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Transcriptional adapter 3 (ADA3 homolog) (hADA3) (STAF54) (Transcriptional adapter 3-like) (ADA3-like protein)

 TADA3_HUMAN             Reviewed;         432 AA.
O75528; Q6FI83; Q9UFS2;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 153.
RecName: Full=Transcriptional adapter 3;
AltName: Full=ADA3 homolog;
Short=hADA3;
AltName: Full=STAF54;
AltName: Full=Transcriptional adapter 3-like;
Short=ADA3-like protein;
Name=TADA3; Synonyms=ADA3, TADA3L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH PCAF; TAF5L; TAF6L; TAF9; TAF10 AND TAF12.
PubMed=9674425; DOI=10.1016/S0092-8674(00)81219-2;
Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T.,
Yang X.-J., Howard B.H., Qin J., Nakatani Y.;
"Histone-like TAFs within the PCAF histone acetylase complex.";
Cell 94:35-44(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Muscle, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
Kundu T.K., Chait B.T., Roeder R.G.;
"Human STAGA complex is a chromatin-acetylating transcription
coactivator that interacts with pre-mRNA splicing and DNA damage-
binding factors in vivo.";
Mol. Cell. Biol. 21:6782-6795(2001).
[8]
INTERACTION WITH TP53 AND THE HIGH-RISK HPV ONCOPROTEIN E6.
PubMed=12138191; DOI=10.1128/MCB.22.16.5801-5812.2002;
Kumar A., Zhao Y., Meng G., Zeng M., Srinivasan S., Delmolino L.M.,
Gao Q., Dimri G., Weber G.F., Wazer D.E., Band H., Band V.;
"Human papillomavirus oncoprotein E6 inactivates the transcriptional
coactivator human ADA3.";
Mol. Cell. Biol. 22:5801-5812(2002).
[9]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=11707411; DOI=10.1093/emboj/20.22.6404;
Wang T., Kobayashi T., Takimoto R., Denes A.E., Snyder E.L.,
el-Deiry W.S., Brachmann R.K.;
"hADA3 is required for p53 activity.";
EMBO J. 20:6404-6413(2001).
[10]
REVIEW, AND PCAF COMPLEX COMPOSITION.
PubMed=9674419; DOI=10.1016/S0092-8674(00)81213-1;
Struhl K., Moqtaderi Z.;
"The TAFs in the HAT.";
Cell 94:1-4(1998).
[11]
IDENTIFICATION IN THE TFTC-HAT COMPLEX.
PubMed=12601814; DOI=10.1002/pmic.200390030;
Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
"Novel subunits of the TATA binding protein free TAFII-containing
transcription complex identified by matrix-assisted laser
desorption/ionization-time of flight mass spectrometry following one-
dimensional gel electrophoresis.";
Proteomics 3:217-223(2003).
[12]
FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
PubMed=19103755; DOI=10.1128/MCB.01599-08;
Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
Lill J.R., Zha J.;
"The double-histone-acetyltransferase complex ATAC is essential for
mammalian development.";
Mol. Cell. Biol. 29:1176-1188(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-298, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-129, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Functions as a component of the PCAF complex. The PCAF
complex is capable of efficiently acetylating histones in a
nucleosomal context. The PCAF complex could be considered as the
human version of the yeast SAGA complex. Also known as a
coactivator for p53/TP53-dependent transcriptional activation.
Component of the ATAC complex, a complex with histone
acetyltransferase activity on histones H3 and H4.
{ECO:0000269|PubMed:11707411, ECO:0000269|PubMed:19103755}.
-!- SUBUNIT: The PCAF complex is composed of a number of TBP-
associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9,
TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs),
such as TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with
TADA2L and PCAF and also with the high-risk HPV oncoprotein E6.
Component of the STAGA transcription coactivator-HAT complex, at
least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L,
TAD1L, TAF10, TAF12, TRRAP and TAF9. Component of the TFTC-HAT
complex. Component of the ADA2A-containing complex (ATAC),
composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2,
CCDC101 and DR1. {ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:11707411, ECO:0000269|PubMed:12138191,
ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:19103755,
ECO:0000269|PubMed:9674425}.
