TAF12_HUMAN
ID TAF12_HUMAN Reviewed; 161 AA.
AC Q16514; D3DPM5; Q15775; Q5T077;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Transcription initiation factor TFIID subunit 12 {ECO:0000305};
DE AltName: Full=Transcription initiation factor TFIID 20/15 kDa subunits {ECO:0000305};
DE Short=TAFII-20/TAFII-15 {ECO:0000305};
DE Short=TAFII20/TAFII15 {ECO:0000312|HGNC:HGNC:11545};
GN Name=TAF12 {ECO:0000312|HGNC:HGNC:11545};
GN Synonyms=TAF15, TAF2J {ECO:0000312|HGNC:HGNC:11545},
GN TAFII20 {ECO:0000312|HGNC:HGNC:11545};
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] (ISOFORM TAFII20), AND FUNCTION.
RX PubMed=8598932; DOI=10.1038/380356a0;
RA Hoffmann A., Chiang C.M., Oelgeschlager T., Xie X., Burley S.K.,
RA Nakatani Y., Roeder R.G.;
RT "A histone octamer-like structure within TFIID.";
RL Nature 380:356-359(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAFII15 AND TAFII20), AND FUNCTION.
RX PubMed=8663456; DOI=10.1074/jbc.271.30.18194;
RA Hoffmann A., Roeder R.G.;
RT "Cloning and characterization of human TAF20/15. Multiple interactions
RT suggest a central role in TFIID complex formation.";
RL J. Biol. Chem. 271:18194-18202(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20).
RX PubMed=8647459; DOI=10.1016/0378-1119(95)00838-1;
RA Choi B., Bando M., Hasegawa S., Horikoshi M.;
RT "Isolation and characterization of a cDNA encoding a novel human
RT transcription factor TFIID subunit containing similarities with histones
RT H2B and H3.";
RL Gene 169:263-267(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TAFII20), PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, AND INTERACTION WITH TBP.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAFII20).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAFII20).
RC TISSUE=Lung;
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 [10]
RP PROTEIN SEQUENCE OF 50-60 AND 115-122, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP 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 [11]
RP FUNCTION, AND IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L;
RP TADA3L; SUPT3H; TAF2; TAF5; TRRAP; TAF4; 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 FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH
RP SF3B3; GCN5L2; SUPT7L; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 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 [13]
RP FUNCTION, AND IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L;
RP TAF5L; SUPT3H; TAF6L; TAF10; 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 [14]
RP INTERACTION WITH ATF7.
RX PubMed=15735663; DOI=10.1038/sj.onc.1208565;
RA Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C.,
RA Chatton B.;
RT "A functional interaction between ATF7 and TAF12 that is modulated by
RT TAF4.";
RL Oncogene 24:3472-3483(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-51, AND
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 57-128 IN COMPLEX WITH TAF4, AND
RP MUTAGENESIS OF 87-ILE--PHE-91; 95-VAL-VAL-96 AND 99-ALA--ALA-103.
RX PubMed=10594036; DOI=10.1128/mcb.20.1.340-351.2000;
RA Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D.,
RA Davidson I.;
RT "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA
RT components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.";
RL Mol. Cell. Biol. 20:340-351(2000).
RN [22] {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). Component
CC of the TATA-binding protein-free TAF complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex
CC (PubMed:10373431, PubMed:7729427, PubMed:8598932, PubMed:8663456,
CC PubMed:9674425, PubMed:9885574). {ECO:0000269|PubMed:10373431,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:7729427,
CC ECO:0000269|PubMed:8598932, ECO:0000269|PubMed:8663456,
CC ECO:0000269|PubMed:9674425, 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:10373431,
CC PubMed:11564863, PubMed:9885574, PubMed:10594036). Component of the
CC PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3,
CC TAF5L/PAF65-beta, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP
CC (PubMed:9885574). Component of the STAGA transcription coactivator-HAT
CC complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, STAF65-
CC gamma/SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9
CC (PubMed:11564863, PubMed:10594036). Interacts with ATF7 (via the
CC transactivation domain); the interaction is prevented by sumoylation of
CC ATF7 (PubMed:15735663). {ECO:0000269|PubMed:10373431,
CC ECO:0000269|PubMed:10594036, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:9885574}.
