ID TAF5L_HUMAN Reviewed; 589 AA. AC O75529; Q5TDI5; Q5TDI6; Q8IW31; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 10-FEB-2021, entry version 182. DE RecName: Full=TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L {ECO:0000305}; DE Short=TAF5L {ECO:0000305}; DE AltName: Full=PCAF-associated factor 65 beta; DE Short=PAF65-beta; GN Name=TAF5L {ECO:0000312|HGNC:HGNC:17304}; Synonyms=PAF65B; 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] (ISOFORM 1), PROTEIN SEQUENCE OF 123-134 AND RP 167-177, 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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 330-589 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11124703; RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h; RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., RA Zimbello R., Lanfranchi G., Valle G.; RT "Characterization of 16 novel human genes showing high similarity to yeast RT sequences."; RL Yeast 18:69-80(2001). RN [6] 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 [7] 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 [8] 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). 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 TAF6L, 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 (By similarity). CC {ECO:0000250|UniProtKB:Q91WQ5, 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 O75529; O43524: FOXO3; NbExp=2; IntAct=EBI-1785876, EBI-1644164; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, CC ECO:0000269|PubMed:9674425}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75529-1; Sequence=Displayed; CC Name=2; CC IsoId=O75529-2; Sequence=VSP_010156, VSP_010157; CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the WD repeat TAF5 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; AF069736; AAC39906.1; -; mRNA. DR EMBL; AL121990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW69902.1; -; Genomic_DNA. DR EMBL; CH471098; EAW69903.1; -; Genomic_DNA. DR EMBL; BC041094; AAH41094.1; -; mRNA. DR EMBL; AJ009770; CAA08816.1; -; mRNA. DR CCDS; CCDS1581.1; -. [O75529-1] DR CCDS; CCDS31051.1; -. [O75529-2] DR RefSeq; NP_001020418.1; NM_001025247.1. [O75529-2] DR RefSeq; NP_055224.1; NM_014409.3. [O75529-1] DR RefSeq; XP_005273156.1; XM_005273099.4. [O75529-1] DR BioGRID; 117998; 53. DR ComplexPortal; CPX-900; SAGA complex. DR ComplexPortal; CPX-903; TFTC histone acetylation complex. DR ComplexPortal; CPX-989; PCAF histone acetylase complex. DR CORUM; O75529; -. DR DIP; DIP-28147N; -. DR IntAct; O75529; 30. DR MINT; O75529; -. DR STRING; 9606.ENSP00000258281; -. DR iPTMnet; O75529; -. DR PhosphoSitePlus; O75529; -. DR BioMuta; TAF5L; -. DR EPD; O75529; -. DR jPOST; O75529; -. DR MassIVE; O75529; -. DR MaxQB; O75529; -. DR PaxDb; O75529; -. DR PeptideAtlas; O75529; -. DR PRIDE; O75529; -. DR ProteomicsDB; 50066; -. [O75529-1] DR ProteomicsDB; 50067; -. [O75529-2] DR Antibodypedia; 20789; 210 antibodies. DR DNASU; 27097; -. DR Ensembl; ENST00000258281; ENSP00000258281; ENSG00000135801. [O75529-1] DR Ensembl; ENST00000366675; ENSP00000355635; ENSG00000135801. [O75529-2] DR Ensembl; ENST00000366676; ENSP00000355636; ENSG00000135801. [O75529-1] DR GeneID; 27097; -. DR KEGG; hsa:27097; -. DR UCSC; uc001htq.5; human. [O75529-1] DR CTD; 27097; -. DR DisGeNET; 27097; -. DR GeneCards; TAF5L; -. DR HGNC; HGNC:17304; TAF5L. DR HPA; ENSG00000135801; Low tissue specificity. DR neXtProt; NX_O75529; -. DR OpenTargets; ENSG00000135801; -. DR PharmGKB; PA38223; -. DR VEuPathDB; HostDB:ENSG00000135801.9; -. DR eggNOG; KOG0263; Eukaryota. DR GeneTree; ENSGT00940000153342; -. DR HOGENOM; CLU_005884_3_0_1; -. DR InParanoid; O75529; -. DR OMA; CLAEPQQ; -. DR OrthoDB; 620721at2759; -. DR PhylomeDB; O75529; -. DR TreeFam; TF300669; -. DR PathwayCommons; O75529; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; O75529; -. DR BioGRID-ORCS; 27097; 141 hits in 886 CRISPR screens. DR ChiTaRS; TAF5L; human. DR GeneWiki; TAF5L; -. DR GenomeRNAi; 27097; -. DR Pharos; O75529; Tbio. DR PRO; PR:O75529; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O75529; protein. DR Bgee; ENSG00000135801; Expressed in thoracic aorta and 217 other tissues. DR ExpressionAtlas; O75529; baseline and differential. DR Genevisible; O75529; HS. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA. DR GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030914; C:STAGA complex; IDA:UniProtKB. DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB. DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd08044; TAF5_NTD2; 1. DR Gene3D; 1.25.40.500; -; 1. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR037783; Taf5. DR InterPro; IPR037826; TAF5L. 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; IPR017986; WD40_repeat_dom. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR19879; PTHR19879; 1. DR PANTHER; PTHR19879:SF6; PTHR19879:SF6; 1. DR Pfam; PF04494; TFIID_NTD2; 1. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF160897; SSF160897; 1. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW WD repeat. FT CHAIN 1..589 FT /note="TAF5-like RNA polymerase II p300/CBP-associated FT factor-associated factor 65 kDa subunit 5L" FT /id="PRO_0000051261" FT REPEAT 266..305 FT /note="WD 1" FT REPEAT 340..379 FT /note="WD 2" FT REPEAT 382..421 FT /note="WD 3" FT REPEAT 424..463 FT /note="WD 4" FT REPEAT 466..505 FT /note="WD 5" FT REPEAT 508..547 FT /note="WD 6" FT VAR_SEQ 325 FT /note="D -> V (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010156" FT VAR_SEQ 326..589 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010157" SQ SEQUENCE 589 AA; 66155 MW; BBF0A1CDD17EE22E CRC64; MKRVRTEQIQ MAVSCYLKRR QYVDSDGPLK QGLRLSQTAE EMAANLTVQS ESGCANIVSA APCQAEPQQY EVQFGRLRNF LTDSDSQHSH EVMPLLYPLF VYLHLNLVQN SPKSTVESFY SRFHGMFLQN ASQKDVIEQL QTTQTIQDIL SNFKLRAFLD NKYVVRLQED SYNYLIRYLQ SDNNTALCKV LTLHIHLDVQ PAKRTDYQLY ASGSSSRSEN NGLEPPDMPS PILQNEAALE VLQESIKRVK DGPPSLTTIC FYAFYNTEQL LNTAEISPDS KLLAAGFDNS CIKLWSLRSK KLKSEPHQVD VSRIHLACDI LEEEDDEDDN AGTEMKILRG HCGPVYSTRF LADSSGLLSC SEDMSIRYWD LGSFTNTVLY QGHAYPVWDL DISPYSLYFA SGSHDRTARL WSFDRTYPLR IYAGHLADVD CVKFHPNSNY LATGSTDKTV RLWSAQQGNS VRLFTGHRGP VLSLAFSPNG KYLASAGEDQ RLKLWDLASG TLYKELRGHT DNITSLTFSP DSGLIASASM DNSVRVWDIR NTYCSAPADG SSSELVGVYT GQMSNVLSVQ FMACNLLLVT GITQENQEH //