-!- INTERACTION:
P24863:CCNC; NbExp=3; IntAct=EBI-473249, EBI-395261;
Q96MH2:HEXIM2; NbExp=3; IntAct=EBI-473249, EBI-5460660;
Q8N2W9:PIAS4; NbExp=2; IntAct=EBI-473249, EBI-473160;
P28702-3:RXRB; NbExp=3; IntAct=EBI-473249, EBI-16429492;
Q96ES7:SGF29; NbExp=9; IntAct=EBI-473249, EBI-743117;
P45974:USP5; NbExp=2; IntAct=EBI-473249, EBI-741277;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
ECO:0000269|PubMed:9674425}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75528-1; Sequence=Displayed;
Name=2;
IsoId=O75528-2; Sequence=VSP_009739;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- SIMILARITY: Belongs to the NGG1 family. {ECO:0000305}.
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EMBL; AF069733; AAC39903.1; -; mRNA.
EMBL; AL117487; CAB55957.1; -; mRNA.
EMBL; AK000228; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR533543; CAG38574.1; -; mRNA.
EMBL; CH471055; EAW63994.1; -; Genomic_DNA.
EMBL; BC009240; AAH09240.1; -; mRNA.
EMBL; BC013433; AAH13433.1; -; mRNA.
CCDS; CCDS2583.1; -. [O75528-1]
CCDS; CCDS2584.1; -. [O75528-2]
PIR; T17267; T17267.
RefSeq; NP_001265199.1; NM_001278270.1. [O75528-1]
RefSeq; NP_006345.1; NM_006354.3. [O75528-1]
RefSeq; NP_597814.1; NM_133480.2. [O75528-2]
UniGene; Hs.386390; -.
ProteinModelPortal; O75528; -.
SMR; O75528; -.
BioGrid; 115737; 69.
CORUM; O75528; -.
IntAct; O75528; 36.
MINT; O75528; -.
STRING; 9606.ENSP00000307684; -.
iPTMnet; O75528; -.
PhosphoSitePlus; O75528; -.
EPD; O75528; -.
MaxQB; O75528; -.
PaxDb; O75528; -.
PeptideAtlas; O75528; -.
PRIDE; O75528; -.
DNASU; 10474; -.
Ensembl; ENST00000301964; ENSP00000307684; ENSG00000171148. [O75528-1]
Ensembl; ENST00000343450; ENSP00000343649; ENSG00000171148. [O75528-2]
Ensembl; ENST00000440161; ENSP00000393471; ENSG00000171148. [O75528-1]
GeneID; 10474; -.
KEGG; hsa:10474; -.
UCSC; uc003bsx.3; human. [O75528-1]
CTD; 10474; -.
DisGeNET; 10474; -.
EuPathDB; HostDB:ENSG00000171148.13; -.
GeneCards; TADA3; -.
HGNC; HGNC:19422; TADA3.
HPA; HPA042250; -.
MIM; 602945; gene.
neXtProt; NX_O75528; -.
OpenTargets; ENSG00000171148; -.
PharmGKB; PA165698494; -.
eggNOG; KOG4191; Eukaryota.
eggNOG; ENOG410XQUH; LUCA.
GeneTree; ENSGT00390000008947; -.
HOGENOM; HOG000007362; -.
HOVERGEN; HBG055283; -.
InParanoid; O75528; -.
KO; K11315; -.
OMA; PNKFWAS; -.
OrthoDB; EOG091G0DWR; -.
PhylomeDB; O75528; -.
TreeFam; TF323397; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; TADA3; human.
GeneWiki; TADA3L; -.
GenomeRNAi; 10474; -.
PRO; PR:O75528; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000171148; -.
CleanEx; HS_TADA3L; -.
ExpressionAtlas; O75528; baseline and differential.
Genevisible; O75528; HS.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; TAS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0031063; P:regulation of histone deacetylation; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR019340; Histone_AcTrfase_su3.
PANTHER; PTHR13556; PTHR13556; 2.
Pfam; PF10198; Ada3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 432 Transcriptional adapter 3.
/FTId=PRO_0000072416.
COILED 40 69 {ECO:0000255}.
COILED 367 407 {ECO:0000255}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 418 418 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 370 432 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_009739.
CONFLICT 168 168 E -> G (in Ref. 3; AK000228).
{ECO:0000305}.
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


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