RT106_YEAST
ID RT106_YEAST Reviewed; 455 AA.
AC P40161; D6W0Y4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Histone chaperone RTT106;
DE AltName: Full=Regulator of Ty1 transposition protein 106;
GN Name=RTT106 {ECO:0000303|PubMed:16157874}; OrderedLocusNames=YNL206C;
GN ORFNames=N1346;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7725799; DOI=10.1002/yea.320101213;
RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT new open reading frames of unknown function.";
RL Yeast 10:1639-1645(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=11779788; DOI=10.1093/genetics/159.4.1449;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have
RT conserved roles in genome maintenance.";
RL Genetics 159:1449-1465(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH HISTONE H3; HISTONE H4 AND RLF2.
RX PubMed=16157874; DOI=10.1073/pnas.0506176102;
RA Huang S., Zhou H., Katzmann D., Hochstrasser M., Atanasova E., Zhang Z.;
RT "Rtt106p is a histone chaperone involved in heterochromatin-mediated
RT silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13410-13415(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH SIR4.
RX PubMed=17410207; DOI=10.1038/sj.emboj.7601670;
RA Huang S., Zhou H., Tarara J., Zhang Z.;
RT "A novel role for histone chaperones CAF-1 and Rtt106p in heterochromatin
RT silencing.";
RL EMBO J. 26:2274-2283(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP FUNCTION, INTERACTION WITH HIR AND CAF-1 COMPLEXES; CAC2; MSI1; HIR1; HIR2
RP AND HPC2, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP RTT106.
RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023;
RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K.,
RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J.,
RA Andrews B.J.;
RT "Two-color cell array screen reveals interdependent roles for histone
RT chaperones and a chromatin boundary regulator in histone gene repression.";
RL Mol. Cell 35:340-351(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408; SER-411 AND SER-450, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP FUNCTION, AND INTERACTION WITH HISTONE H3.
RX PubMed=20188666; DOI=10.1016/j.molcel.2010.01.020;
RA Burgess R.J., Zhou H., Han J., Zhang Z.;
RT "A role for Gcn5 in replication-coupled nucleosome assembly.";
RL Mol. Cell 37:469-480(2010).
RN [13]
RP FUNCTION.
RX PubMed=21763693; DOI=10.1016/j.febslet.2011.06.036;
RA Wan Y., Chen W., Xing J., Tan J., Li B., Chen H., Lin Z., Chiang J.H.,
RA Saleem R.A.;
RT "Transcriptome profiling reveals a novel role for trichostatin A in
RT antagonizing histone chaperone Chz1 mediated telomere anti-silencing.";
RL FEBS Lett. 585:2519-2525(2011).
RN [14]
RP FUNCTION, DNA-BINDING, INTERACTION WITH YTA7, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22156209; DOI=10.1101/gad.173427.111;
RA Kurat C.F., Lambert J.P., van Dyk D., Tsui K., van Bakel H.,
RA Kaluarachchi S., Friesen H., Kainth P., Nislow C., Figeys D.,
RA Fillingham J., Andrews B.J.;
RT "Restriction of histone gene transcription to S phase by phosphorylation of
RT a chromatin boundary protein.";
RL Genes Dev. 25:2489-2501(2011).
RN [15]
RP FUNCTION, AND INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=21444721; DOI=10.1128/mcb.01432-10;
RA Yu Y., Srinivasan M., Nakanishi S., Leatherwood J., Shilatifard A.,
RA Sternglanz R.;
RT "A conserved patch near the C terminus of histone H4 is required for genome
RT stability in budding yeast.";
RL Mol. Cell. Biol. 31:2311-2325(2011).
RN [16]
RP FUNCTION, AND INTERACTION WITH SWI/SNF; RSC AND HIR COMPLEXES.
RX PubMed=21698254; DOI=10.1371/journal.pone.0021113;
RA Ferreira M.E., Flaherty K., Prochasson P.;
RT "The Saccharomyces cerevisiae histone chaperone Rtt106 mediates the cell
RT cycle recruitment of SWI/SNF and RSC to the HIR-dependent histone genes.";
RL PLoS ONE 6:E21113-E21113(2011).
