ATAD2_YEAST
ID ATAD2_YEAST Reviewed; 1379 AA.
AC P40340; D6VV47;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=ATPase histone chaperone YTA7 {ECO:0000250|UniProtKB:O14114};
DE EC=3.6.1.- {ECO:0000269|PubMed:32079723};
DE AltName: Full=ATPase family AAA domain-containing protein YTA7 {ECO:0000305};
DE Short=AAA-ATPase {ECO:0000305};
DE AltName: Full=Tat-binding homolog 7;
GN Name=YTA7 {ECO:0000303|PubMed:7754704};
GN OrderedLocusNames=YGR270W {ECO:0000312|SGD:S000003502};
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=C836;
RX PubMed=7754704; DOI=10.1002/yea.320100903;
RA Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S., Schwarzlose C.,
RA Vetter I., Feldmann H.;
RT "Identification of a set of yeast genes coding for a novel family of
RT putative ATPases with high similarity to constituents of the 26S protease
RT complex.";
RL Yeast 10:1141-1155(1994).
RN [2]
RP SEQUENCE REVISION.
RA Feldmann H.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9605509;
RX DOI=10.1002/(sici)1097-0061(19980430)14:6<587::aid-yea268>3.0.co;2-i;
RA Agostoni Carbone M.L., Lucchini G., Melchioretto P., Nardese V., Vanoni M.,
RA Panzeri L.;
RT "A 9359 bp fragment from the right arm of Saccharomyces cerevisiae
RT chromosome VII includes the FOL2 and YTA7 genes and three unknown open
RT reading frames.";
RL Yeast 14:587-591(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [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, INTERACTION WITH HISTONES H3 AND H4, AND DISRUPTION PHENOTYPE.
RX PubMed=16079223; DOI=10.1534/genetics.105.046938;
RA Jambunathan N., Martinez A.W., Robert E.C., Agochukwu N.B., Ibos M.E.,
RA Dugas S.L., Donze D.;
RT "Multiple bromodomain genes are involved in restricting the spread of
RT heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA
RT boundary.";
RL Genetics 171:913-922(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11 AND SER-17, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-212; SER-241;
RP SER-259; SER-285; SER-1142 AND SER-1256, AND IDENTIFICATION BY MASS
RP 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-229; SER-259;
RP SER-367; SER-369; SER-370; SER-735; SER-1142 AND SER-1256, 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 [13]
RP FUNCTION, INTERACTION WITH SPT16; CKA1; CKA2; CKB1; CKB2; POB3 AND RNA
RP POLYMERASE II, SUBCELLULAR LOCATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-11; THR-67; SER-94; THR-212; SER-230; SER-241;
RP SER-259; SER-285; SER-304; SER-369; SER-370; THR-380; THR-445 AND LYS-460.
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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 [15]
RP FUNCTION, INTERACTION WITH CSE4/CENP-A AND SCM3, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=32079723; DOI=10.1073/pnas.1917814117;
RA Shahnejat-Bushehri S., Ehrenhofer-Murray A.E.;
RT "The ATAD2/ANCCA homolog Yta7 cooperates with Scm3HJURP to deposit
RT Cse4CENP-A at the centromere in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:5386-5393(2020).
CC -!- FUNCTION: Functions as an ATP-dependent nucleosome disassembly factor
CC that helps evict canonical histone H3 from the 5'-end of genes upon
CC their induction (PubMed:25406467). Also contributes to kinetochore
CC assembly by cooperating with SCM3 to load the histone H3 variant
CC CSE4/CENP-A at centromeres (PubMed:32079723). Provides a chromatin
CC boundary function at the 5'-end of genes that restricts access by
CC RTT106 and thus prevents ectopic spreading of repressive chromatin into
CC coding regions (PubMed:19683497, PubMed:25406467, PubMed:22156209).
CC Also prevents heterochromatin spreading downstream of the silent
CC mating-type locus HMR, this function is independent of the tRNA
CC boundary element (PubMed:16079223). Contributes to appropriate cell
CC cycle regulation of histone gene expression by recruiting RNA
CC polymerase II to histone genes, and subsequent CDK1- and casein kinase
CC II-dependent eviction from chromatin is required to promote
CC transcriptional elongation (PubMed:22156209).
CC {ECO:0000269|PubMed:16079223, ECO:0000269|PubMed:19683497,
CC ECO:0000269|PubMed:22156209, ECO:0000269|PubMed:25406467,
CC ECO:0000269|PubMed:32079723}.
CC -!- SUBUNIT: Interacts with CSE4/CENP-A (PubMed:32079723). Interacts with
CC SCM3 (PubMed:32079723). Interacts with SPT16 (PubMed:22156209).
