TAF1C_MOUSE
ID TAF1C_MOUSE Reviewed; 836 AA.
AC Q6PDZ2; P97359; Q3U3B6; Q8BN54;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=TATA box-binding protein-associated factor RNA polymerase I subunit C;
DE AltName: Full=RNA polymerase I-specific TBP-associated factor 95 kDa;
DE Short=TAFI95;
DE AltName: Full=TATA box-binding protein-associated factor 1C;
DE Short=TBP-associated factor 1C;
DE AltName: Full=Transcription initiation factor SL1/TIF-IB subunit C;
GN Name=Taf1c;
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 [MRNA], AND INTERACTION WITH TBP; TAF1A AND TAF1B.
RX PubMed=9050847; DOI=10.1073/pnas.94.5.1733;
RA Heix J., Zomerdijk J.C.B.M., Ravanpay A., Tjian R., Grummt I.;
RT "Cloning of murine RNA polymerase I-specific TAF factors: conserved
RT interactions between the subunits of the species-specific transcription
RT initiation factor TIF-IB/SL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1733-1738(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE RNA POLYMERASE I
RP HOLOCOMPLEX.
RX PubMed=9451438; DOI=10.1006/jmbi.1997.1434;
RA Seither P., Iben S., Grummt I.;
RT "Mammalian RNA polymerase I exists as a holoenzyme with associated basal
RT transcription factors.";
RL J. Mol. Biol. 275:43-53(1998).
RN [5]
RP INTERACTION WITH RRN3.
RX PubMed=12393749; DOI=10.1093/embo-reports/kvf212;
RA Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.;
RT "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits
RT regulate preinitiation complex assembly at the ribosomal gene promoter.";
RL EMBO Rep. 3:1082-1087(2002).
CC -!- FUNCTION: Component of the transcription factor SL1/TIF-IB complex,
CC which is involved in the assembly of the PIC (preinitiation complex)
CC during RNA polymerase I-dependent transcription. The rate of PIC
CC formation probably is primarily dependent on the rate of association of
CC SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in
CC stabilization of nucleolar transcription factor 1/UBTF on rDNA.
CC Formation of SL1/TIF-IB excludes the association of TBP with TFIID
CC subunits. Recruits RNA polymerase I to the rRNA gene promoter via
CC interaction with RRN3 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the transcription factor SL1/TIF-IB complex,
CC composed of TBP and at least TAF1A, TAF1B, TAF1C and TAF1D. In the
CC complex interacts directly with TBP, TAF1A and TAF1B. Interaction of
CC the SL1/TIF-IB subunits with TBP excludes interaction of TBP with the
CC transcription factor IID (TFIID) subunits. Interacts with MYC and RRN3.
CC Interacts with p53/TP53; the interaction prevents the association of
CC SL1/TIF-IB with UBTF and represses RNA polymerase I transcription (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9451438}.
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DR EMBL; Y09974; CAA71093.1; -; mRNA.
DR EMBL; AK087534; BAC39916.1; -; mRNA.
DR EMBL; AK154846; BAE32872.1; -; mRNA.
DR EMBL; BC058383; AAH58383.1; -; mRNA.
DR CCDS; CCDS40493.1; -.
DR RefSeq; NP_067416.2; NM_021441.2.
DR AlphaFoldDB; Q6PDZ2; -.
DR BioGRID; 203958; 6.
DR CORUM; Q6PDZ2; -.
DR STRING; 10090.ENSMUSP00000090789; -.
DR iPTMnet; Q6PDZ2; -.
DR PhosphoSitePlus; Q6PDZ2; -.
DR EPD; Q6PDZ2; -.
DR MaxQB; Q6PDZ2; -.
DR PaxDb; Q6PDZ2; -.
DR PeptideAtlas; Q6PDZ2; -.
DR PRIDE; Q6PDZ2; -.
DR ProteomicsDB; 254492; -.
DR Antibodypedia; 17054; 156 antibodies from 26 providers.