RN [17]
RP FUNCTION.
RX PubMed=21978826; DOI=10.1016/j.bbagrm.2011.09.003;
RA Amin A.D., Dimova D.K., Ferreira M.E., Vishnoi N., Hancock L.C.,
RA Osley M.A., Prochasson P.;
RT "The mitotic Clb cyclins are required to alleviate HIR-mediated repression
RT of the yeast histone genes at the G1/S transition.";
RL Biochim. Biophys. Acta 1819:16-27(2012).
RN [18]
RP DISRUPTION PHENOTYPE.
RX PubMed=25406467; DOI=10.1534/genetics.114.168039;
RA Lombardi L.M., Davis M.D., Rine J.;
RT "Maintenance of nucleosomal balance in cis by conserved AAA-ATPase Yta7.";
RL Genetics 199:105-116(2015).
RN [19]
RP FUNCTION.
RX PubMed=22128187; DOI=10.1074/jbc.m111.316489;
RA Silva A.C., Xu X., Kim H.S., Fillingham J., Kislinger T., Mennella T.A.,
RA Keogh M.C.;
RT "The replication-independent histone H3-H4 chaperones HIR, ASF1, and RTT106
RT co-operate to maintain promoter fidelity.";
RL J. Biol. Chem. 287:1709-1718(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 65-320, DNA-BINDING, INTERACTION
RP WITH HISTONES H3 AND H4, AND FUNCTION.
RX PubMed=20007951; DOI=10.1074/jbc.m109.055996;
RA Liu Y., Huang H., Zhou B.O., Wang S.S., Hu Y., Li X., Liu J., Zang J.,
RA Niu L., Wu J., Zhou J.Q., Teng M., Shi Y.;
RT "Structural analysis of Rtt106p reveals a DNA binding role required for
RT heterochromatin silencing.";
RL J. Biol. Chem. 285:4251-4262(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 68-301, DOMAIN, SUBUNIT,
RP INTERACTION WITH HISTONES H3 AND H4, AND MUTAGENESIS OF ILE-259; TYR-261;
RP PHE-269; GLN-288 AND ILE-294.
RX PubMed=22307274; DOI=10.1038/nature10861;
RA Su D., Hu Q., Li Q., Thompson J.R., Cui G., Fazly A., Davies B.A.,
RA Botuyan M.V., Zhang Z., Mer G.;
RT "Structural basis for recognition of H3K56-acetylated histone H3-H4 by the
RT chaperone Rtt106.";
RL Nature 483:104-107(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 69-300.
RX PubMed=22198837; DOI=10.1073/pnas.1119095109;
RA Zunder R.M., Antczak A.J., Berger J.M., Rine J.;
RT "Two surfaces on the histone chaperone Rtt106 mediate histone binding,
RT replication, and silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E144-E153(2012).
CC -!- FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome
CC formation and heterochromatin silencing. Required for the deposition of
CC H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role
CC in the transcriptional regulation of the cell-cycle dependent histone
CC genes by directly recruiting the SWI/SNF and RSC chromatin remodeling
CC complexes to the histone genes in a cell cycle dependent manner. In
CC cooperation with HIR and ASF1, creates a repressive structure at the
CC core histone gene promoter and contributes to their repression outside
CC of S phase. Involved in regulation of Ty1 transposition.
CC {ECO:0000269|PubMed:11779788, ECO:0000269|PubMed:16157874,
CC ECO:0000269|PubMed:17410207, ECO:0000269|PubMed:19683497,
CC ECO:0000269|PubMed:20007951, ECO:0000269|PubMed:20188666,
CC ECO:0000269|PubMed:21444721, ECO:0000269|PubMed:21698254,
CC ECO:0000269|PubMed:21763693, ECO:0000269|PubMed:21978826,
CC ECO:0000269|PubMed:22128187, ECO:0000269|PubMed:22156209}.
CC -!- SUBUNIT: Homodimers (via the N-terminal domain) (PubMed:22307274).
