TAD2A_HUMAN
ID TAD2A_HUMAN Reviewed; 443 AA.
AC O75478; A8MVD0; B3KMU9; Q9BVJ0; Q9UCW2; Q9UP49;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Transcriptional adapter 2-alpha;
DE AltName: Full=Transcriptional adapter 2-like;
DE Short=ADA2-like protein;
GN Name=TADA2A; Synonyms=TADA2L; ORFNames=KL04P;
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), CHARACTERIZATION, AND VARIANT
RP SER-6.
RC TISSUE=Testis;
RX PubMed=8552087; DOI=10.1128/mcb.16.2.593;
RA Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A.,
RA Berger S.L.;
RT "Identification of human proteins functionally conserved with the yeast
RT putative adaptors ADA2 and GCN5.";
RL Mol. Cell. Biol. 16:593-602(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-6.
RC TISSUE=Dendritic cell;
RA Huang X., Li N., Zhao Z., Zhu X., Cao X.;
RT "A novel gene from human dendritic cell.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-6 AND
RP VAL-115.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-6.
RC TISSUE=Eye, and Muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-443, 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 [7]
RP INTERACTION WITH NR3C1.
RX PubMed=9154805; DOI=10.1128/mcb.17.6.3065;
RA Henriksson A., Almloef T., Ford J., McEwan I.J., Gustafsson J.-A.,
RA Wright A.P.H.;
RT "Role of the Ada adaptor complex in gene activation by the glucocorticoid
RT receptor.";
RL Mol. Cell. Biol. 17:3065-3073(1997).
RN [8]
RP IDENTIFICATION IN THE PCAF COMPLEX WITH TRRAP; TADA3L; TAF5L; SUPT3H;
RP TAF6L; TAF10; TAF12 AND TAF9.
RX PubMed=9885574; DOI=10.1016/s1097-2765(00)80301-9;
RA Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J.,
RA Nakatani Y.;
RT "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the
RT ATM superfamily.";
RL Mol. Cell 2:869-875(1998).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [10]
RP FUNCTION, INTERACTION WITH CCDC134, AND SUBCELLULAR LOCATION.
RX PubMed=22644376; DOI=10.1007/s00418-012-0932-5;
RA Huang J., Zhang L., Liu W., Liao Q., Shi T., Xiao L., Hu F., Qiu X.;
RT "CCDC134 interacts with hADA2a and functions as a regulator of hADA2a in
RT acetyltransferase activity, DNA damage-induced apoptosis and cell cycle
RT arrest.";
RL Histochem. Cell Biol. 138:41-55(2012).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP STRUCTURE BY NMR OF 72-118.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Myb-like DNA binding domain of human
RT transcriptional adaptor 2-like, isoform B.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 (VARIANT SER-6), VARIANT
RP [LARGE SCALE ANALYSIS] SER-6, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4. Required for the
CC function of some acidic activation domains, which activate
CC transcription from a distant site (By similarity). Binds double-
CC stranded DNA. Binds dinucleosomes, probably at the linker region
CC between neighboring nucleosomes. Plays a role in chromatin remodeling.
CC May promote TP53/p53 'Lys-321' acetylation, leading to reduced TP53
CC stability and transcriptional activity (PubMed:22644376). May also
CC promote XRCC6 acetylation thus facilitating cell apoptosis in response
CC to DNA damage (PubMed:22644376). {ECO:0000250|UniProtKB:Q8CHV6,
CC ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:22644376}.
CC -!- SUBUNIT: Interacts with GCN5 and NR3C1. Associated with the P/CAF
CC protein in the PCAF complex. Component of the PCAF complex, at least
CC composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-
CC alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component
CC of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A,
CC TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. Interacts
CC with CCDC134 (PubMed:22644376). {ECO:0000269|PubMed:19103755,
CC ECO:0000269|PubMed:22644376, ECO:0000269|PubMed:9154805,
CC ECO:0000269|PubMed:9885574}.
