ID TAD3L_HUMAN Reviewed; 432 AA. AC O75528; Q9UFS2; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 28-JUL-2009, entry version 70. DE RecName: Full=Transcriptional adapter 3-like; DE Short=ADA3-like protein; DE AltName: Full=ADA3 homolog; DE Short=hADA3; DE AltName: Full=STAF54; GN Name=TADA3L; Synonyms=ADA3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP INTERACTION WITH PCAF; TAF5L; TAF6L; TAF9; TAF10 AND TAF12. RX MEDLINE=98337182; PubMed=9674425; DOI=10.1016/S0092-8674(00)81219-2; RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., RA Yang X.-J., 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] (ISOFORM 2). RC TISSUE=Testis; RX MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon mucosa; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Muscle, and Pancreas; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND MASS RP SPECTROMETRY. RX MEDLINE=21448975; PubMed=11564863; RX 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 RT coactivator that interacts with pre-mRNA splicing and DNA damage- RT binding factors in vivo."; RL Mol. Cell. Biol. 21:6782-6795(2001). RN [6] RP INTERACTION WITH TP53 AND THE HIGH-RISK HPV ONCOPROTEIN E6. RX MEDLINE=22133594; PubMed=12138191; RX DOI=10.1128/MCB.22.16.5801-5812.2002; RA Kumar A., Zhao Y., Meng G., Zeng M., Srinivasan S., Delmolino L.M., RA Gao Q., Dimri G., Weber G.F., Wazer D.E., Band H., Band V.; RT "Human papillomavirus oncoprotein E6 inactivates the transcriptional RT coactivator human ADA3."; RL Mol. Cell. Biol. 22:5801-5812(2002). RN [7] RP FUNCTION, AND INTERACTION WITH TP53. RX MEDLINE=21564072; PubMed=11707411; DOI=10.1093/emboj/20.22.6404; RA Wang T., Kobayashi T., Takimoto R., Denes A.E., Snyder E.L., RA el-Deiry W.S., Brachmann R.K.; RT "hADA3 is required for p53 activity."; RL EMBO J. 20:6404-6413(2001). RN [8] RP REVIEW, AND PCAF COMPLEX COMPOSITION. RX MEDLINE=98337176; 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 [9] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX. 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 CC nucleosomal context. The PCAF complex could be considered as the CC human version of the yeast SAGA complex. Also known as a CC coactivator for p53/TP53-dependent transcriptional activation. CC -!- SUBUNIT: The PCAF complex is composed of a number of TBP- CC associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, CC TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs), CC such as TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with CC TADA2L and PCAF and also with the high-risk HPV oncoprotein E6. CC Component of the STAGA transcription coactivator-HAT complex, at CC least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, CC TAD1L, TAF10, TAF12, TRRAP and TAF9. Component of the TFTC-HAT CC complex. CC -!- INTERACTION: CC Q8N2W9:PIAS4; NbExp=1; IntAct=EBI-473249, EBI-473160; CC P45974:USP5; NbExp=1; IntAct=EBI-473249, EBI-741277; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75528-1; Sequence=Displayed; CC Name=2; CC IsoId=O75528-2; Sequence=VSP_009739; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- SIMILARITY: Belongs to the NGG1 family. 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; AF069733; AAC39903.1; -; mRNA. DR EMBL; AL117487; CAB55957.1; -; mRNA. DR EMBL; AK000228; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC009240; AAH09240.1; -; mRNA. DR EMBL; BC013433; AAH13433.1; -; mRNA. DR IPI; IPI00220486; -. DR IPI; IPI00375534; -. DR PIR; T17267; T17267. DR RefSeq; NP_006345.1; -. DR RefSeq; NP_597814.1; -. DR UniGene; Hs.386390; -. DR IntAct; O75528; 17. DR PhosphoSite; O75528; -. DR PRIDE; O75528; -. DR Ensembl; ENST00000301964; ENSP00000307684; ENSG00000171148; Homo sapiens. DR Ensembl; ENST00000343450; ENSP00000343649; ENSG00000171148; Homo sapiens. DR GeneID; 10474; -. DR KEGG; hsa:10474; -. DR UCSC; uc003bsx.1; human. DR GeneCards; GC03M009796; -. DR HGNC; HGNC:19422; TADA3L. DR MIM; 602945; gene. DR PharmGKB; PA134910395; -. DR HOGENOM; O75528; -. DR HOVERGEN; O75528; -. DR OMA; O75528; GCPFGPL. DR NextBio; 39724; -. DR ArrayExpress; O75528; -. DR Bgee; O75528; -. DR CleanEx; HS_TADA3L; -. DR GermOnline; ENSG00000171148; Homo sapiens. 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:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription from RNA polyme...; TAS:ProtInc. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR019340; Histone_AcTrfase_su3. DR Pfam; PF10198; Ada3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Complete proteome; Nucleus; KW Transcription; Transcription regulation. FT CHAIN 1 432 Transcriptional adapter 3-like. FT /FTId=PRO_0000072416. FT COILED 40 69 Potential. FT COILED 367 407 Potential. FT VAR_SEQ 370 432 Missing (in isoform 2). FT /FTId=VSP_009739. FT CONFLICT 168 168 E -> G (in Ref. 3; AK000228). SQ SEQUENCE 432 AA; 48902 MW; C86153CFA83F9226 CRC64; MSELKDCPLQ FHDFKSVDHL KVCPRYTAVL ARSEDDGIGI EELDTLQLEL ETLLSSASRR LRVLEAETQI LTDWQDKKGD RRFLKLGRDH ELGAPPKHGK PKKQKLEGKA GHGPGPGPGR PKSKNLQPKI QEYEFTDDPI DVPRIPKNDA PNRFWASVEP YCADITSEEV RTLEELLKPP EDEAEHYKIP PLGKHYSQRW AQEDLLEEQK DGARAAAVAD KKKGLMGPLT ELDTKDVDAL LKKSEAQHEQ PEDGCPFGAL TQRLLQALVE ENIISPMEDS PIPDMSGKES GADGASTSPR NQNKPFSVPH TKSLESRIKE ELIAQGLLES EDRPAEDSED EVLAELRKRQ AELKALSAHN RTKKHDLLRL AKEEVSRQEL RQRVRMADNE VMDAFRKIMA ARQKKRTPTK KEKDQAWKTL KERESILKLL DG //