ING2_HUMAN
ID ING2_HUMAN Reviewed; 280 AA.
AC Q9H160; B6ZDS1; O95698;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Inhibitor of growth protein 2;
DE AltName: Full=Inhibitor of growth 1-like protein;
DE Short=ING1Lp;
DE AltName: Full=p32;
DE AltName: Full=p33ING2;
GN Name=ING2; Synonyms=ING1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM ING2A), AND TISSUE
RP SPECIFICITY.
RX PubMed=10072587; DOI=10.1159/000015188;
RA Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M.;
RT "Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor
RT suppressor.";
RL Cytogenet. Cell Genet. 83:232-235(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A), FUNCTION, AND INDUCTION.
RX PubMed=11481424; DOI=10.1073/pnas.161151798;
RA Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P., Pedeux R.,
RA Wang X.W., Yokota J., Riabowol K., Harris C.C.;
RT "DNA damage-inducible gene p33ING2 negatively regulates cell proliferation
RT through acetylation of p53.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2B), AND ALTERNATIVE SPLICING.
RX PubMed=18951897; DOI=10.1016/j.febslet.2008.10.024;
RA Unoki M., Kumamoto K., Robles A.I., Shen J.C., Zheng Z.-M., Harris C.C.;
RT "A novel ING2 isoform, ING2b, synergizes with ING2a to prevent cell cycle
RT arrest and apoptosis.";
RL FEBS Lett. 582:3868-3874(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A).
RC TISSUE=Mammary tumor;
RA Cal S., Freije J.M., Lopez-Otin C.;
RT "ING2, a new possible gene suppressor tumor.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ING2B).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ING2A).
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11784859; DOI=10.1128/mcb.22.3.835-848.2002;
RA Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Role of the Sin3-histone deacetylase complex in growth regulation by the
RT candidate tumor suppressor p33(ING1).";
RL Mol. Cell. Biol. 22:835-848(2002).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12859901; DOI=10.1016/s0092-8674(03)00480-x;
RA Gozani O., Karuman P., Jones D.R., Ivanov D., Cha J., Lugovskoy A.A.,
RA Baird C.L., Zhu H., Field S.J., Lessnick S.L., Villasenor J., Mehrotra B.,
RA Chen J., Rao V.R., Brugge J.S., Ferguson C.G., Payrastre B., Myszka D.G.,
RA Cantley L.C., Wagner G., Divecha N., Prestwich G.D., Yuan J.;
RT "The PHD finger of the chromatin-associated protein ING2 functions as a
RT nuclear phosphoinositide receptor.";
RL Cell 114:99-111(2003).
RN [10]
RP PHOSPHOINOSITIDE-BINDING.
RX PubMed=16893883; DOI=10.1074/jbc.m605624200;
RA Kaadige M.R., Ayer D.E.;
RT "The polybasic region that follows the plant homeodomain zinc finger 1 of
RT Pf1 is necessary and sufficient for specific phosphoinositide binding.";
RL J. Biol. Chem. 281:28831-28836(2006).
RN [11]
RP IDENTIFICATION IN MSIN3A COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [12]
RP DOMAIN PHD-TYPE ZINC-FINGER, AND INTERACTION WITH HISTONES H3K4ME3 AND
RP H3K4ME2.
RX PubMed=16728974; DOI=10.1038/nature04835;
RA Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., Carney D.,
RA Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C., Davrazou F., Saha A.,
RA Cairns B.R., Ayer D.E., Kutateladze T.G., Shi Y., Cote J., Chua K.F.,
RA Gozani O.;
RT "ING2 PHD domain links histone H3 lysine 4 methylation to active gene
RT repression.";
RL Nature 442:96-99(2006).
RN [13]
RP SUMOYLATION AT LYS-195.
RX PubMed=20676127; DOI=10.1038/onc.2010.325;
RA Ythier D., Larrieu D., Binet R., Binda O., Brambilla C., Gazzeri S.,
RA Pedeux R.;
RT "Sumoylation of ING2 regulates the transcription mediated by Sin3A.";
RL Oncogene 29:5946-5956(2010).
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). {ECO:0000269|PubMed:11481424, ECO:0000269|PubMed:12859901}.
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.
CC {ECO:0000269|PubMed:11784859, ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:16728974}.
CC -!- INTERACTION:
CC Q9H160; P12004: PCNA; NbExp=3; IntAct=EBI-389787, EBI-358311;
CC Q9H160; Q96ST3: SIN3A; NbExp=2; IntAct=EBI-389787, EBI-347218;
CC Q9H160; Q9HCE7-2: SMURF1; NbExp=3; IntAct=EBI-389787, EBI-9845742;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12859901}.
CC Note=Predominantly nuclear. Localized to chromatin and nuclear matrix.
CC Upon reduced PtdIns(5)P levels seems to be released from chromatin and,
CC at least partially, translocated to the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=ING2a;
CC IsoId=Q9H160-1; Sequence=Displayed;
CC Name=ING2b;
CC IsoId=Q9H160-2; Sequence=VSP_047821;
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher expressed in colon-cancer
CC tumor than in normal colon tissues. {ECO:0000269|PubMed:10072587}.
CC -!- INDUCTION: Induced by the DNA-damaging agents etoposide and
CC neocarzinostatin. {ECO:0000269|PubMed:11481424}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:16728974}.
CC -!- DOMAIN: The polybasic region (PBR) is responsive to the binding to
CC phosphoinositides (PtdInsPs), including phosphatidylinositol 5-
CC phosphate (PtdIns(5)P). {ECO:0000269|PubMed:16728974}.
