TAF12_MOUSE
ID TAF12_MOUSE Reviewed; 161 AA.
AC Q8VE65; Q3V0S7; Q9CZ11; Q9D8Q0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcription initiation factor TFIID subunit 12;
DE AltName: Full=Transcription initiation factor TFIID 20 kDa subunits;
DE Short=TAFII-20;
DE Short=TAFII20;
GN Name=Taf12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of TBP and TBP-associated factors (TAFs), including TAF1,
CC TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and
CC TAF13. Component of the TATA-binding protein-free TAF complex (TFTC),
CC the PCAF histone acetylase complex and the STAGA transcription
CC coactivator-HAT complex. {ECO:0000250|UniProtKB:Q16514}.
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. Component of the
CC TATA-binding protein-free TAF complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex.
CC Component of the PCAF complex, at least composed of TADA2L/ADA2,
CC TADA3L/ADA3, TAF5L/PAF65-beta, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and
CC TRRAP. Component of the STAGA transcription coactivator-HAT complex, at
CC least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, STAF65-gamma/SUPT7L,
CC TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Interacts with ATF7 (via
CC the transactivation domain); the interaction is prevented by
CC sumoylation of ATF7. {ECO:0000250|UniProtKB:Q16514}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
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DR EMBL; AK007811; BAB25276.1; -; mRNA.
DR EMBL; AK013133; BAB28669.1; -; mRNA.
DR EMBL; AK132927; BAE21426.1; -; mRNA.
DR EMBL; BC019668; AAH19668.1; -; mRNA.
DR CCDS; CCDS18721.1; -.
DR RefSeq; NP_079855.2; NM_025579.3.
DR RefSeq; XP_006539170.2; XM_006539107.3.
DR RefSeq; XP_006539172.1; XM_006539109.1.
DR RefSeq; XP_006539173.1; XM_006539110.1.
DR RefSeq; XP_017175839.1; XM_017320350.1.
DR AlphaFoldDB; Q8VE65; -.
DR SMR; Q8VE65; -.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q8VE65; -.
DR DIP; DIP-29178N; -.
DR IntAct; Q8VE65; 3.
DR MINT; Q8VE65; -.
DR STRING; 10090.ENSMUSP00000030731; -.
DR iPTMnet; Q8VE65; -.
DR PhosphoSitePlus; Q8VE65; -.
DR EPD; Q8VE65; -.
DR jPOST; Q8VE65; -.
DR MaxQB; Q8VE65; -.
DR PaxDb; Q8VE65; -.
DR PeptideAtlas; Q8VE65; -.
DR PRIDE; Q8VE65; -.
DR ProteomicsDB; 254646; -.
DR Antibodypedia; 1777; 214 antibodies from 27 providers.
DR DNASU; 66464; -.
DR Ensembl; ENSMUST00000030731; ENSMUSP00000030731; ENSMUSG00000028899.
DR GeneID; 66464; -.
DR KEGG; mmu:66464; -.
DR UCSC; uc008vax.3; mouse.
DR CTD; 6883; -.
DR MGI; MGI:1913714; Taf12.
DR VEuPathDB; HostDB:ENSMUSG00000028899; -.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR HOGENOM; CLU_093619_3_1_1; -.
DR InParanoid; Q8VE65; -.
DR OMA; HRRDTTV; -.
DR OrthoDB; 1569957at2759; -.
DR PhylomeDB; Q8VE65; -.
DR TreeFam; TF323652; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 66464; 21 hits in 81 CRISPR screens.
DR ChiTaRS; Taf12; mouse.
DR PRO; PR:Q8VE65; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VE65; protein.
DR Bgee; ENSMUSG00000028899; Expressed in animal zygote and 238 other tissues.
DR ExpressionAtlas; Q8VE65; baseline and differential.
DR Genevisible; Q8VE65; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000124; C:SAGA complex; IDA:MGI.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
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 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_0000118908"
FT DOMAIN 56..128
FT /note="Histone-fold"
FT /evidence="ECO:0000305"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16514"
FT CONFLICT 77
FT /note="D -> G (in Ref. 1; BAB28669)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="M -> I (in Ref. 1; BAB28669)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="K -> N (in Ref. 1; BAB25276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17875 MW; B3C11D70B6E94E35 CRC64;
MNQFGPSALI NLSSFSSVKP EPASTPPQGS MANSTTVGKI AGTPGTGGRL SPENNQVLTK
KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC QLARHRKSST LEVKDVQLHL
ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ RMALIRKTTK K