CC Interacts with POB3 (PubMed:22156209). Interacts with the casein kinase
CC II complex subunits CKA1, CKA2, CKB1 and CKB2 (PubMed:22156209).
CC Interacts with RNA polymerase II (PubMed:22156209). Interacts (via
CC Bromo domain) with histone H3 (PubMed:16079223). Interacts (via Bromo
CC domain) with histone H4 (PubMed:16079223).
CC {ECO:0000269|PubMed:16079223, ECO:0000269|PubMed:22156209,
CC ECO:0000269|PubMed:32079723}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:32079723}. Nucleus {ECO:0000269|PubMed:32079723}.
CC Chromosome {ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:22156209,
CC ECO:0000269|PubMed:25406467}. Note=Binds near the 5'-end within
CC protein-coding genes (PubMed:25406467, PubMed:19683497). Localizes to
CC the negative regulatory element NEG and promoter of the HTA1 gene
CC during G2 and M-phase, and its open reading frame during G1/S
CC (PubMed:22156209, PubMed:19683497). {ECO:0000269|PubMed:19683497,
CC ECO:0000269|PubMed:22156209, ECO:0000269|PubMed:25406467}.
CC -!- PTM: Phosphorylated by CDK1 and casein kinase II during S-phase, which
CC leads to its eviction from histone gene promoters and promotes histone
CC gene transcription. {ECO:0000269|PubMed:22156209}.
CC -!- DISRUPTION PHENOTYPE: Decreases the level of CSE4/CENP-A at centromeres
CC (PubMed:32079723). Decreases internucleosome spacing at protein-coding
CC genes (PubMed:25406467). Decreases localization of RNA polymerase II to
CC the histone HTA1-HTB1 gene locus during the G1/S transition
CC (PubMed:22156209). Decreases HTA1 RNA level (PubMed:19683497).
CC Heterochromatin spreading downstream of the silent mating-type locus
CC HMR (PubMed:16079223). Decreases cell population growth; simultaneous
CC disruption of proteins required for maintaining centromere and
CC kinetochore function, including CLH4 and CBF1, enhances the growth
CC defect (PubMed:32079723). {ECO:0000269|PubMed:16079223,
CC ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:22156209,
CC ECO:0000269|PubMed:25406467, ECO:0000269|PubMed:32079723}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; X81072; CAA56963.1; -; Genomic_DNA.
DR EMBL; Y07893; CAA69201.1; -; Genomic_DNA.
DR EMBL; Z73055; CAA97300.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08358.1; -; Genomic_DNA.
DR PIR; S64603; S64603.
DR RefSeq; NP_011786.1; NM_001181399.1.
DR AlphaFoldDB; P40340; -.
DR SMR; P40340; -.
DR BioGRID; 33519; 595.
DR DIP; DIP-6557N; -.
DR IntAct; P40340; 88.
DR MINT; P40340; -.
DR STRING; 4932.YGR270W; -.
DR iPTMnet; P40340; -.
DR MaxQB; P40340; -.
DR PaxDb; P40340; -.
DR PRIDE; P40340; -.
DR EnsemblFungi; YGR270W_mRNA; YGR270W; YGR270W.
DR GeneID; 853186; -.
DR KEGG; sce:YGR270W; -.
DR SGD; S000003502; YTA7.
DR VEuPathDB; FungiDB:YGR270W; -.
DR eggNOG; KOG0732; Eukaryota.
DR GeneTree; ENSGT00550000074694; -.
DR HOGENOM; CLU_000536_6_1_1; -.
DR InParanoid; P40340; -.
DR OMA; NAQMGIE; -.
DR BioCyc; YEAST:G3O-30936-MON; -.
DR PRO; PR:P40340; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P40340; protein.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IMP:UniProtKB.
DR GO; GO:0140674; F:ATP-dependent histone chaperone activity; IGI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IGI:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23069; PTHR23069; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Bromodomain; Centromere; Chromosome; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CHAIN 2..1379
FT /note="ATPase histone chaperone YTA7"
FT /id="PRO_0000084771"
FT DOMAIN 1044..1086
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..578
FT /note="AAA-ATPase; required for its chromatin boundary
FT function"
FT /evidence="ECO:0000305|PubMed:22156209"
FT REGION 1233..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 11
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-67; A-94; A-212; A-230; A-241; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 67
FT /note="T->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-94; A-212; A-230; A-241; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 94
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-212; A-230; A-241; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 212
FT /note="T->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-230; A-241; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 230
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-241; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 241
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-259; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 259
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 285; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 285
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-304; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 304
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-285; A-369; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 369
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-285; A-304; A-370; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 370
FT /note="S->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-285; A-304; A-369; A-380 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 380
FT /note="T->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-285; A-304; A-369; A-370 and A-445."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 445
FT /note="T->A: Severely decreases phosphorylation, causes a
FT G2/M transition delay, and leads to sensitivity to 6-
FT azauracil (impairs transcriptional elongation); when
FT associated with A-11; A-67; A-94; A-212; A-230; A-241; A-
FT 259; A-285; A-304; A-369; A-370 and A-380."
