ING3_CHICK
ID ING3_CHICK Reviewed; 417 AA.
AC Q5ZK36;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Inhibitor of growth protein 3;
GN Name=ING3; ORFNames=RCJMB04_13g20;
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 the NuA4 histone acetyltransferase (HAT) complex
CC which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histone H4 and H2A. This
CC modification may both alter nucleosome - DNA interactions and promote
CC interaction of the modified histones with other proteins which
CC positively regulate transcription (By similarity). NuA4 may also play a
CC direct role in DNA repair when directly recruited to sites of DNA
CC damage (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC Component of the NuA4 histone acetyltransferase complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; AJ720248; CAG31907.1; -; mRNA.
DR RefSeq; NP_001025904.2; NM_001030733.2.
DR AlphaFoldDB; Q5ZK36; -.
DR BMRB; Q5ZK36; -.
DR SMR; Q5ZK36; -.
DR STRING; 9031.ENSGALP00000014665; -.
DR PaxDb; Q5ZK36; -.
DR GeneID; 417762; -.
DR KEGG; gga:417762; -.
DR CTD; 54556; -.
DR VEuPathDB; HostDB:geneid_417762; -.
DR eggNOG; KOG1973; Eukaryota.
DR InParanoid; Q5ZK36; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q5ZK36; -.
DR PRO; PR:Q5ZK36; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd15585; PHD_ING3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038004; ING3.
DR InterPro; IPR042020; ING3_PHD.
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:SF99; PTHR10333:SF99; 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 Chromatin regulator; Growth regulation; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..417
FT /note="Inhibitor of growth protein 3"
FT /id="PRO_0000354693"
FT ZN_FING 359..408
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 128..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 361
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 372
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 376
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 384
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
SQ SEQUENCE 417 AA; 46566 MW; FC8CD86FD275C7EE CRC64;
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVNEFFMNA KKNKPEWREE
QMTSIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE
RRSLELDTPS QPVNNHHAHS HTPVEKRKHN PSSHHGATDH VPEKKFKSEA LLSTLTSDAS
KENTPGRRNN NSSSSSNNAY NTNSSQPLAS YNLGSLSSGS GAGAITMAAA QAVQATAQMK
EGRRTSSLKA SYEAFKNNDF QLGREFSLSR DSTGYSSSAL ASTLTQTLSS SSTDSRSGRK
SKNNNKSSSQ QSSSSSSSSS LSSCSSSSAL AQELSQQTAV IPESDSNSQV DWTYDPNEPR
YCICNQVSYG EMVGCDNQDC PIEWFHYGCV GLTEAPKGKW YCPQCTAAMK RRGSRHK
