ING4_BOVIN
ID ING4_BOVIN Reviewed; 248 AA.
AC Q3T095;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Inhibitor of growth protein 4;
DE AltName: Full=p29ING4;
GN Name=ING4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. May inhibit tumor progression by
CC modulating the transcriptional output of signaling pathways which
CC regulate cell proliferation. Can suppress brain tumor angiogenesis
CC through transcriptional repression of RELA/NFKB3 target genes when
CC complexed with RELA. May also specifically suppress loss of contact
CC inhibition elicited by activated oncogenes such as MYC. Represses
CC hypoxia inducible factor's (HIF) activity by interacting with HIF
CC prolyl hydroxylase 2 (EGLN1) (By similarity). Can enhance apoptosis
CC induced by serum starvation in mammary epithelial cell line HC11 (By
CC similarity). {ECO:0000250|UniProtKB:Q8C0D7,
CC ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SUBUNIT: Homodimer. Component of the HBO1 complex composed of
CC KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit: complexes
CC containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1
CC specificity towards H3K14ac, while complexes containing JADE scaffold
CC (JADE1, JADE2 and JADE3) mediate acetylation of histone H4. Interacts
CC with H3K4me3 and to a lesser extent with H3K4me2, the interaction
CC augments KAT7/HBO1 acetylation activity on H3 tails. Interacts with
CC EP300, RELA and TP53; these interactions may be indirect. Interacts
CC with EGLN1 (By similarity). Interacts with BCL2A1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8C0D7, 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|UniProtKB:Q9UNL4}.
CC -!- DOMAIN: The N-terminal coiled-coil domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- PTM: Citrullination by PADI4 within the nuclear localization signal
CC disrupts the interaction with p53 and increases susceptibility to
CC degradation. {ECO:0000250|UniProtKB:Q9UNL4}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- CAUTION: Lacks the Trp (here Arg-220), a conserved feature of the
CC aromatic cage required for the interaction with histone H3K4me3/2.
CC {ECO:0000305}.
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DR EMBL; BC102494; AAI02495.1; -; mRNA.
DR RefSeq; NP_001030466.1; NM_001035389.2.
DR AlphaFoldDB; Q3T095; -.
DR BMRB; Q3T095; -.
DR SMR; Q3T095; -.
DR STRING; 9913.ENSBTAP00000022686; -.
DR PaxDb; Q3T095; -.
DR PRIDE; Q3T095; -.
DR GeneID; 532483; -.
DR KEGG; bta:532483; -.
DR CTD; 51147; -.
DR eggNOG; KOG1973; Eukaryota.
DR InParanoid; Q3T095; -.
DR OrthoDB; 1434088at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
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 Acetylation; Apoptosis; Cell cycle; Chromatin regulator; Citrullination;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Tumor suppressor;
KW Zinc; Zinc-finger.
FT CHAIN 1..248
FT /note="Inhibitor of growth protein 4"
FT /id="PRO_0000212667"
FT ZN_FING 195..244
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 MOTIF 127..147
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 197
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 208
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 212
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0D7"
FT MOD_RES 132
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNL4"
FT MOD_RES 165
FT /note="Citrulline"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 28429 MW; DA0C4EBC3211E1BC CRC64;
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLASEYM SSARSRSSEE
KLALLRQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD
YDSSSSKGKK SRTQKEKKAA RARSKGKNSD EEAPKAAQKK LKLVRTSPEY GMPSVTFGSV
HPSDVLDMPV DPNEPTYCLC HQVSYGEMIG CDNPDCSIER FHFACVGLTT KPRGKWFCPR
CSQERKKK
