TAF5_MOUSE
ID TAF5_MOUSE Reviewed; 801 AA.
AC Q8C092; Q8BTR2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Transcription initiation factor TFIID subunit 5;
DE AltName: Full=Transcription initiation factor TFIID 100 kDa subunit;
DE Short=TAF(II)100;
DE Short=TAFII-100;
DE Short=TAFII100;
GN Name=Taf5;
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=Medulla oblongata, and Thymus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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. The TFIID complex structure can be divided into 3 modules TFIID-
CC A, TFIID-B, and TFIID-C. TAF5 is involved in two modules of TFIID, in
CC TFIID-A together with TAF3 and TBP, and in TFIID-B with TAF8. Involved
CC in contacts between TFIID and TFIIF in the PIC.
CC {ECO:0000250|UniProtKB:Q15542}.
CC -!- SUBUNIT: Homodimer. Component of the TFIID basal transcription factor
CC complex, 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. The TFIID
CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and
CC TFIID-C. TAF5 forms the TFIID-A module together with TAF3 and TBP, and
CC in TFIID-B with TAF8. Component of the TFTC-HAT complex, at least
CC composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2, TAF4, TAF5,
CC GCN5L2/GCN5, TAF10 and TRRAP. TBP is not part of the TFTC-HAT complex.
CC Interacts strongly with the histone H4-related TAF6 and the histone H3-
CC related TAF9, as well as a stable complex comprised of both TAF6 and
CC TAF9. Apparently weaker interactions with TBP, TAF1, TAF11, and TAF12,
CC but not TAF7, also have been observed. {ECO:0000250|UniProtKB:Q15542}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: Distinct domains of TAF5/TAFII100 are required for functional
CC interaction with transcription factor TFIIFB (RAP30) and incorporation
CC into the TFIID complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}.
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DR EMBL; AK031985; BAC27638.1; -; mRNA.
DR EMBL; AK088953; BAC40670.1; -; mRNA.
DR CCDS; CCDS29886.1; -.
DR RefSeq; NP_796316.2; NM_177342.3.
DR AlphaFoldDB; Q8C092; -.
DR SMR; Q8C092; -.
DR BioGRID; 230488; 4.
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; Q8C092; -.
DR IntAct; Q8C092; 4.
DR STRING; 10090.ENSMUSP00000026027; -.
DR iPTMnet; Q8C092; -.
DR PhosphoSitePlus; Q8C092; -.
DR EPD; Q8C092; -.
DR MaxQB; Q8C092; -.
DR PaxDb; Q8C092; -.
DR PeptideAtlas; Q8C092; -.
DR PRIDE; Q8C092; -.
DR ProteomicsDB; 263243; -.
DR DNASU; 226182; -.
DR GeneID; 226182; -.
DR KEGG; mmu:226182; -.
DR CTD; 6877; -.
DR MGI; MGI:2442144; Taf5.
DR eggNOG; KOG0263; Eukaryota.
DR InParanoid; Q8C092; -.
DR OrthoDB; 620721at2759; -.
DR PhylomeDB; Q8C092; -.
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-6807505; RNA polymerase II transcribes snRNA genes.
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; 226182; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Taf5; mouse.
DR PRO; PR:Q8C092; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C092; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA: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:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; 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 CDD; cd08044; TAF5_NTD2; 1.
DR Gene3D; 1.25.40.500; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037783; Taf5.
DR InterPro; IPR007582; TFIID_NTD2.
DR InterPro; IPR037264; TFIID_NTD2_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19879; PTHR19879; 1.
DR Pfam; PF04494; TFIID_NTD2; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF160897; SSF160897; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..801
FT /note="Transcription initiation factor TFIID subunit 5"
FT /id="PRO_0000051258"
FT DOMAIN 93..125
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 469..508
FT /note="WD 1"
FT REPEAT 542..581
FT /note="WD 2"
FT REPEAT 584..625
FT /note="WD 3"
FT REPEAT 626..667
FT /note="WD 4"
FT REPEAT 668..707
FT /note="WD 5"
FT REPEAT 710..749
FT /note="WD 6"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 27
FT /note="Q -> E (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="G -> C (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 37..38
FT /note="GG -> VV (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> S (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..80
FT /note="AVSAAAPAGAA -> GASGGDPEEAV (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..86
FT /note="AAP -> DAL (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="PH -> TN (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Y -> S (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="Y -> F (in Ref. 1; BAC27638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 87045 MW; 3E71FF4A99741CCB CRC64;
MAALAEEQTE VAVKLEPEGP PTLLPPQAGD GAGEGSGGTP NNGPNGGGGG NVAVAAAAGG
DGGTPKPGVA VSAAAPAGAA PVPAAPAEAG APHDRQTLLA VLQFLRQSNL REAEEALRRE
ARLLEEAVAG SGAPGELDGA GAEAASALLS RVTASVPGSA APEPPGTGAS VTSVFSGSAS
GPAAPGKVAS VAVEDQPDVS AVLSAYNQQG DPTMYEEYYS GLKHFIECSL DCHRAELSQL
FYPLFVHMYL ELVYNQHENE AKSFFEKFHG DQECYYQDDL RVLSSLTKKE HMKGNETMLD
FRTSKFVLRI YRDSYQLLKR HLQEKQNNQI WNIVQEHLYI DIFDGMPRSK QQIDAMVGSL
AGEAKREANK SKVFFGLLKE PEIEVPLDDE DEEGENEEGK PKKKKPKKDS IGSKSKKQDP
NAPPQNRIPL PELKDSDKLD KIMNMKETTK RVRLGPDCLP SICFYTFLNA YQGLTAVDVT
DDSSLIAGGF ADSTVRVWSV TPKKLRSVKQ ASDLSLIDKE SDDVLERIMD EKTASELKIL
YGHSGPVYGA SFSPDRNYLL SSSEDGTVRL WSLQTFTCLV GYKGHNYPVW DTQFSPYGYY
FVSGGHDRVA RLWATDHYQP LRIFAGHLAD VNCTRYHPNS NYVATGSADR TVRLWDVLNG
NCVRIFTGHK GPIHSLTFSP NGRFLATGAT DGRVLLWDIG HGLMVGELKG HTDTVCSLRF
SRDGEILASG SMDNTVRLWD AVKAFEDLET DDFTTATGHI NLPENSQELL LGTYMTKSTP
VVHLHFTRRN LVLAAGAYSP Q
