ING1_MOUSE
ID ING1_MOUSE Reviewed; 279 AA.
AC Q9QXV3; B2RWH0; Q9QUP8; Q9QXV4; Q9QZX3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Inhibitor of growth protein 1;
GN Name=Ing1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ; TISSUE=Brain, Embryonic fibroblast, and Spleen;
RX PubMed=10542254; DOI=10.1074/jbc.274.45.32172;
RA Zeremski M., Hill J.E., Kwek S.S.S., Grigorian I.A., Gurova K.V.,
RA Garkavtsev I.V., Diatchenko L., Koonin E.V., Gudkov A.V.;
RT "Structure and regulation of the mouse ing1 gene. Three alternative
RT transcripts encode two PHD finger proteins that have opposite effects on
RT p53 function.";
RL J. Biol. Chem. 274:32172-32181(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Rancourt D., Garkavtsev I.;
RT "Structural organization and expression pattern of the murine ING1 gene.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Isoform 1 inhibits p53-dependent transcriptional activation
CC and may function as an oncoprotein. Isoform 2 acts as a negative growth
CC regulator by cooperating with p53 in transcriptional activation of p53-
CC responsive genes and may act as a tumor suppressor.
CC {ECO:0000269|PubMed:10542254}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC Isoform 2 interacts with RSL1D1. {ECO:0000250|UniProtKB:Q9UK53}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1b, p37;
CC IsoId=Q9QXV3-1; Sequence=Displayed;
CC Name=2; Synonyms=1a, 1c, p31;
CC IsoId=Q9QXV3-2; Sequence=VSP_050378;
CC -!- TISSUE SPECIFICITY: In the adult, widely expressed with highest levels
CC in thymus and testis. {ECO:0000269|PubMed:10542254}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the whole embryo at all
CC stages of development examined. At day 10, highest expression is found
CC in the yolk sac while at day 16 and 18, higher levels are found in
CC inner compartments of bone. In the embryo, highest expression of
CC isoform 1 is found at day 11 while highest expression of isoform 2 is
CC found at day 7. {ECO:0000269|PubMed:10542254}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250}.
CC -!- DOMAIN: The polybasic region (PBR) is responsive to the binding to
CC phosphoinositides (PtdInsPs), including phosphatidylinositol 5-
CC phosphate (PtdIns(5)P). {ECO:0000250|UniProtKB:Q9UK53}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; AF177753; AAF16911.1; -; Genomic_DNA.
DR EMBL; AF177755; AAF16908.1; -; mRNA.
DR EMBL; AF177756; AAF16909.1; -; mRNA.
DR EMBL; AF177757; AAF16910.1; -; mRNA.
DR EMBL; AF149820; AAF09183.1; -; mRNA.
DR EMBL; BC016573; AAH16573.1; -; mRNA.
DR EMBL; BC147770; AAI47771.1; -; mRNA.
DR EMBL; BC147784; AAI47785.1; -; mRNA.
DR CCDS; CCDS22097.1; -. [Q9QXV3-1]
DR CCDS; CCDS85499.1; -. [Q9QXV3-2]
DR RefSeq; NP_001289386.1; NM_001302457.1. [Q9QXV3-2]
DR RefSeq; NP_001289387.1; NM_001302458.1. [Q9QXV3-2]
DR RefSeq; NP_001289388.1; NM_001302459.1. [Q9QXV3-2]
DR RefSeq; NP_001289389.1; NM_001302460.1. [Q9QXV3-2]
DR RefSeq; NP_036049.2; NM_011919.5. [Q9QXV3-1]
DR AlphaFoldDB; Q9QXV3; -.
DR SMR; Q9QXV3; -.
DR BioGRID; 204916; 4.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR IntAct; Q9QXV3; 1.
DR STRING; 10090.ENSMUSP00000062593; -.
DR PhosphoSitePlus; Q9QXV3; -.
DR EPD; Q9QXV3; -.
DR MaxQB; Q9QXV3; -.
DR PaxDb; Q9QXV3; -.
DR PeptideAtlas; Q9QXV3; -.
DR PRIDE; Q9QXV3; -.
DR ProteomicsDB; 266990; -. [Q9QXV3-1]
DR ProteomicsDB; 266991; -. [Q9QXV3-2]
DR Antibodypedia; 4248; 522 antibodies from 38 providers.
DR DNASU; 26356; -.
DR Ensembl; ENSMUST00000054399; ENSMUSP00000062593; ENSMUSG00000045969. [Q9QXV3-1]
DR Ensembl; ENSMUST00000209565; ENSMUSP00000147892; ENSMUSG00000045969. [Q9QXV3-2]
DR Ensembl; ENSMUST00000210041; ENSMUSP00000147270; ENSMUSG00000045969. [Q9QXV3-2]
DR Ensembl; ENSMUST00000210740; ENSMUSP00000147476; ENSMUSG00000045969. [Q9QXV3-2]
DR Ensembl; ENSMUST00000211007; ENSMUSP00000148030; ENSMUSG00000045969. [Q9QXV3-2]
DR GeneID; 26356; -.
DR KEGG; mmu:26356; -.
DR UCSC; uc009kvk.2; mouse. [Q9QXV3-1]
DR CTD; 3621; -.
DR MGI; MGI:1349481; Ing1.
DR VEuPathDB; HostDB:ENSMUSG00000045969; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000155401; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q9QXV3; -.
DR OMA; KMQIVNH; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9QXV3; -.
DR TreeFam; TF352014; -.
DR BioGRID-ORCS; 26356; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q9QXV3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9QXV3; protein.
DR Bgee; ENSMUSG00000045969; Expressed in metanephric cortical collecting duct and 266 other tissues.
DR ExpressionAtlas; Q9QXV3; baseline and differential.
DR Genevisible; Q9QXV3; MM.
DR GO; GO:0005634; C:nucleus; IMP:MGI.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0010941; P:regulation of cell death; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028643; ING1.
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:SF85; PTHR10333:SF85; 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 Alternative splicing; Cell cycle; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..279
FT /note="Inhibitor of growth protein 1"
FT /id="PRO_0000212662"
FT ZN_FING 210..259
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 115..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..279
FT /note="PBR"
FT /evidence="ECO:0000250|UniProtKB:Q9H160"
FT COMPBIAS 137..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 215
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="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 212
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 223
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 227
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 235
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10542254"
FT /id="VSP_050378"
FT CONFLICT 203
FT /note="L -> F (in Ref. 2; AAF09183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 32109 MW; 6765C984EEF179F4 CRC64;
MLSPANGEQI HLVNYVEDYL DSIESLPFDL QRNVSLMREI DAKYQEILKE LDDYYEKFKR
ETDGTQKRRV LHCIQRALIR SQELGDEKIQ IVSQMVELVE NRSRQVDSHV ELFEAHQDIS
DGTGGSGKAG QDKSKSEAIT QADKPNNKRS RRQRNNENRE NASNNHDHDD ITSGTPKEKK
AKTSKKKKRS KAKAEREASP ADLPIDPNEP TYCLCNQVSY GEMIGCDNDE CPIEWFHFSC
VGLNHKPKGK WYCPKCRGES EKTMDKALEK SKKERAYNR