CC -!- INTERACTION:
CC O75478; Q9NY61: AATF; NbExp=4; IntAct=EBI-742268, EBI-372428;
CC O75478; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-742268, EBI-8643161;
CC O75478; Q8IYX3: CCDC116; NbExp=5; IntAct=EBI-742268, EBI-744311;
CC O75478; Q9H6E4: CCDC134; NbExp=6; IntAct=EBI-742268, EBI-953766;
CC O75478; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-742268, EBI-10175300;
CC O75478; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-742268, EBI-5278764;
CC O75478; O60573: EIF4E2; NbExp=3; IntAct=EBI-742268, EBI-398610;
CC O75478; A0A0S2Z3R2: FANCG; NbExp=3; IntAct=EBI-742268, EBI-16438045;
CC O75478; A0A0S2Z4A7: FANCG; NbExp=3; IntAct=EBI-742268, EBI-16433879;
CC O75478; O95363: FARS2; NbExp=3; IntAct=EBI-742268, EBI-2513774;
CC O75478; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-742268, EBI-10244131;
CC O75478; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-742268, EBI-347538;
CC O75478; O14964: HGS; NbExp=4; IntAct=EBI-742268, EBI-740220;
CC O75478; Q9NSK0: KLC4; NbExp=3; IntAct=EBI-742268, EBI-949319;
CC O75478; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-742268, EBI-6426443;
CC O75478; P52292: KPNA2; NbExp=3; IntAct=EBI-742268, EBI-349938;
CC O75478; P25800: LMO1; NbExp=3; IntAct=EBI-742268, EBI-8639312;
CC O75478; P61326: MAGOH; NbExp=3; IntAct=EBI-742268, EBI-299134;
CC O75478; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-742268, EBI-746778;
CC O75478; P55081: MFAP1; NbExp=3; IntAct=EBI-742268, EBI-1048159;
CC O75478; Q13064: MKRN3; NbExp=3; IntAct=EBI-742268, EBI-2340269;
CC O75478; O75431: MTX2; NbExp=3; IntAct=EBI-742268, EBI-7415268;
CC O75478; Q16236: NFE2L2; NbExp=2; IntAct=EBI-742268, EBI-2007911;
CC O75478; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-742268, EBI-10293968;
CC O75478; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-742268, EBI-1567797;
CC O75478; P47897: QARS1; NbExp=3; IntAct=EBI-742268, EBI-347462;
CC O75478; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-742268, EBI-16428950;
CC O75478; Q17RB0: RTL8B; NbExp=3; IntAct=EBI-742268, EBI-10238588;
CC O75478; Q12874: SF3A3; NbExp=3; IntAct=EBI-742268, EBI-1051880;
CC O75478; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-742268, EBI-750487;
CC O75478; Q96FV9: THOC1; NbExp=3; IntAct=EBI-742268, EBI-1765605;
CC O75478; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-742268, EBI-6447954;
CC O75478; Q8N5M4: TTC9C; NbExp=3; IntAct=EBI-742268, EBI-2851213;
CC O75478; Q9BRG1: VPS25; NbExp=3; IntAct=EBI-742268, EBI-741945;
CC O75478; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-742268, EBI-748373;
CC O75478; Q68DK2-5: ZFYVE26; NbExp=3; IntAct=EBI-742268, EBI-8656416;
CC O75478; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-742268, EBI-740727;
CC O75478; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-742268, EBI-10273713;
CC O75478; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-742268, EBI-16429014;
CC O75478; Q5W150; NbExp=3; IntAct=EBI-742268, EBI-10248148;
CC O75478-2; O14964: HGS; NbExp=3; IntAct=EBI-16433586, EBI-740220;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22644376}. Chromosome
CC {ECO:0000250|UniProtKB:Q8CHV6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75478-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75478-2; Sequence=VSP_040347, VSP_040348;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues, but most abundantly in
CC testis.
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DR EMBL; AF064094; AAC26659.1; -; mRNA.
DR EMBL; AK022767; BAG51111.1; -; mRNA.
DR EMBL; AC004099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001172; AAH01172.1; -; mRNA.
DR EMBL; BC011753; AAH11753.1; -; mRNA.
DR EMBL; AF069732; AAC39902.1; -; mRNA.
DR CCDS; CCDS11319.1; -. [O75478-1]
DR CCDS; CCDS45656.1; -. [O75478-2]
DR RefSeq; NP_001159577.2; NM_001166105.2.
DR RefSeq; NP_001278847.1; NM_001291918.1.
DR RefSeq; NP_001479.4; NM_001488.4.
DR RefSeq; NP_597683.3; NM_133439.3.
DR PDB; 1X41; NMR; -; A=72-116.
DR PDBsum; 1X41; -.
DR AlphaFoldDB; O75478; -.
DR SMR; O75478; -.
DR BioGRID; 112734; 199.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; O75478; -.
DR DIP; DIP-28151N; -.
DR IntAct; O75478; 69.
DR MINT; O75478; -.
DR STRING; 9606.ENSP00000481091; -.
DR iPTMnet; O75478; -.
DR PhosphoSitePlus; O75478; -.