CC -!- SUBUNIT: [Isoform TAFII20]: Interacts with TBP; the interaction is
CC direct (PubMed:7729427). Interacts with TAF10; the interaction is
CC direct (PubMed:7729427). Interacts with ATF7, promoting transactivation
CC by ATF7 (PubMed:15735663). {ECO:0000269|PubMed:15735663,
CC ECO:0000269|PubMed:7729427}.
CC -!- SUBUNIT: [Isoform TAFII15]: Does not promote the transactivation of
CC ATF7. {ECO:0000269|PubMed:15735663}.
CC -!- INTERACTION:
CC Q16514; P31323: PRKAR2B; NbExp=3; IntAct=EBI-1034238, EBI-2930670;
CC Q16514; Q6DHZ2: PRKAR2B; NbExp=3; IntAct=EBI-1034238, EBI-10185196;
CC Q16514; Q15572: TAF1C; NbExp=2; IntAct=EBI-1034238, EBI-2510659;
CC Q16514; P20226: TBP; NbExp=3; IntAct=EBI-1034238, EBI-355371;
CC Q16514-1; O00268: TAF4; NbExp=16; IntAct=EBI-1034253, EBI-1034261;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9674425}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=TAFII20;
CC IsoId=Q16514-1; Sequence=Displayed;
CC Name=TAFII15;
CC IsoId=Q16514-2; Sequence=VSP_018888;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf12/";
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DR EMBL; U57693; AAC50600.1; -; mRNA.
DR EMBL; U57693; AAC50601.1; -; mRNA.
DR EMBL; D50544; BAA09112.1; -; mRNA.
DR EMBL; X84002; CAA58826.1; -; mRNA.
DR EMBL; BT007031; AAP35678.1; -; mRNA.
DR EMBL; AY206865; AAO13491.1; -; Genomic_DNA.
DR EMBL; AL513497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07682.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07683.1; -; Genomic_DNA.
DR EMBL; BC011986; AAH11986.1; -; mRNA.
DR CCDS; CCDS326.1; -. [Q16514-1]
DR PIR; JC4676; JC4676.
DR RefSeq; NP_001128690.1; NM_001135218.1. [Q16514-1]
DR RefSeq; NP_005635.1; NM_005644.3. [Q16514-1]
DR PDB; 1H3O; X-ray; 2.30 A; B/D=57-128.
DR PDB; 6MZC; EM; 4.50 A; R=1-161.
DR PDB; 6MZD; EM; 9.80 A; Q=1-161.
DR PDB; 6MZL; EM; 23.00 A; Q/R=1-161.
DR PDB; 6MZM; EM; 7.50 A; R=1-161.
DR PDB; 7EDX; EM; 4.50 A; L/l=1-161.
DR PDB; 7EG7; EM; 6.20 A; L/l=1-161.
DR PDB; 7EG8; EM; 7.40 A; L/l=1-161.
DR PDB; 7EG9; EM; 3.70 A; L/l=1-161.
DR PDB; 7EGA; EM; 4.10 A; L/l=1-161.
DR PDB; 7EGB; EM; 3.30 A; L/l=1-161.
DR PDB; 7EGC; EM; 3.90 A; L/l=1-161.
DR PDB; 7EGD; EM; 6.75 A; L/l=1-161.
DR PDB; 7EGE; EM; 9.00 A; L/l=1-161.
DR PDB; 7EGF; EM; 3.16 A; l=1-161.
DR PDB; 7EGG; EM; 2.77 A; L=1-161.
DR PDB; 7EGI; EM; 9.82 A; L/l=1-161.
DR PDB; 7EGJ; EM; 8.64 A; L/l=1-161.
DR PDB; 7ENA; EM; 4.07 A; DL/Dl=1-161.
DR PDB; 7ENC; EM; 4.13 A; DL/Dl=1-161.
DR PDB; 7KTR; EM; 2.93 A; G=1-161.
DR PDB; 7KTS; EM; 19.09 A; G=1-161.
DR PDBsum; 1H3O; -.
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; Q16514; -.
DR SMR; Q16514; -.
DR BioGRID; 112746; 92.
