TAD2B_ARATH
ID TAD2B_ARATH Reviewed; 487 AA.
AC Q9ATB4; O23486; Q3EA06; Q3EA07;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcriptional adapter ADA2b;
DE Short=AtADA2b;
DE AltName: Full=Protein PROPORZ 1;
GN Name=ADA2B; Synonyms=PRZ1; OrderedLocusNames=At4g16420; ORFNames=dl4235c;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH GCN5 AND DREB1B/CBF1.
RX PubMed=11266554; DOI=10.1093/nar/29.7.1524;
RA Stockinger E.J., Mao Y., Regier M.K., Triezenberg S.J., Thomashow M.F.;
RT "Transcriptional adaptor and histone acetyltransferase proteins in
RT Arabidopsis and their interactions with CBF1, a transcriptional activator
RT involved in cold-regulated gene expression.";
RL Nucleic Acids Res. 29:1524-1533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION.
RX PubMed=12747832; DOI=10.1016/s0960-9822(03)00327-0;
RA Sieberer T., Hauser M.-T., Seifert G.J., Luschnig C.;
RT "PROPORZ1, a putative Arabidopsis transcriptional adaptor protein, mediates
RT auxin and cytokinin signals in the control of cell proliferation.";
RL Curr. Biol. 13:837-842(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12615937; DOI=10.1105/tpc.007922;
RA Vlachonasios K.E., Thomashow M.F., Triezenberg S.J.;
RT "Disruption mutations of ADA2b and GCN5 transcriptional adaptor genes
RT dramatically affect Arabidopsis growth, development, and gene expression.";
RL Plant Cell 15:626-638(2003).
RN [9]
RP INTERACTION WITH GCN5 AND DREB1B/CBF1, ACETYLATION AT LYS-216,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-216.
RX PubMed=16603259; DOI=10.1016/j.bbaexp.2006.02.006;
RA Mao Y., Pavangadkar K.A., Thomashow M.F., Triezenberg S.J.;
RT "Physical and functional interactions of Arabidopsis ADA2 transcriptional
RT coactivator proteins with the acetyltransferase GCN5 and with the cold-
RT induced transcription factor CBF1.";
RL Biochim. Biophys. Acta 1759:69-79(2006).
RN [10]
RP FUNCTION.
RX PubMed=21193996; DOI=10.1007/s00425-010-1337-0;
RA Kaldis A., Tsementzi D., Tanriverdi O., Vlachonasios K.E.;
RT "Arabidopsis thaliana transcriptional co-activators ADA2b and SGF29a are
RT implicated in salt stress responses.";
RL Planta 233:749-762(2011).
RN [11]
RP INTERACTION WITH BZIP11.
RX PubMed=24861440; DOI=10.1038/ncomms4883;
RA Weiste C., Droege-Laser W.;
RT "The Arabidopsis transcription factor bZIP11 activates auxin-mediated
RT transcription by recruiting the histone acetylation machinery.";
RL Nat. Commun. 5:3883-3883(2014).
CC -!- FUNCTION: Required for the function of some acidic activation domains,
CC which activate transcription from a distant site. The exact mechanism
CC of action is not yet known (By similarity). ADA2 stimulates the
CC acetyltransferase activity of GCN5 on free histones or nucleosomes,
CC probably by opening up the promoter region. Mediates auxin and
CC cytokinin signals in the control of cell proliferation and might be
CC involved in repression of a freezing tolerance pathway at warm
CC temperature (PubMed:12615937, PubMed:12747832). Involved in the
CC positive regulation of salt-induced gene expression by maintaining
CC locus-specific acetylation of histones H4 and H3 (PubMed:21193996).
CC {ECO:0000250, ECO:0000269|PubMed:12615937, ECO:0000269|PubMed:12747832,
CC ECO:0000269|PubMed:21193996}.
CC -!- SUBUNIT: Interacts in vitro with the HAT domain of GCN5 and with the
CC DNA-binding domain of the transcriptional activator DREB1B/CBF1
CC (PubMed:11266554, PubMed:16603259). Interacts with BZIP11
CC (PubMed:24861440). {ECO:0000269|PubMed:11266554,
CC ECO:0000269|PubMed:16603259, ECO:0000269|PubMed:24861440}.
CC -!- INTERACTION:
CC Q9ATB4; Q9FLI3: AHG1; NbExp=3; IntAct=EBI-979237, EBI-2363348;
CC Q9ATB4; A0A178VY90: At2g32840; NbExp=4; IntAct=EBI-979237, EBI-25510857;
CC Q9ATB4; Q9LHI5: At3g12210; NbExp=3; IntAct=EBI-979237, EBI-25520098;
CC Q9ATB4; Q945P2: At5g49210; NbExp=3; IntAct=EBI-979237, EBI-4436601;
CC Q9ATB4; Q9AR19: HAG1; NbExp=5; IntAct=EBI-979237, EBI-979271;
CC Q9ATB4; Q84JZ6: MORF3; NbExp=3; IntAct=EBI-979237, EBI-4465639;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:12747832}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ATB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ATB4-2; Sequence=VSP_022096;
CC Name=3;
CC IsoId=Q9ATB4-3; Sequence=VSP_022095;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques, with the strongest activity in the meristematic zones.
