ING5_DROME
ID ING5_DROME Reviewed; 285 AA.
AC Q9VJY8; Q8IP71; Q95RB4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Inhibitor of growth protein 5 {ECO:0000305};
DE AltName: Full=Inhibitor of growth family member 5 {ECO:0000312|FlyBase:FBgn0032516};
GN Name=Ing5 {ECO:0000312|FlyBase:FBgn0032516};
GN ORFNames=CG9293 {ECO:0000312|FlyBase:FBgn0032516};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAN10835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAN10835.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAN10835.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ADR66771.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE ENOK COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=27198229; DOI=10.1101/gad.271429.115;
RA Huang F., Saraf A., Florens L., Kusch T., Swanson S.K., Szerszen L.T.,
RA Li G., Dutta A., Washburn M.P., Abmayr S.M., Workman J.L.;
RT "The Enok acetyltransferase complex interacts with Elg1 and negatively
RT regulates PCNA unloading to promote the G1/S transition.";
RL Genes Dev. 30:1198-1210(2016).
CC -!- FUNCTION: Component of the Enok complex which has a histone H3
CC acetyltransferase activity. {ECO:0000269|PubMed:27198229}.
CC -!- SUBUNIT: Component of the Enok complex composed at least Br140, enok,
CC Eaf6 and Ing5. {ECO:0000269|PubMed:27198229}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU361213,
CC ECO:0000269|PubMed:27198229}. Chromosome
CC {ECO:0000250|UniProtKB:Q8WYH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0032516};
CC IsoId=Q9VJY8-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0032516};
CC IsoId=Q9VJY8-2; Sequence=VSP_061597;
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000255|RuleBase:RU361213}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000255|RuleBase:RU361213}.
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DR EMBL; AE014134; AAF53297.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10835.1; -; Genomic_DNA.
DR EMBL; AY061507; AAL29055.1; -; mRNA.
DR EMBL; BT125797; ADR66771.1; -; mRNA.
DR RefSeq; NP_609647.1; NM_135803.4.
DR RefSeq; NP_723814.1; NM_165042.3.
DR SMR; Q9VJY8; -.
DR IntAct; Q9VJY8; 2.
DR STRING; 7227.FBpp0080103; -.
DR DNASU; 34752; -.
DR EnsemblMetazoa; FBtr0080525; FBpp0080103; FBgn0032516.
DR GeneID; 34752; -.
DR KEGG; dme:Dmel_CG9293; -.
DR UCSC; CG9293-RA; d. melanogaster.
DR CTD; 84289; -.
DR FlyBase; FBgn0032516; Ing5.
DR VEuPathDB; VectorBase:FBgn0032516; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000158159; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR OMA; QPKGKWF; -.
DR OrthoDB; 1434088at2759; -.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 34752; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CG9293; fly.
DR GenomeRNAi; 34752; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032516; Expressed in saliva-secreting gland and 29 other tissues.
DR ExpressionAtlas; Q9VJY8; baseline and differential.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028638; ING4/ING5.
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 PANTHER; PTHR10333:SF41; PTHR10333:SF41; 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 Alternative splicing; Chromatin regulator; Chromosome; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..285
FT /note="Inhibitor of growth protein 5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000456246"
FT ZN_FING 232..281
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-51,
FT ECO:0000255|PROSITE-ProRule:PRU00146"
FT SITE 234
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-50"
FT SITE 245
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-50"
FT SITE 249
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-50"
FT SITE 257
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000255|PIRSR:PIRSR628651-50"
FT VAR_SEQ 185..198
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_061597"
SQ SEQUENCE 285 AA; 32080 MW; C098B515673FEAAC CRC64;
MSSAIYLENY LDGLESLPTE LERNFKLMRK LDDRAQTAMK SIDSHAKDFM RKLGENGAMS
EDERRERQED IKALFGKAKE YSDDKVQLAI QTYELVDKQI RRLDNDLARF EGEIQEKASS
TRAKSEEVVA KKGRKKTKDS KTTGKKKKSA SSDEETGRGN NQSNANSSVN SSSNAGQGSK
KKKSKVNQEK ETRKGGAQKK TVEVDDSEKE SCHTAATHPS DVMDMPVDPN EPTYCLCHQV
SYGEMIGCDN PDCPIEWFHF ACVGLTTKPK GKWFCPKCTQ DRKKK