DR DNASU; 21341; -.
DR Ensembl; ENSMUST00000093099; ENSMUSP00000090789; ENSMUSG00000031832.
DR GeneID; 21341; -.
DR KEGG; mmu:21341; -.
DR UCSC; uc009npy.1; mouse.
DR CTD; 9013; -.
DR MGI; MGI:109576; Taf1c.
DR VEuPathDB; HostDB:ENSMUSG00000031832; -.
DR eggNOG; ENOG502QTCT; Eukaryota.
DR GeneTree; ENSGT00390000010767; -.
DR HOGENOM; CLU_360905_0_0_1; -.
DR InParanoid; Q6PDZ2; -.
DR OMA; CCRRWLK; -.
DR OrthoDB; 372910at2759; -.
DR PhylomeDB; Q6PDZ2; -.
DR TreeFam; TF351959; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR BioGRID-ORCS; 21341; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Taf1c; mouse.
DR PRO; PR:Q6PDZ2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6PDZ2; protein.
DR Bgee; ENSMUSG00000031832; Expressed in saccule of membranous labyrinth and 237 other tissues.
DR ExpressionAtlas; Q6PDZ2; baseline and differential.
DR Genevisible; Q6PDZ2; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000120; C:RNA polymerase I transcription regulator complex; TAS:MGI.
DR GO; GO:0005668; C:RNA polymerase transcription factor SL1 complex; IPI:MGI.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0006360; P:transcription by RNA polymerase I; TAS:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR038801; TAF1C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15319; PTHR15319; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..836
FT /note="TATA box-binding protein-associated factor RNA
FT polymerase I subunit C"
FT /id="PRO_0000118864"
FT REGION 662..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 802
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15572"
FT CONFLICT 89
FT /note="R -> Q (in Ref. 2; BAC39916)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="G -> A (in Ref. 1; CAA71093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 92023 MW; BAB6A50F5369368D CRC64;
MDFPGTLRPS LFKAGPLGMT DGPDLSFMCS WRDALTLPGS QPQNCKDPTL SFAKNLLWEP
STPGPLPLLM PPDPDPWDPG VTAQDFLFRG GHCYQYQSQA VLDVTEQLSR FLWDHGDIAF
APLGRLMLEN FRLEGNRGYS KKMTIVSAKK LLQDLGGHQP WGCPWASLSR RLRRFSIVGG
PVLSRSVSLL MGKLLHEELA MRWEQLLMDE AFTGGALAWL PGRTARAGQL VYPSGGALDK
LYFQEVSVTS GGNPRILENP GHVQLRGPVR QVVTSTVQGE TLLAVRSDYH CATWKIDKQG
PPALLQVMQV EKGATGISLS PHLSGELAIC SRSGAVCLWT PQAGLQTIYK DTETLAFRDP
SPWRWADFTA HPRVLTVGDR TGVKMVDIQG PPGCGLLLFR AGAEAACQKG ERVLLAQYLG
QPGQTPPSLH LICTQFSIYL MDERLPLVPM LKWDHGLPSA PLLARLLPPA SPGHPRPLLL
GGQGGQLQLL HITGEGTSMP QLAGPPQSLP SITESLSAFP LLEPKKQQLL QERLEAPVIG
LAAVPLCASA PGLLLFQLSA AGDVFYQHLR LLQASSPRKV PEQATAPSVD QVSTPSWTPQ
ASARCSRWLE DLMELSPTRP LWVAPTFSHR RFLGHMERQK SQETMPQKLR AAMAKGQLLR
PGDLSTLPRA EPPPAPQCSQ QDELTERLTE AWEGRVTAWW RRHRGETSET QTQSKRPKRR
TQLSSTFSSF TSYLDSPDAS SAPRSQDLST SEARLQSPRV PPSQELTQEV WGQGVKRERR
QTLRDHTDKL PLKRDTPGPV ATPPSQASSL QTMSFRQQTP VHSGSQPPQK KPRMGF
