ID G2WFG5_YEASK Unreviewed; 282 AA.
AC G2WFG5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Chromatin modification-related protein {ECO:0000256|RuleBase:RU361213};
GN Name=K7_YNG2 {ECO:0000313|EMBL:GAA23808.1};
GN ORFNames=SYK7_032101 {ECO:0000313|EMBL:GAA23808.1};
OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA23808.1, ECO:0000313|Proteomes:UP000001608};
RN [1] {ECO:0000313|EMBL:GAA23808.1, ECO:0000313|Proteomes:UP000001608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT 7.";
RL DNA Res. 18:423-434(2011).
CC -!- FUNCTION: Component of an histone acetyltransferase complex.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Involved in cell cycle progression and
CC meiosis. {ECO:0000256|ARBA:ARBA00037044}.
CC -!- SUBUNIT: Component of an histone acetyltransferase complex. Interacts
CC with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU361213}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000256|ARBA:ARBA00010210,
CC ECO:0000256|RuleBase:RU361213}.
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DR EMBL; DG000044; GAA23808.1; -; Genomic_DNA.
DR AlphaFoldDB; G2WFG5; -.
DR HOGENOM; CLU_031900_2_0_1; -.
DR Proteomes; UP000001608; Chromosome VIII.
DR GO; GO:0000785; C:chromatin; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd16858; ING_ING3_Yng2p; 1.
DR CDD; cd15505; PHD_ING; 1.
DR Gene3D; 6.10.140.1740; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028651; ING_fam.
DR InterPro; IPR024610; ING_N_histone-binding.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10333:SF100; CHROMATIN MODIFICATION-RELATED PROTEIN YNG2; 1.
DR PANTHER; PTHR10333; INHIBITOR OF GROWTH PROTEIN; 1.
DR Pfam; PF12998; ING; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|RuleBase:RU361213};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR628651-51};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR628651-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 222..271
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 123..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT SITE 224
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 235
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 239
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 247
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 282 AA; 32088 MW; A41F0E74261CA44B CRC64;
MDPSLVLEQT IQDVSNLPSE FRYLLEEIGS NDLKLIEEKK KYEQKESQIH KFIRQQGSIP
KHPQEDGLDK EIKESLLKCQ SLQREKCVLA NTALFLIARH LNKLEKNIAL LEEDGVLAPV
EEDGDMDSAA EASRESSVVS NSSVKKRRAA SSSGSVPPTL KKKKTSRTSK LQNEIDVSSR
EKSVTPVSLS IENKIARTKE FKNSRNGKGQ NGSPENEEED KTLYCFCQRV SFGEMVACDG
PNCKYEWFHY DCVNLKEPPK GTWYCPECKI EMEKNKLKRK RN
//
