TAF6L_HUMAN
ID TAF6L_HUMAN Reviewed; 622 AA.
AC Q9Y6J9; B2RAT0; Q96HA6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L;
DE Short=TAF6L {ECO:0000305};
DE AltName: Full=PCAF-associated factor 65-alpha;
DE Short=PAF65-alpha;
GN Name=TAF6L {ECO:0000312|HGNC:HGNC:17305}; Synonyms=PAF65A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-14; 62-70; 205-221 AND
RP 577-593, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2;
RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J.,
RA Howard B.H., Qin J., Nakatani Y.;
RT "Histone-like TAFs within the PCAF histone acetylase complex.";
RL Cell 94:35-44(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP REVIEW, AND PCAF COMPLEX COMPOSITION.
RX PubMed=9674419; DOI=10.1016/s0092-8674(00)81213-1;
RA Struhl K., Moqtaderi Z.;
RT "The TAFs in the HAT.";
RL Cell 94:1-4(1998).
RN [5]
RP IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [6]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12601814; DOI=10.1002/pmic.200390030;
RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
RT "Novel subunits of the TATA binding protein free TAFII-containing
RT transcription complex identified by matrix-assisted laser
RT desorption/ionization-time of flight mass spectrometry following one-
RT dimensional gel electrophoresis.";
RL Proteomics 3:217-223(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-555; ARG-561 AND ARG-593, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
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 (Probable). With TAF5L, acts as an epigenetic
CC regulator essential for somatic reprogramming. Regulates target genes
CC through H3K9ac deposition and MYC recruitment which trigger MYC
CC regulatory network to orchestrate gene expression programs to control
CC embryonic stem cell state. Functions with MYC to activate target gene
CC expression through RNA polymerase II pause release (By similarity).
CC {ECO:0000250|UniProtKB:Q8R2K4, ECO:0000305|PubMed:9674419}.
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. Component of the STAGA transcription
CC coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L,
CC TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9.
CC {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:12601814,
CC ECO:0000269|PubMed:9674425}.
CC -!- INTERACTION:
CC Q9Y6J9; Q99471: PFDN5; NbExp=3; IntAct=EBI-743984, EBI-357275;
CC Q9Y6J9; Q16594: TAF9; NbExp=9; IntAct=EBI-743984, EBI-712521;
CC Q9Y6J9; Q9HBM6: TAF9B; NbExp=10; IntAct=EBI-743984, EBI-751601;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9674425}.
CC -!- SIMILARITY: Belongs to the TAF6 family. {ECO:0000305}.
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DR EMBL; AF069735; AAC39905.1; -; mRNA.
DR EMBL; AK314330; BAG36977.1; -; mRNA.
DR EMBL; CH471076; EAW74093.1; -; Genomic_DNA.
DR CCDS; CCDS8035.1; -.
DR RefSeq; NP_006464.1; NM_006473.3.
DR PDB; 7KTR; EM; 2.93 A; F=1-622.
DR PDB; 7KTS; EM; 19.09 A; F=1-622.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; Q9Y6J9; -.
DR SMR; Q9Y6J9; -.
DR BioGRID; 115873; 105.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; Q9Y6J9; -.
DR IntAct; Q9Y6J9; 40.
DR MINT; Q9Y6J9; -.
DR STRING; 9606.ENSP00000294168; -.
DR iPTMnet; Q9Y6J9; -.
DR PhosphoSitePlus; Q9Y6J9; -.
DR BioMuta; TAF6L; -.
DR DMDM; 46577572; -.
DR EPD; Q9Y6J9; -.
DR jPOST; Q9Y6J9; -.
DR MassIVE; Q9Y6J9; -.
DR MaxQB; Q9Y6J9; -.
DR PaxDb; Q9Y6J9; -.
DR PeptideAtlas; Q9Y6J9; -.
DR PRIDE; Q9Y6J9; -.
DR ProteomicsDB; 86707; -.
