ING2_SCHPO
ID ING2_SCHPO Reviewed; 305 AA.
AC O74736;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Chromatin modification-related protein png2;
DE AltName: Full=ING1 homolog 2;
GN Name=png2; ORFNames=SPBC1709.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=10805724; DOI=10.1128/mcb.20.11.3807-3816.2000;
RA Loewith R., Meijer M., Lees-Miller S.P., Riabowol K., Young D.;
RT "Three yeast proteins related to the human candidate tumor suppressor
RT p33(ING1) are associated with histone acetyltransferase activities.";
RL Mol. Cell. Biol. 20:3807-3816(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP IDENTIFICATION IN THE CLR6 HISTONE DEACETYLATION COMPLEX I-PRIME,
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CLR6, AND FUNCTION.
RX PubMed=17450151; DOI=10.1038/nsmb1239;
RA Nicolas E., Yamada T., Cam H.P., Fitzgerald P.C., Kobayashi R.,
RA Grewal S.I.S.;
RT "Distinct roles of HDAC complexes in promoter silencing, antisense
RT suppression and DNA damage protection.";
RL Nat. Struct. Mol. Biol. 14:372-380(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181; THR-183; SER-197 AND
RP SER-198, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Component of the clr6 histone deacetylase complex I'
CC responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events. Has a role in silencing of mating type genes.
CC {ECO:0000269|PubMed:10805724, ECO:0000269|PubMed:17450151}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By
CC similarity). Component of the clr6 histone deacetylase complex
CC I'composed of at least clr6, png2, prw1, pst1 and sds3. {ECO:0000250,
CC ECO:0000269|PubMed:17450151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21250.1; -; Genomic_DNA.
DR PIR; T39639; T39639.
DR RefSeq; NP_595444.1; NM_001021353.2.
DR AlphaFoldDB; O74736; -.
DR SMR; O74736; -.
DR BioGRID; 276497; 101.
DR DIP; DIP-29344N; -.
DR IntAct; O74736; 4.
DR STRING; 4896.SPBC1709.11c.1; -.
DR iPTMnet; O74736; -.
DR MaxQB; O74736; -.
DR PaxDb; O74736; -.
DR PRIDE; O74736; -.
DR EnsemblFungi; SPBC1709.11c.1; SPBC1709.11c.1:pep; SPBC1709.11c.
DR PomBase; SPBC1709.11c; png2.
DR VEuPathDB; FungiDB:SPBC1709.11c; -.
DR eggNOG; KOG1973; Eukaryota.
DR HOGENOM; CLU_031900_2_1_1; -.
DR InParanoid; O74736; -.
DR OMA; SHGQMIM; -.
DR PhylomeDB; O74736; -.
DR Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SPO-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:O74736; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 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; PTHR10333; 1.
DR Pfam; PF12998; ING; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..305
FT /note="Chromatin modification-related protein png2"
FT /id="PRO_0000362155"
FT ZN_FING 248..297
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 135..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 250
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 261
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 265
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 273
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 305 AA; 34877 MW; 3E509927B8C82885 CRC64;
MGTSGIEIFA ALNDFTDAIV SVPESVCGKF TSLKEIDAQV RDIRQNVIQE IGVVLKNEKN
DELSGEERCE RLQKTLKEIL PYSDSKICLA TDAMNNIKSC IDRLDAGFEY VELEIPQQLR
LGYPDDRALM NYHSTVTPQT SERRRETRRH QNNQHSQQYS SQERSSSYNN FEDASSPQSS
YHTPTKRRKN AVPRKSSSPP LSSTKHAPQS TERRPVRRSE SRLKQTNGEP LVKHDTLDSS
DISREGEQLY CYCQQVSYGQ MIGCDNENCK REWFHLPCVG LVEPPKGIWY CKECEELAKS
SESRQ