CC {ECO:0000269|PubMed:11266554, ECO:0000269|PubMed:12747832}.
CC -!- DOMAIN: The middle domain of ADA2b is sufficient for interaction with
CC the HAT catalytic domain of GCN5.
CC -!- PTM: Acetylated in vitro by GCN5, but acetylation is not essential for
CC biological activity. {ECO:0000269|PubMed:16603259}.
CC -!- DISRUPTION PHENOTYPE: Plants have pleiotropic effects on plant growth
CC and development, including dwarf size, aberrant root development, and
CC short petals and stamens in flowers. ADA2a cannot rescue any of the
CC mutant phenotypes. {ECO:0000269|PubMed:12615937,
CC ECO:0000269|PubMed:12747832}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78684.1; Type=Erroneous gene model prediction; Evidence={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; AF338770; AAK31320.1; -; mRNA.
DR EMBL; Z97341; CAB10418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161544; CAB78684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83744.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83745.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83746.1; -; Genomic_DNA.
DR EMBL; AY143911; AAN28850.1; -; mRNA.
DR EMBL; AY050348; AAK91365.1; -; mRNA.
DR EMBL; BX827435; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX827480; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H71430; H71430.
DR RefSeq; NP_567495.1; NM_117737.5. [Q9ATB4-1]
DR RefSeq; NP_974560.1; NM_202831.3. [Q9ATB4-2]
DR RefSeq; NP_974561.1; NM_202832.2. [Q9ATB4-3]
DR AlphaFoldDB; Q9ATB4; -.
DR SMR; Q9ATB4; -.
DR BioGRID; 12629; 12.
DR IntAct; Q9ATB4; 7.
DR STRING; 3702.AT4G16420.1; -.
DR iPTMnet; Q9ATB4; -.
DR PaxDb; Q9ATB4; -.
DR PRIDE; Q9ATB4; -.
DR ProteomicsDB; 233000; -. [Q9ATB4-1]
DR EnsemblPlants; AT4G16420.1; AT4G16420.1; AT4G16420. [Q9ATB4-1]
DR EnsemblPlants; AT4G16420.2; AT4G16420.2; AT4G16420. [Q9ATB4-2]
DR EnsemblPlants; AT4G16420.3; AT4G16420.3; AT4G16420. [Q9ATB4-3]
DR GeneID; 827336; -.
DR Gramene; AT4G16420.1; AT4G16420.1; AT4G16420. [Q9ATB4-1]
DR Gramene; AT4G16420.2; AT4G16420.2; AT4G16420. [Q9ATB4-2]
DR Gramene; AT4G16420.3; AT4G16420.3; AT4G16420. [Q9ATB4-3]
DR KEGG; ath:AT4G16420; -.
DR Araport; AT4G16420; -.
DR TAIR; locus:2130609; AT4G16420.
DR eggNOG; KOG0457; Eukaryota.
DR InParanoid; Q9ATB4; -.
DR OMA; EFETEYF; -.
DR OrthoDB; 812864at2759; -.
DR PhylomeDB; Q9ATB4; -.
DR PRO; PR:Q9ATB4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ATB4; baseline and differential.
DR Genevisible; Q9ATB4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009631; P:cold acclimation; IMP:TAIR.
DR GO; GO:0016571; P:histone methylation; IEP:TAIR.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
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; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..487
FT /note="Transcriptional adapter ADA2b"
FT /id="PRO_0000269751"
FT DOMAIN 100..152
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 401..487
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 42..98
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 216
FT /note="N6-acetyllysine; by GCN5"
FT /evidence="ECO:0000269|PubMed:16603259"
FT VAR_SEQ 183
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_022095"
FT VAR_SEQ 206..209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_022096"
FT MUTAGEN 216
FT /note="K->A,R: No phenotypic effect."
FT /evidence="ECO:0000269|PubMed:16603259"
SQ SEQUENCE 487 AA; 56186 MW; 51914B5A31724CDC CRC64;
MGRSRGNFQN FEDPTQRTRK KKNAANVENF ESTSLVPGAE GGGKYNCDYC QKDITGKIRI
KCAVCPDFDL CIECMSVGAE ITPHKCDHPY RVMGNLTFPL ICPDWSADDE MLLLEGLEIY
GLGNWAEVAE HVGTKSKEQC LEHYRNIYLN SPFFPLPDMS HVAGKNRKEL QAMAKGRIDD
KKAEQNMKEE YPFSPPKVKV EDTQKESFVD RSFGGKKPVS TSVNNSLVEL SNYNQKREEF
DPEYDNDAEQ LLAEMEFKEN DTPEEHELKL RVLRIYSKRL DERKRRKEFI IERNLLYPNP
FEKDLSQEEK VQCRRLDVFM RFHSKEEHDE LLRNVVSEYR MVKRLKDLKE AQVAGCRSTA
EAERYLGRKR KRENEEGMNR GKESGQFGQI AGEMGSRPPV QASSSYVNDL DLIGFTESQL
LSESEKRLCS EVKLVPPVYL QMQQVMSHEI FKGNVTKKSD AYSLFKIDPT KVDRVYDMLV
KKGIAQL
