CHZ1_YEAST
ID CHZ1_YEAST Reviewed; 153 AA.
AC P40019; D3DLS9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone H2A.Z-specific chaperone CHZ1;
GN Name=CHZ1; OrderedLocusNames=YER030W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17289584; DOI=10.1016/j.molcel.2006.12.015;
RA Luk E., Vu N.-D., Patteson K., Mizuguchi G., Wu W.-H., Ranjan A.,
RA Backus J., Sen S., Lewis M., Bai Y., Wu C.;
RT "Chz1, a nuclear chaperone for histone H2AZ.";
RL Mol. Cell 25:357-368(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-70, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-70, 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 [10]
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).
CC -!- FUNCTION: Forms a chaperone-bound H2A.Z-H2B complex that acts as a
CC source for SWR1 complex-dependent H2A to H2A.Z histone replacement in
CC chromatin. {ECO:0000269|PubMed:17289584}.
CC -!- SUBUNIT: Forms a heterotrimer with H2A.Z-H2B, stabilizing the
CC association of the histone dimer. Also, with a lower affinity, forms a
CC heterotrimer with H2A-H2B. {ECO:0000269|PubMed:17289584}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17289584}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CHZ1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U18778; AAB64563.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006939; DAA07683.1; -; Genomic_DNA.
DR PIR; S50488; S50488.
DR RefSeq; NP_010947.2; NM_001178921.1.
DR PDB; 2JSS; NMR; -; B=64-125.
DR PDB; 6AE8; X-ray; 1.65 A; C/D=64-153.
DR PDBsum; 2JSS; -.
DR PDBsum; 6AE8; -.
DR AlphaFoldDB; P40019; -.
DR BMRB; P40019; -.
DR SMR; P40019; -.
DR BioGRID; 36765; 59.
DR DIP; DIP-6361N; -.
DR IntAct; P40019; 2.
DR MINT; P40019; -.
DR STRING; 4932.YER030W; -.
DR iPTMnet; P40019; -.
DR MaxQB; P40019; -.
DR PaxDb; P40019; -.
DR PRIDE; P40019; -.
DR EnsemblFungi; YER030W_mRNA; YER030W; YER030W.
DR GeneID; 856752; -.
DR KEGG; sce:YER030W; -.
DR SGD; S000000832; CHZ1.
DR VEuPathDB; FungiDB:YER030W; -.
DR eggNOG; ENOG502SCUM; Eukaryota.
DR HOGENOM; CLU_126134_1_0_1; -.
DR InParanoid; P40019; -.
DR OMA; RRNYDDY; -.
DR BioCyc; YEAST:G3O-30211-MON; -.
DR EvolutionaryTrace; P40019; -.
DR PRO; PR:P40019; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40019; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IPI:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IPI:SGD.
DR DisProt; DP01135; -.
DR IDEAL; IID50210; -.
DR InterPro; IPR019098; Histone_chaperone_domain_CHZ.
DR Pfam; PF09649; CHZ; 1.
DR SMART; SM01082; CHZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..153
FT /note="Histone H2A.Z-specific chaperone CHZ1"
FT /id="PRO_0000202623"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..108
FT /note="Important for H2A.Z-H2B binding"
FT COMPBIAS 1..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
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 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2JSS"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2JSS"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2JSS"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2JSS"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2JSS"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6AE8"
SQ SEQUENCE 153 AA; 17463 MW; CE1DCBEFC035BC08 CRC64;
MSDEAKEKRE LESQKESSHN KSEKSVEPKP KRRRRRNYDD YDAEVAKEET KAKNGLTKSE
NNGTVEDSES DMDDAKLDAL MGNEGEEEED DLAEIDTSNI ITSGRRTRGK VIDYKKTAEE
LDKKEPSTGS KDDVGYGEKE EDDEDEEDDD FKE