DR Antibodypedia; 14977; 235 antibodies from 27 providers.
DR DNASU; 10629; -.
DR Ensembl; ENST00000294168.8; ENSP00000294168.3; ENSG00000162227.8.
DR GeneID; 10629; -.
DR KEGG; hsa:10629; -.
DR MANE-Select; ENST00000294168.8; ENSP00000294168.3; NM_006473.4; NP_006464.1.
DR UCSC; uc001nvc.4; human.
DR CTD; 10629; -.
DR GeneCards; TAF6L; -.
DR HGNC; HGNC:17305; TAF6L.
DR HPA; ENSG00000162227; Low tissue specificity.
DR MIM; 602946; gene.
DR neXtProt; NX_Q9Y6J9; -.
DR OpenTargets; ENSG00000162227; -.
DR PharmGKB; PA38224; -.
DR VEuPathDB; HostDB:ENSG00000162227; -.
DR eggNOG; KOG2549; Eukaryota.
DR GeneTree; ENSGT00640000091486; -.
DR HOGENOM; CLU_022764_0_0_1; -.
DR InParanoid; Q9Y6J9; -.
DR OMA; LYFQEDR; -.
DR OrthoDB; 384329at2759; -.
DR PhylomeDB; Q9Y6J9; -.
DR TreeFam; TF328731; -.
DR PathwayCommons; Q9Y6J9; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9Y6J9; -.
DR BioGRID-ORCS; 10629; 240 hits in 1086 CRISPR screens.
DR ChiTaRS; TAF6L; human.
DR GeneWiki; TAF6L; -.
DR GenomeRNAi; 10629; -.
DR Pharos; Q9Y6J9; Tdark.
DR PRO; PR:Q9Y6J9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y6J9; protein.
DR Bgee; ENSG00000162227; Expressed in metanephros cortex and 105 other tissues.
DR ExpressionAtlas; Q9Y6J9; baseline and differential.
DR Genevisible; Q9Y6J9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
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:0003677; F:DNA binding; TAS:ProtInc.
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; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
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; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS: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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..622
FT /note="TAF6-like RNA polymerase II p300/CBP-associated
FT factor-associated factor 65 kDa subunit 6L"
FT /id="PRO_0000118879"
FT REGION 403..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 555
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 561
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 593
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 30..56
FT /evidence="ECO:0007829|PDB:7KTR"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 622 AA; 67814 MW; F294E71AF7D4C8C3 CRC64;
MSEREERRFV EIPRESVRLM AESTGLELSD EVAALLAEDV CYRLREATQN SSQFMKHTKR
RKLTVEDFNR ALRWSSVEAV CGYGSQEALP MRPAREGELY FPEDREVNLV ELALATNIPK
GCAETAVRVH VSYLDGKGNL APQGSVPSAV SSLTDDLLKY YHQVTRAVLG DDPQLMKVAL
QDLQTNSKIG ALLPYFVYVV SGVKSVSHDL EQLHRLLQVA RSLFRNPHLC LGPYVRCLVG
SVLYCVLEPL AASINPLNDH WTLRDGAALL LSHIFWTHGD LVSGLYQHIL LSLQKILADP
VRPLCCHYGA VVGLHALGWK AVERVLYPHL STYWTNLQAV LDDYSVSNAQ VKADGHKVYG
AILVAVERLL KMKAQAAEPN RGGPGGRGCR RLDDLPWDSL LFQESSSGGG AEPSFGSGLP
LPPGGAGPED PSLSVTLADI YRELYAFFGD SLATRFGTGQ PAPTAPRPPG DKKEPAAAPD
SVRKMPQLTA SAIVSPHGDE SPRGSGGGGP ASASGPAASE SRPLPRVHRA RGAPRQQGPG
TGTRDVFQKS RFAPRGAPHF RFIIAGRQAG RRCRGRLFQT AFPAPYGPSP ASRYVQKLPM
IGRTSRPARR WALSDYSLYL PL
