TAF2_MOUSE
ID TAF2_MOUSE Reviewed; 1104 AA.
AC Q8C176; Q8BKQ7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Transcription initiation factor TFIID subunit 2;
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;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-610.
RC STRAIN=C57BL/6J; TISSUE=Skin, and Spinal ganglion;
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).
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. TAF2 forms a promoter DNA binding subcomplex of TFIID, together
CC with TAF7 and TAF1. {ECO:0000250|UniProtKB:Q6P1X5}.
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. Interacts with
CC TAF2C1. Component of the TFTC-HAT complex.
CC {ECO:0000250|UniProtKB:Q6P1X5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
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DR EMBL; AC137950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK028828; BAC26141.1; -; mRNA.
DR EMBL; AK051126; BAC34531.1; -; mRNA.
DR AlphaFoldDB; Q8C176; -.
DR SMR; Q8C176; -.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q8C176; -.
DR IntAct; Q8C176; 1.
DR STRING; 10090.ENSMUSP00000043733; -.
DR MEROPS; M01.972; -.
DR iPTMnet; Q8C176; -.
DR PhosphoSitePlus; Q8C176; -.
DR EPD; Q8C176; -.
DR jPOST; Q8C176; -.
DR MaxQB; Q8C176; -.
DR PaxDb; Q8C176; -.
DR PeptideAtlas; Q8C176; -.
DR PRIDE; Q8C176; -.
DR ProteomicsDB; 263065; -.
DR MGI; MGI:2443028; Taf2.
DR eggNOG; KOG1932; Eukaryota.
DR InParanoid; Q8C176; -.
DR PhylomeDB; Q8C176; -.
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 ChiTaRS; Taf2; mouse.
DR PRO; PR:Q8C176; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C176; protein.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
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: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:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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 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 2: Evidence at transcript level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1104
FT /note="Transcription initiation factor TFIID subunit 2"
FT /id="PRO_0000252425"
FT REGION 1040..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1077
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1X5"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1X5"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1X5"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1X5"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1X5"
SQ SEQUENCE 1104 AA; 126997 MW; A557FFDF19E9A0F0 CRC64;
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 TSYIHEVFEF YEEILTCRYP YSCFKTVFID
EAYVEVAAYA SMSIFSTNLL HSAMIIDETP LTRRCLAQAL AQQFFGCFIS RMSWSDEWVL
KGISGYIYGL WMKKTFGVNE YHHWIKEELD KIVAYELKTG GVLLHPIFGG GKEKDNPASH
LHFSIKHPHT LSWEYYTMFQ CKAHLVMRLI ENRISMEFML QVFNKLLSLA STASSQKFQS
HMWSQMLVST YGFLKSISNV SGKDIQPLIK QWLDQSGVVK FYGSFAFNRK RNVLELEIKQ
DYTSPGTQKY VGPLKVTVQE LDGSFNHTLQ IEENSLKHDI PCHSKSRRNK KKKIPLMNGE
EVDMDLSAME ADSPLLWIRI DPDMSVLRKV EFEQADFMWQ YELRYERDVV AQQESILALE
KFPTPASRLA LTDILEQEQC FYRVRMSACF CLAKIANSMV STWTGPPAMK SLFTRMFCCK
TCPNIVKTNN FMSFQSYFLQ KTMPVAMALL RDVHNLCPKE VLTFILDLIK YNDNRKNKFS
DNYYRAEMID ALANSVTPAV SVNNEVRTLD NLNPDVRLIL EEITRFLNME KLLPSYRHTI
TVSCLRAIRV LQKNGHVPSD ASLFKSYAEY GHFVDIRIAA LEAVVDYTKV DRSYEELQWL
LNMIQTDPVP YVRHKILNML TKNPPFTKNM ESPLCNEALV DQLWKLMNSG TAHDWRLRCG
AVDLYFTLFG LSRPSCLPLP ELGLVLNLKE KKAVLNPTII PEAGVGNQFS SSQDEEEVDM
DTVHDSQAFI SHHLNMLERP STPGLSKYRP HHHHHHHEHK KKKKKHKHKH KHKHKHDSKD
KDREPFAFSS PASGRSVRSP SLSD
