TAF6L_MOUSE
ID TAF6L_MOUSE Reviewed; 616 AA.
AC Q8R2K4; Q8C5T2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L {ECO:0000305};
DE Short=TAF6L {ECO:0000305};
DE AltName: Full=PCAF-associated factor 65-alpha;
DE Short=PAF65-alpha;
GN Name=Taf6l {ECO:0000312|MGI:MGI:2444957}; Synonyms=Paf65a;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-549 AND ARG-555, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31005419; DOI=10.1016/j.molcel.2019.03.025;
RA Seruggia D., Oti M., Tripathi P., Canver M.C., LeBlanc L.,
RA Di Giammartino D.C., Bullen M.J., Nefzger C.M., Sun Y.B.Y., Farouni R.,
RA Polo J.M., Pinello L., Apostolou E., Kim J., Orkin S.H., Das P.P.;
RT "TAF5L and TAF6L Maintain Self-Renewal of Embryonic Stem Cells via the MYC
RT Regulatory Network.";
RL Mol. Cell 74:1148.E7-1163.E7(2019).
CC -!- FUNCTION: Functions as a component of the PCAF complex. The PCAF
CC complex is capable of efficiently acetylating histones in a nucleosomal
CC context. The PCAF complex could be considered as the human version of
CC the yeast SAGA complex (By similarity). With TAF5L, acts as an
CC epigenetic regulator essential for somatic reprogramming. Regulates
CC target genes through H3K9ac deposition and MYC recruitment which
CC trigger MYC regulatory network to orchestrate gene expression programs
CC to control embryonic stem cell state (PubMed:31005419). Functions with
CC MYC to activate target gene expression through RNA polymerase II pause
CC release (PubMed:31005419). {ECO:0000250|UniProtKB:Q9Y6J9,
CC ECO:0000269|PubMed:31005419}.
CC -!- SUBUNIT: The PCAF complex is composed of a number of TBP-associated
CC factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and
CC TAF12, PCAF, and also PCAF-associated factors (PAFs), such as
CC TADA2L/ADA2, TADA3L/ADA3 and SPT3 (By similarity). Component of the
CC STAGA transcription coactivator-HAT complex, at least composed of
CC SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12,
CC TRRAP and TAF9. {ECO:0000250|UniProtKB:Q9Y6J9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31005419}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2K4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2K4-2; Sequence=VSP_010158;
CC -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK077149; BAC36645.1; -; mRNA.
DR EMBL; BC028647; AAH28647.1; -; mRNA.
DR RefSeq; NP_001171269.1; NM_001177798.1.
DR RefSeq; NP_666204.2; NM_146092.2.
DR AlphaFoldDB; Q8R2K4; -.
DR SMR; Q8R2K4; -.
DR BioGRID; 230442; 7.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR IntAct; Q8R2K4; 2.
DR MINT; Q8R2K4; -.
DR STRING; 10090.ENSMUSP00000135193; -.
DR iPTMnet; Q8R2K4; -.
DR PhosphoSitePlus; Q8R2K4; -.
DR EPD; Q8R2K4; -.
DR MaxQB; Q8R2K4; -.
DR PaxDb; Q8R2K4; -.
DR PRIDE; Q8R2K4; -.
DR ProteomicsDB; 254813; -. [Q8R2K4-1]
DR ProteomicsDB; 254814; -. [Q8R2K4-2]
DR Antibodypedia; 14977; 235 antibodies from 27 providers.
DR DNASU; 225895; -.
DR Ensembl; ENSMUST00000177056; ENSMUSP00000135028; ENSMUSG00000003680. [Q8R2K4-1]
DR GeneID; 225895; -.
DR KEGG; mmu:225895; -.
DR CTD; 10629; -.
DR MGI; MGI:2444957; Taf6l.
DR VEuPathDB; HostDB:ENSMUSG00000003680; -.
DR eggNOG; KOG2549; Eukaryota.
DR GeneTree; ENSGT00640000091486; -.
DR HOGENOM; CLU_022764_0_0_1; -.
DR InParanoid; Q8R2K4; -.
DR OrthoDB; 384329at2759; -.
DR PhylomeDB; Q8R2K4; -.
DR BioGRID-ORCS; 225895; 22 hits in 76 CRISPR screens.
DR ChiTaRS; Taf6l; mouse.
DR PRO; PR:Q8R2K4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R2K4; protein.
DR Bgee; ENSMUSG00000003680; Expressed in saccule of membranous labyrinth and 206 other tissues.
DR ExpressionAtlas; Q8R2K4; baseline and differential.
DR Genevisible; Q8R2K4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; ISO:MGI.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; 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:0045893; P:positive regulation of transcription, DNA-templated; IC: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:1904672; P:regulation of somatic stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR CDD; cd08050; TAF6C; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.25.40.770; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037796; TAF6.
DR InterPro; IPR011442; TAF6_C.
DR InterPro; IPR046344; TAF6_C_sf.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR PANTHER; PTHR10221; PTHR10221; 1.
DR Pfam; PF02969; TAF; 1.
DR Pfam; PF07571; TAF6_C; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..616
FT /note="TAF6-like RNA polymerase II p300/CBP-associated
FT factor-associated factor 65 kDa subunit 6L"
FT /id="PRO_0000118880"
FT REGION 399..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J9"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J9"
FT MOD_RES 549
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 555
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 587
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J9"
FT VAR_SEQ 179..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010158"
SQ SEQUENCE 616 AA; 67236 MW; 42584DC7F09E75AE CRC64;
MSEREERRFV EIPRESVRLM AESTGLELSD EVAALLAEDV CYRLREATQN SSQFMKHTKR
RKLTVEDFNR ALRWSSVEAV CGYGSQEALP LRPAREGDLY FPEDREVSLV ELALATNIPK
GCAETAVRVH VSYLDGKGNL APQGSVPSAV SSLTDDLLKY YQQVTRAVLG DDPQLMKVAL
QDLQTNSKIA ALLPYFVYVV SGVKSVSHDL EQLHRLLQVA RSLIRNPHLC LGPYVRSLVG
SVLYCVLEPL AASINPLNDH WTLRDGAALL LSHIFWTHGD LVSGLYQQIL LSLQKVLTDP
VRPLCSHYGA VVGLHALGWK AVERVLYPHL PTYWTNLQAV LDDYSVSNAQ VKADGHKVYG
AILVAVERLL KMKAQAAEPN RGGLGGRGYR PAEDLPWDSL LLQESPPGGS SETGFGSGLP
PPSGVAGPED PSSLTLADIY RELYSFFGDS LATRFGTGQP APTAPRPPGD KKEPAAAPDS
VRKMPQLTAS AVVSPQGDES PCGGTLATAT AASESRPLPR VHRARGAPRQ QGPGAGTRDV
FQKSRFAPRG APHFRFIIAG RQAGRRCRGR LFQTAFPAPY GPSPASRYVQ KLPMIGRTGR
PARRWALSDY SLYLPL
