ID H0X1T8_OTOGA Unreviewed; 249 AA.
AC H0X1T8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Inhibitor of growth protein {ECO:0000256|RuleBase:RU361213};
GN Name=ING4 {ECO:0000313|Ensembl:ENSOGAP00000008974.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000008974.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000008974.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of an histone acetyltransferase complex.
CC {ECO:0000256|RuleBase:RU361213}.
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; AAQR03127867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0X1T8; -.
DR STRING; 30611.ENSOGAP00000008974; -.
DR Ensembl; ENSOGAT00000010047.2; ENSOGAP00000008974.2; ENSOGAG00000010044.2.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000159033; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; H0X1T8; -.
DR OMA; PIYITPQ; -.
DR OrthoDB; 3140066at2759; -.
DR TreeFam; TF352014; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0140889; P:DNA replication-dependent chromatin disassembly; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IEA:Ensembl.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
DR CDD; cd16862; ING_ING4; 1.
DR CDD; cd15684; PHD_ING4; 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; INHIBITOR OF GROWTH PROTEIN; 1.
DR PANTHER; PTHR10333:SF106; INHIBITOR OF GROWTH PROTEIN 4; 1.
DR Pfam; PF12998; ING; 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 Reference proteome {ECO:0000313|Proteomes:UP000005225};
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 196..245
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 115..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT SITE 198
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 209
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 213
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 221
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 249 AA; 28500 MW; A55272BC8B49FD18 CRC64;
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE
KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD
YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKAAQK KLKLVRTSPE YGMPSVTFGS
VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP
RCSQERKKK
//