DR BioMuta; TADA2A; -.
DR EPD; O75478; -.
DR jPOST; O75478; -.
DR MassIVE; O75478; -.
DR MaxQB; O75478; -.
DR PaxDb; O75478; -.
DR PeptideAtlas; O75478; -.
DR PRIDE; O75478; -.
DR ProteomicsDB; 50040; -. [O75478-1]
DR ProteomicsDB; 50041; -. [O75478-2]
DR DNASU; 6871; -.
DR Ensembl; ENST00000617828.4; ENSP00000482484.1; ENSG00000277104.4. [O75478-1]
DR Ensembl; ENST00000622522.2; ENSP00000481283.1; ENSG00000277104.4. [O75478-1]
DR Ensembl; ENST00000633468.1; ENSP00000488016.1; ENSG00000277104.4. [O75478-1]
DR Ensembl; ENST00000633584.1; ENSP00000487973.1; ENSG00000277104.4. [O75478-2]
DR GeneID; 6871; -.
DR KEGG; hsa:6871; -.
DR UCSC; uc032ghw.2; human. [O75478-1]
DR CTD; 6871; -.
DR DisGeNET; 6871; -.
DR GeneCards; TADA2A; -.
DR HGNC; HGNC:11531; TADA2A.
DR MIM; 602276; gene.
DR neXtProt; NX_O75478; -.
DR PharmGKB; PA36306; -.
DR eggNOG; KOG0457; Eukaryota.
DR InParanoid; O75478; -.
DR OrthoDB; 812864at2759; -.
DR PhylomeDB; O75478; -.
DR TreeFam; TF313975; -.
DR PathwayCommons; O75478; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; O75478; -.
DR BioGRID-ORCS; 6871; 234 hits in 1102 CRISPR screens.
DR ChiTaRS; TADA2A; human.
DR EvolutionaryTrace; O75478; -.
DR GeneWiki; TADA2L; -.
DR GenomeRNAi; 6871; -.
DR Pharos; O75478; Tbio.
DR PRO; PR:O75478; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75478; protein.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Transcriptional adapter 2-alpha"
FT /id="PRO_0000197083"
FT DOMAIN 70..122
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 356..443
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 12..69
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT DNA_BIND 426..435
FT /evidence="ECO:0000250"
FT REGION 348..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 6
FT /note="Phosphoserine; in variant Ser-6"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 275..305
FT /note="LEFELRREIKRLQEYRTAGITNFCSARTYDH -> CRWFLSLEQYLCVYIYI
FT NRRDNGVFYVKFYK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040347"
FT VAR_SEQ 306..443
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040348"
FT VARIANT 6
FT /note="P -> S (in dbSNP:rs7211875)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8552087,
FT ECO:0000269|Ref.2, ECO:0007744|PubMed:23186163"
FT /id="VAR_047466"
FT VARIANT 115
FT /note="M -> V (in dbSNP:rs1054865)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_047467"
FT VARIANT 351
FT /note="I -> M (in dbSNP:rs2522969)"
FT /id="VAR_047468"
FT CONFLICT 117
FT /note="H -> Y (in Ref. 5; AAH01172)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> L (in Ref. 6; AAC39902)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="W -> R (in Ref. 2; AAC26659)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="D -> N (in Ref. 2; AAC26659)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="D -> G (in Ref. 2; AAC26659)"
FT /evidence="ECO:0000305"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1X41"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1X41"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1X41"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1X41"
SQ SEQUENCE 443 AA; 51506 MW; A4E1D87B1B3F6BA5 CRC64;
MDRLGPFSND PSDKPPCRGC SSYLMEPYIK CAECGPPPFF LCLQCFTRGF EYKKHQSDHT
YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN QMCTKTKEEC EKHYMKHFIN
NPLFASTLLN LKQAEEAKTA DTAIPFHSTD DPPRPTFDSL LSRDMAGYMP ARADFIEEFD
NYAEWDLRDI DFVEDDSDIL HALKMAVVDI YHSRLKERQR RKKIIRDHGL INLRKFQLME
RRYPKEVQDL YETMRRFARI VGPVEHDKFI ESHALEFELR REIKRLQEYR TAGITNFCSA
RTYDHLKKTR EEERLKRTML SEVLQYIQDS SACQQWLRRQ ADIDSGLSPS IPMASNSGRR
SAPPLNLTGL PGTEKLNEKE KELCQMVRLV PGAYLEYKSA LLNECNKQGG LRLAQARALI
KIDVNKTRKI YDFLIREGYI TKG
