ING2_MOUSE
ID ING2_MOUSE Reviewed; 281 AA.
AC Q9ESK4; Q4VAD7; Q80VI5; Q8BGU8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Inhibitor of growth protein 2;
DE AltName: Full=Inhibitor of growth 1-like protein;
DE AltName: Full=p33ING2;
GN Name=Ing2; Synonyms=Ing1l;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagashima M., Hagiwara K., Hancock A.R., Harris C.C.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Brain, Mammary gland, and Olfactory epithelium;
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).
RN [6]
RP STRUCTURE BY NMR OF 205-262.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain of inhibitor of growth family, member 1-
RT like.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Seems to be involved in p53/TP53 activation and p53/TP53-
CC dependent apoptotic pathways, probably by enhancing acetylation of
CC p53/TP53. Component of a mSin3A-like corepressor complex, which is
CC probably involved in deacetylation of nucleosomal histones. ING2
CC activity seems to be modulated by binding to phosphoinositides
CC (PtdInsPs) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1,
CC HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Predominantly
CC cytoplasmic. Localized to chromatin and nuclear matrix. Upon reduced
CC PtdIns(5)P levels seems to be released from chromatin and, at least
CC partially, translocated to the cytoplasm (By similarity).
CC {ECO:0000250}.
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}.
CC -!- PTM: Sumoylation enhances its association with SIN3A and is required
CC for binding to some target gene promoters, this is the case for TMEM71.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50003.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF078834; AAG12173.1; -; mRNA.
DR EMBL; AK048800; BAC33461.1; -; mRNA.
DR EMBL; AK083144; BAC38783.1; -; mRNA.
DR EMBL; AC107236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466554; EDL35605.1; -; Genomic_DNA.
DR EMBL; BC096433; AAH96433.1; -; mRNA.
DR EMBL; BC138229; AAI38230.1; -; mRNA.
DR EMBL; BC050003; AAH50003.1; ALT_SEQ; mRNA.
DR CCDS; CCDS22298.1; -.
DR RefSeq; NP_075992.2; NM_023503.3.
DR PDB; 1WES; NMR; -; A=205-262.
DR PDB; 2G6Q; X-ray; 2.00 A; A=205-264.
DR PDBsum; 1WES; -.
DR PDBsum; 2G6Q; -.
DR AlphaFoldDB; Q9ESK4; -.
DR SMR; Q9ESK4; -.
DR BioGRID; 213322; 3.
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 DIP; DIP-38912N; -.
DR MINT; Q9ESK4; -.
DR STRING; 10090.ENSMUSP00000079226; -.
DR PhosphoSitePlus; Q9ESK4; -.
DR EPD; Q9ESK4; -.
DR MaxQB; Q9ESK4; -.
DR PaxDb; Q9ESK4; -.
DR PeptideAtlas; Q9ESK4; -.
DR PRIDE; Q9ESK4; -.
DR ProteomicsDB; 267137; -.
DR Antibodypedia; 17300; 323 antibodies from 32 providers.
DR DNASU; 69260; -.
DR Ensembl; ENSMUST00000080353; ENSMUSP00000079226; ENSMUSG00000063049.
DR GeneID; 69260; -.
DR KEGG; mmu:69260; -.
DR UCSC; uc009lrf.2; mouse.
DR CTD; 3622; -.
DR MGI; MGI:1916510; Ing2.
DR VEuPathDB; HostDB:ENSMUSG00000063049; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000158194; -.
DR InParanoid; Q9ESK4; -.
DR OMA; ESRDSTH; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9ESK4; -.
DR TreeFam; TF352014; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation.
DR BioGRID-ORCS; 69260; 12 hits in 75 CRISPR screens.
DR EvolutionaryTrace; Q9ESK4; -.
DR PRO; PR:Q9ESK4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ESK4; protein.
DR Bgee; ENSMUSG00000063049; Expressed in lens of camera-type eye and 252 other tissues.
DR Genevisible; Q9ESK4; MM.
DR GO; GO:0016602; C:CCAAT-binding factor complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:BHF-UCL.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IMP:BHF-UCL.
DR GO; GO:0007141; P:male meiosis I; IMP:BHF-UCL.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
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:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
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:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:2000772; P:regulation of cellular senescence; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:BHF-UCL.
DR GO; GO:0007286; P:spermatid development; IMP:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; IMP:BHF-UCL.
DR CDD; cd15683; PHD_ING2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028639; ING2.
DR InterPro; IPR042019; ING2_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:SF37; PTHR10333:SF37; 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 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; Growth regulation;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..281
FT /note="Inhibitor of growth protein 2"
FT /id="PRO_0000212664"
FT ZN_FING 213..262
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 123..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..281
FT /note="PBR"
FT /evidence="ECO:0000250|UniProtKB:Q9H160"
FT COILED 49..101
FT /evidence="ECO:0000255"
FT COMPBIAS 131..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 215
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 226
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 230
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 238
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9H160"
FT CONFLICT 26
FT /note="S -> T (in Ref. 1; AAG12173 and 5; AAH50003)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="K -> E (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> N (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="E -> G (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> S (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> S (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> H (in Ref. 1; AAG12173)"
FT /evidence="ECO:0000305"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1WES"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:2G6Q"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2G6Q"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2G6Q"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2G6Q"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2G6Q"
SQ SEQUENCE 281 AA; 32978 MW; 6D953B52822C2D8A CRC64;
MLGQQQQQQL YSSAALLTGE RSRLLSCYVQ DYLECVESLP HDMQRNVSVL RELDNKYQET
LKEIDDVYEK YKKEDDSNQK KRLQQHLQRA LINSQELGDE KIQIVTQMLE LVENRARQME
LHSQCFQDPA ESERASDKSK MDSSQPERSS RRPRRQRTSE SRDLCHMTNG IDDCDDQPPK
EKRSKSAKKK KRSKAKQERE ASPVEFAIDP NEPTYCLCNQ VSYGEMIGCD NEQCPIEWFH
FSCVSLTYKP KGKWYCPKCR GDNEKTMDKS TEKTKKERRA R
