVP YVRHKILNML TKNPPFTKNM ESPLCNEALV DQLWKLMNSG
TSHDWRLRCG AVDLYFTLFG LSRPSCLPLP ELGLVLNLKE KKAVLNPTII PESVAGNQEA
ANNPSSHPQL VGFQNPFSSS QDEEEIDMDT VHDSQAFISH HLNMLERPST PGLSKYRPAS
SRSALIPQHS AGCDSTPTTK PQWSLELARK GTGKEQAPLE MSMHPAASAP LSVFTKESTA
SKHSDHHHHH HHEHKKKKKK HKHKHKHKHK HDSKEKDKEP FTFSSPASGR SIRSPSLSD