CC Interacts with the SWI/SNF complex (PubMed:21698254). Interacts with
CC the RSC complex (PubMed:21698254). Interacts with the HIR complex
CC (PubMed:21698254, PubMed:19683497). Interacts with the CAF-1 complex
CC (PubMed:19683497). Interacts with RLF2 (PubMed:16157874). Interacts
CC with SIR4 (PubMed:17410207). Interacts with YTA7 (PubMed:22156209).
CC Interacts with CAC2 (PubMed:19683497). Interacts with HPC2
CC (PubMed:19683497). Interacts with HIR2 (PubMed:19683497). Interacts
CC with MSI1 (PubMed:19683497). Interacts with HIR1 (PubMed:19683497).
CC Interacts with histone H3 (PubMed:16157874, PubMed:20007951,
CC PubMed:20188666, PubMed:21444721, PubMed:22307274). Interacts with
CC histone H4 (PubMed:16157874, PubMed:20007951, PubMed:21444721,
CC PubMed:22307274). {ECO:0000269|PubMed:16157874,
CC ECO:0000269|PubMed:17410207, ECO:0000269|PubMed:19683497,
CC ECO:0000269|PubMed:20007951, ECO:0000269|PubMed:20188666,
CC ECO:0000269|PubMed:21444721, ECO:0000269|PubMed:21698254,
CC ECO:0000269|PubMed:22156209, ECO:0000269|PubMed:22307274}.
CC -!- INTERACTION:
CC P40161; P32447: ASF1; NbExp=5; IntAct=EBI-29119, EBI-3003;
CC P40161; P61830: HHT2; NbExp=6; IntAct=EBI-29119, EBI-8098;
CC P40161; P40161: RTT106; NbExp=5; IntAct=EBI-29119, EBI-29119;
CC P40161; P11978: SIR4; NbExp=2; IntAct=EBI-29119, EBI-17237;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19683497}. Chromosome
CC {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of
CC histones HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2,.
CC {ECO:0000269|PubMed:19683497}.
CC -!- DOMAIN: The N-ter domain (residues 1-67) homodimerizes and interacts
CC with H3-H4 independently of acetylation while the double pleckstrin-
CC homology (PH) domain (residues 68-301) binds the 'Lys-56'-containing
CC region of H3. {ECO:0000269|PubMed:22307274}.
CC -!- DISRUPTION PHENOTYPE: Decreases nucleosomal density (PubMed:25406467,
CC PubMed:19683497). Increases HTA1 RNA level; simultaneous disruption
CC RTT109 alleviates the effect (PubMed:22156209, PubMed:19683497).
CC {ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:22156209,
CC ECO:0000269|PubMed:25406467}.
CC -!- MISCELLANEOUS: Present with 11100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RTT106 family. {ECO:0000305}.
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DR EMBL; X78898; CAA55502.1; -; Genomic_DNA.
DR EMBL; Z71482; CAA96106.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10350.1; -; Genomic_DNA.
DR PIR; S50725; S50725.
DR RefSeq; NP_014193.1; NM_001183044.1.
DR PDB; 2LH0; NMR; -; A/B=1-67.
DR PDB; 3FSS; X-ray; 1.43 A; A=68-301.
DR PDB; 3GYO; X-ray; 3.10 A; A=65-320.
DR PDB; 3GYP; X-ray; 2.41 A; A=65-320.
DR PDB; 3TO1; X-ray; 2.60 A; A/B=69-300.
DR PDB; 3TVV; X-ray; 2.59 A; A/B=68-315.
DR PDB; 3TW1; X-ray; 1.77 A; A=68-301.
DR PDB; 6THL; X-ray; 2.80 A; A=65-301.
DR PDBsum; 2LH0; -.
DR PDBsum; 3FSS; -.
DR PDBsum; 3GYO; -.
DR PDBsum; 3GYP; -.
DR PDBsum; 3TO1; -.
DR PDBsum; 3TVV; -.
DR PDBsum; 3TW1; -.
DR PDBsum; 6THL; -.
DR AlphaFoldDB; P40161; -.
DR SMR; P40161; -.