FT /evidence="ECO:0000269|PubMed:22156209"
FT MUTAGEN 460
FT /note="K->A: Increases YTA7 binding to the HTA1 open
FT reading frame outside of S-phase. Increases localization of
FT RTT106 and RSC8 to the HTA1 gene locus. Increases
FT nucleosome occupancy at core histone loci. Decreases
FT transcription of HTA1."
FT /evidence="ECO:0000269|PubMed:22156209"
FT CONFLICT 70
FT /note="D -> E (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="S -> N (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="S -> N (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1142
FT /note="S -> N (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="K -> E (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="P -> L (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="I -> R (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="Q -> P (in Ref. 1; CAA56963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1379 AA; 157407 MW; 31D1F6F87E62E04F CRC64;
MARNLRNRRG SDVEDASNAK VGYETQIKDE NGIIHTTTRS LRKINYAEIE KVFDFLEDDQ
VMDKDETPVD VTSDEHHNNN QKGDDEDDDV DLVSPHENAR TNEELTNERN LRKRKAHDPE
EDDESFHEED VDDDEEEEEA DEFEDEYLDE DSKDNNRRRR AADRKFVVPD PDDDEEYDED
DEEGDRISHS ASSKRLKRAN SRRTRSSRHP ETPPPVRRAL RSRTRHSRTS NEENDDENDN
SRNEALTLAD EIRELQEDSP IREKRFLRER TKPVNYKLPP PLTASNAEEF IDKNNNALSF
HNPSPARRGR GGWNASQNSG PTRRLFPTGG PFGGNDVTTI FGKNTNFYNQ VPSAFSDNNN
NKLILDSDSS DDEILPLGVT PKTKKENTQK KKKKKPEIAD LDPLGVDMNV NFDDIGGLDN
YIDQLKEMVA LPLLYPELYQ NFNITPPRGV LFHGPPGTGK TLMARALAAS CSSDERKITF
FMRKGADILS KWVGEAERQL RLLFEEAKKH QPSIIFFDEI DGLAPVRSSK QEQIHASIVS
TLLALMDGMD NRGQVIVIGA TNRPDAVDPA LRRPGRFDRE FYFPLPDVKA RFKILQIQTR
KWSSPLSTNF IDKLAFLTKG YGGADLRSLC TEAALISIQR SFPQIYRSND KLLVDPSKIK
VKVSDFMLAL KKIVPSSARS TGSSPQPLPE LIKPLLADQL NNLKNKLDYM LNIKDTTFQR
NTSLLQNFID YEEYSGEEEE HDKYGGNEDT SSFRSYEFFE SMAESQICKP RLLINGPKGN
GQQYVGAAIL NYLEEFNVQN LDLASLVSES SRTIEAAVVQ SFMEAKKRQP SVVFIPNLDI
WINTIPENVI LVLSGLFRSL QSNEKILLLC LAENLDISEV KNGILSDFAF DKNIFQLHKP
SKENITRYFS NLIELLKTKP SDIPMKKRRV KPLPELQKVT SNAAPTNFDE NGEPLSEKVV
LRRKLKSFQH QDMRLKNVLK IKLSGLMDLF KNRYKRFRKP PIDDAFLVHL FEPETSNDPN
WQPAYIKDEN MILEVSTGRK FFNMDLDIVE ERLWNGYYSE PKQFLKDIEL IYRDANTIGD
RERVIKASEM FANAQMGIEE ISTPDFIQEC KATRQRDLER QELFLEDEEK RAAMELEAKE
QSQENILQEP DLKDNKANEF GVAAGNQLQA QLQTTINTAS IVNNSEVPQP IDTNLYKKEI
PAAIPSAVDK EKAVIPEDSG ANEEYTTELI QATCTSEITT DDDERARKEP KENEDSLQTQ
VTEENFSKID ANTNNINHVK EIQSVNKPNS LHETVEKRER SPIPKEVVEP EQGKKSDKEL
ILTPEQIKKV SACLIEHCQN FTVSQLEDVH SSVAKIIWKS KSAWDKTGTV DEIIKFLSE