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:0000269|PubMed:20676127}.
CC -!- MISCELLANEOUS: [Isoform ING2b]: Low expression except in testis, where
CC it reaches half of ING2a levels. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ING2ID40975ch4q35.html";
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DR EMBL; AB012853; BAA36419.1; -; mRNA.
DR EMBL; AF053537; AAG11395.1; -; mRNA.
DR EMBL; AF062748; AAG11396.1; -; Genomic_DNA.
DR EMBL; AF062747; AAG11396.1; JOINED; Genomic_DNA.
DR EMBL; AB196793; BAF30476.1; -; mRNA.
DR EMBL; AJ006851; CAC20567.1; -; mRNA.
DR EMBL; AK294310; BAH11731.1; -; mRNA.
DR EMBL; AC107214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030128; AAH30128.1; -; mRNA.
DR CCDS; CCDS3833.1; -. [Q9H160-1]
DR RefSeq; NP_001278888.1; NM_001291959.1. [Q9H160-2]
DR RefSeq; NP_001555.1; NM_001564.3. [Q9H160-1]
DR AlphaFoldDB; Q9H160; -.
DR SMR; Q9H160; -.
DR BioGRID; 109834; 67.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR CORUM; Q9H160; -.
DR IntAct; Q9H160; 41.
DR MINT; Q9H160; -.
DR STRING; 9606.ENSP00000307183; -.
DR BindingDB; Q9H160; -.
DR ChEMBL; CHEMBL3784904; -.
DR iPTMnet; Q9H160; -.
DR PhosphoSitePlus; Q9H160; -.
DR BioMuta; ING2; -.
DR DMDM; 59798471; -.
DR EPD; Q9H160; -.
DR jPOST; Q9H160; -.
DR MassIVE; Q9H160; -.
DR MaxQB; Q9H160; -.
DR PaxDb; Q9H160; -.
DR PeptideAtlas; Q9H160; -.
DR PRIDE; Q9H160; -.
DR ProteomicsDB; 6258; -.
DR ProteomicsDB; 80360; -. [Q9H160-1]
DR Antibodypedia; 17300; 323 antibodies from 32 providers.
DR DNASU; 3622; -.
DR Ensembl; ENST00000302327.4; ENSP00000307183.3; ENSG00000168556.7. [Q9H160-1]
DR GeneID; 3622; -.
DR KEGG; hsa:3622; -.
DR MANE-Select; ENST00000302327.4; ENSP00000307183.3; NM_001564.4; NP_001555.1.
DR UCSC; uc003ivs.2; human. [Q9H160-1]
DR CTD; 3622; -.
DR DisGeNET; 3622; -.
DR GeneCards; ING2; -.
DR HGNC; HGNC:6063; ING2.
DR HPA; ENSG00000168556; Low tissue specificity.
DR MIM; 604215; gene.
DR neXtProt; NX_Q9H160; -.
DR OpenTargets; ENSG00000168556; -.
DR PharmGKB; PA29873; -.
DR VEuPathDB; HostDB:ENSG00000168556; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000158194; -.
DR HOGENOM; CLU_031900_5_0_1; -.
DR InParanoid; Q9H160; -.
DR OMA; ESRDSTH; -.
DR PhylomeDB; Q9H160; -.
DR TreeFam; TF352014; -.
DR PathwayCommons; Q9H160; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
DR SignaLink; Q9H160; -.
DR SIGNOR; Q9H160; -.
DR BioGRID-ORCS; 3622; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; ING2; human.
DR GeneWiki; ING2; -.
DR GenomeRNAi; 3622; -.
DR Pharos; Q9H160; Tchem.
DR PRO; PR:Q9H160; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9H160; protein.
DR Bgee; ENSG00000168556; Expressed in amniotic fluid and 210 other tissues.
DR ExpressionAtlas; Q9H160; baseline and differential.
DR Genevisible; Q9H160; HS.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:BHF-UCL.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; ISS:BHF-UCL.
DR GO; GO:0007141; P:male meiosis I; ISS:BHF-UCL.
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:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; TAS:BHF-UCL.
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; ISS: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:UniProtKB.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; NAS:BHF-UCL.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; NAS:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; ISS: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 Alternative splicing; Chromatin regulator; Coiled coil;
KW Direct protein sequencing; Growth regulation; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..280
FT /note="Inhibitor of growth protein 2"
FT /id="PRO_0000212663"
FT ZN_FING 212..261
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 122..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..280
FT /note="PBR"
FT /evidence="ECO:0000269|PubMed:16728974"
FT COILED 48..120
FT /evidence="ECO:0000255"
FT COMPBIAS 130..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 214
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 225
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 229
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 237
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:20676127"
FT VAR_SEQ 1..58
FT /note="MLGQQQQQLYSSAALLTGERSRLLTCYVQDYLECVESLPHDMQRNVSVLREL
FT DNKYQE -> MDQDGDQQLGPSRILAPQ (in isoform ING2b)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:18951897"
FT /id="VSP_047821"
FT CONFLICT 21
FT /note="S -> T (in Ref. 4; CAC20567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 32808 MW; DC85A6ECAF7A5D81 CRC64;
MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR ELDNKYQETL
KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK IQIVTQMLEL VENRARQMEL
HSQCFQDPAE SERASDKAKM DSSQPERSSR RPRRQRTSES RDLCHMANGI EDCDDQPPKE
KKSKSAKKKK RSKAKQEREA SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF
SCVSLTYKPK GKWYCPKCRG DNEKTMDKST EKTKKDRRSR
