ING4_CHICK
ID ING4_CHICK Reviewed; 249 AA.
AC Q5ZKY4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Inhibitor of growth protein 4;
DE AltName: Full=p29ING4;
GN Name=ING4; ORFNames=RCJMB04_8l5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Component of HBO1 complexes, which specifically mediate
CC acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced
CC activity toward histone H4. Through chromatin acetylation it may
CC function in DNA replication. {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SUBUNIT: Homodimer. Component of the HBO1 complex.
CC {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; AJ719950; CAG31609.1; -; mRNA.
DR RefSeq; NP_001006251.1; NM_001006251.1.
DR AlphaFoldDB; Q5ZKY4; -.
DR BMRB; Q5ZKY4; -.
DR SMR; Q5ZKY4; -.
DR STRING; 9031.ENSGALP00000023298; -.
DR PaxDb; Q5ZKY4; -.
DR Ensembl; ENSGALT00000023343; ENSGALP00000023298; ENSGALG00000014457.
DR Ensembl; ENSGALT00000061628; ENSGALP00000053802; ENSGALG00000014457.
DR GeneID; 418281; -.
DR KEGG; gga:418281; -.
DR CTD; 51147; -.
DR VEuPathDB; HostDB:geneid_418281; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000159033; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q5ZKY4; -.
DR OMA; SHGQMIM; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q5ZKY4; -.
DR TreeFam; TF352014; -.
DR PRO; PR:Q5ZKY4; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000014457; Expressed in ovary and 13 other tissues.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IEA:InterPro.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell cycle; Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..249
FT /note="Inhibitor of growth protein 4"
FT /id="PRO_0000212670"
FT ZN_FING 196..245
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 115..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..118
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:Q9UK53"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 198
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 209
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 213
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 221
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
SQ SEQUENCE 249 AA; 28556 MW; 436F8C053B6073EF CRC64;
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKS EIDKLATEYI SNARTLSSEE
KLGLLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD
YDSSSSKGKK KGRAQKEKKA ARARSKGKNS DEEAPKTAQK KLKLVRTSTE YGMPSVTFGN
VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP
RCSQERKKK