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; Q16514; -.
DR DIP; DIP-496N; -.
DR IntAct; Q16514; 50.
DR MINT; Q16514; -.
DR STRING; 9606.ENSP00000263974; -.
DR iPTMnet; Q16514; -.
DR PhosphoSitePlus; Q16514; -.
DR BioMuta; TAF12; -.
DR DMDM; 3024708; -.
DR EPD; Q16514; -.
DR jPOST; Q16514; -.
DR MassIVE; Q16514; -.
DR MaxQB; Q16514; -.
DR PaxDb; Q16514; -.
DR PeptideAtlas; Q16514; -.
DR PRIDE; Q16514; -.
DR ProteomicsDB; 60885; -. [Q16514-1]
DR ProteomicsDB; 60886; -. [Q16514-2]
DR Antibodypedia; 1777; 214 antibodies from 27 providers.
DR DNASU; 6883; -.
DR Ensembl; ENST00000263974.4; ENSP00000263974.4; ENSG00000120656.14. [Q16514-1]
DR Ensembl; ENST00000373824.9; ENSP00000362930.4; ENSG00000120656.14. [Q16514-1]
DR Ensembl; ENST00000685312.1; ENSP00000509153.1; ENSG00000120656.14. [Q16514-1]
DR Ensembl; ENST00000689843.1; ENSP00000509370.1; ENSG00000120656.14. [Q16514-1]
DR Ensembl; ENST00000692098.1; ENSP00000509051.1; ENSG00000120656.14. [Q16514-1]
DR GeneID; 6883; -.
DR KEGG; hsa:6883; -.
DR MANE-Select; ENST00000373824.9; ENSP00000362930.4; NM_005644.4; NP_005635.1.
DR UCSC; uc001bqx.5; human. [Q16514-1]
DR CTD; 6883; -.
DR DisGeNET; 6883; -.
DR GeneCards; TAF12; -.
DR HGNC; HGNC:11545; TAF12.
DR HPA; ENSG00000120656; Low tissue specificity.
DR MIM; 600773; gene.
DR neXtProt; NX_Q16514; -.
DR OpenTargets; ENSG00000120656; -.
DR PharmGKB; PA36320; -.
DR VEuPathDB; HostDB:ENSG00000120656; -.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR HOGENOM; CLU_093619_3_1_1; -.
DR InParanoid; Q16514; -.
DR OMA; HRRDTTV; -.
DR OrthoDB; 1569957at2759; -.
DR PhylomeDB; Q16514; -.
DR TreeFam; TF323652; -.
DR PathwayCommons; Q16514; -.
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-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; Q16514; -.
DR SIGNOR; Q16514; -.
DR BioGRID-ORCS; 6883; 422 hits in 1081 CRISPR screens.
DR ChiTaRS; TAF12; human.
DR EvolutionaryTrace; Q16514; -.
DR GeneWiki; TAF12; -.
DR GenomeRNAi; 6883; -.
DR Pharos; Q16514; Tbio.
DR PRO; PR:Q16514; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16514; protein.
DR Bgee; ENSG00000120656; Expressed in oocyte and 173 other tissues.
DR Genevisible; Q16514; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:ARUK-UCL.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
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:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
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: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:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00248; -.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..161
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000033580"
FT DOMAIN 59..126
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 15..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform TAFII15)"
FT /evidence="ECO:0000303|PubMed:8663456"
FT /id="VSP_018888"
FT MUTAGEN 87..91
FT /note="IADDF->EADDK: Drastically reduces binding to TAF4."
FT /evidence="ECO:0000269|PubMed:10594036"
FT MUTAGEN 95..96
FT /note="VV->EK: Drastically reduces binding to TAF4."
FT /evidence="ECO:0000269|PubMed:10594036"
FT MUTAGEN 99..103
FT /note="ACQLA->RCQLR: Drastically reduces binding to TAF4."
FT /evidence="ECO:0000269|PubMed:10594036"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1H3O"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:1H3O"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:1H3O"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 161 AA; 17924 MW; 054B017CD7BF99CE CRC64;
MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGAGGRL SPENNQVLTK
KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC QLARHRKSST LEVKDVQLHL
ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ RMALIRKTTK K