DR BioGRID; 35630; 186.
DR DIP; DIP-4292N; -.
DR IntAct; P40161; 56.
DR MINT; P40161; -.
DR STRING; 4932.YNL206C; -.
DR iPTMnet; P40161; -.
DR MaxQB; P40161; -.
DR PaxDb; P40161; -.
DR PRIDE; P40161; -.
DR EnsemblFungi; YNL206C_mRNA; YNL206C; YNL206C.
DR GeneID; 855515; -.
DR KEGG; sce:YNL206C; -.
DR SGD; S000005150; RTT106.
DR VEuPathDB; FungiDB:YNL206C; -.
DR eggNOG; ENOG502R9PE; Eukaryota.
DR HOGENOM; CLU_040939_1_0_1; -.
DR InParanoid; P40161; -.
DR OMA; TRLTFNV; -.
DR BioCyc; YEAST:G3O-33212-MON; -.
DR EvolutionaryTrace; P40161; -.
DR PRO; PR:P40161; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40161; protein.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IGI:SGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR CDD; cd11604; RTT106_N; 1.
DR DisProt; DP01485; -.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.10.70; -; 1.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040993; Rtt106_N.
DR InterPro; IPR044891; Rtt106_N_sf.
DR InterPro; IPR040770; Rtt106_PH.
DR Pfam; PF18469; PH_18; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF18215; Rtt106_N; 1.
DR SMART; SM01287; Rtt106; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Chromosome; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transposition.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..455
FT /note="Histone chaperone RTT106"
FT /id="PRO_0000203392"
FT DOMAIN 68..200
FT /note="PH 1"
FT DOMAIN 217..301
FT /note="PH 2"
FT REGION 2..67
FT /note="Dimeric region"
FT REGION 68..301
FT /note="Double PH domain"
FT REGION 305..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 259
FT /note="I->A: Decreases histone-binding."
FT /evidence="ECO:0000269|PubMed:22307274"
FT MUTAGEN 261
FT /note="Y->A: Impairs histone-binding."
FT /evidence="ECO:0000269|PubMed:22307274"
FT MUTAGEN 269
FT /note="F->A: Impairs histone-binding."
FT /evidence="ECO:0000269|PubMed:22307274"
FT MUTAGEN 288
FT /note="Q->A: Decreases histone-binding."
FT /evidence="ECO:0000269|PubMed:22307274"
FT MUTAGEN 291
FT /note="Y->A: Impairs histone-binding."
FT MUTAGEN 294
FT /note="I->A: Impairs histone-binding."
FT /evidence="ECO:0000269|PubMed:22307274"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2LH0"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:2LH0"
FT HELIX 27..41
FT /evidence="ECO:0007829|PDB:2LH0"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2LH0"
FT STRAND 71..85
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3FSS"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 220..235
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:3FSS"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3FSS"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:3FSS"
SQ SEQUENCE 455 AA; 51621 MW; 79CACA659A7F4F4D CRC64;
MSKLFLDELP ESLSRKIGTV VRVLPSSLEI FEELYKYALN ENSNDRSGRH KKPRIDVSSD
LLKTDEISET NTIFKLEGVS VLSPLRKKLD LVFYLSNVDG SPVITLLKGN DRELSIYQLN
KNIKMASFLP VPEKPNLIYL FMTYTSCEDN KFSEPVVMTL NKENTLNQFK NLGLLDSNVT
DFEKCVEYIR KQAILTGFKI SNPFVNSTLV DTDAEKINSF HLQCHRGTKE GTLYFLPDHI
IFGFKKPILL FDASDIESIT YSSITRLTFN ASLVTKDGEK YEFSMIDQTE YAKIDDYVKR
KQMKDKSMSE ELKAKSKSKG QATDGTADQP SILQEATRQM QDEKKAGVFS DDDEENDQNF
EAESDLSDGS GQESSDGAED GEEAEEDDEE DDEEEDKKGQ SALNRDNSFA SINGQPEQEL
QYKEFKEPLE LEDIPIEIDN DDDEDDEDGS GVEYD
