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 13-SEP-2023, entry version 153. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8GXQ; EM; 5.04 A; DB=1-1199. DR PDB; 8GXS; EM; 4.16 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 PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR AlphaFoldDB; Q6P1X5; -. DR SMR; Q6P1X5; -. DR BioGRID; 112736; 180. 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 GlyGen; Q6P1X5; 2 sites, 1 O-linked glycan (2 sites). 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 ProteomicsDB; 66877; -. DR Antibodypedia; 26803; 172 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 AGR; HGNC:11536; -. 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; QYMAAQR; -. DR OrthoDB; 11119at2759; -. 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; 572 hits in 1183 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:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal. DR GO; GO:0006282; P:regulation of DNA repair; NAS: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 at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd09839; M1_like_TAF2; 1. DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1. DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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; TRANSCRIPTION INITIATION FACTOR TFIID; 1. DR PANTHER; PTHR15137:SF9; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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 /evidence="ECO:0000269|PubMed:21937992" 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 //