ING3_HUMAN
ID ING3_HUMAN Reviewed; 418 AA.
AC Q9NXR8; A8K790; O60394; Q567P3; Q6GMT3; Q7Z762; Q969G0; Q96DT4; Q9HC99;
AC Q9P081;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Inhibitor of growth protein 3;
DE AltName: Full=p47ING3;
GN Name=ING3; ORFNames=HSPC301;
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 [MRNA] (ISOFORM 1), AND ROLE IN P53 MEDIATED GROWTH
RP SUPPRESSION.
RX PubMed=12545155; DOI=10.1038/sj.onc.1206115;
RA Nagashima M., Shiseki M., Pedeux R.M., Okamura S., Kitahama-Shiseki M.,
RA Miura K., Yokota J., Harris C.C.;
RT "A novel PHD-finger motif protein, p47ING3, modulates p53-mediated
RT transcription, cell cycle control, and apoptosis.";
RL Oncogene 22:343-350(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zenklusen J.C., Green E.D.;
RT "Cloning and characterization of p47ING3, a new member of the p33ING1
RT family of p53 regulators.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Blood, Liver, Lung, Pancreas, and Urinary bladder;
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 80-92, IDENTIFICATION IN NUA4 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [9]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [10]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN NUA4
RP COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [11]
RP IDENTIFICATION IN NUA4 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 DOMAIN PHD-TYPE ZINC-FINGER, AND INTERACTION WITH HISTONES H3K4ME3 AND
RP H3K4ME2.
RX PubMed=19154204; DOI=10.1111/j.1365-313x.2009.03795.x;
RA Lee W.Y., Lee D., Chung W.I., Kwon C.S.;
RT "Arabidopsis ING and Alfin1-like protein families localize to the nucleus
RT and bind to H3K4me3/2 via plant homeodomain fingers.";
RL Plant J. 58:511-524(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-165; LYS-167 AND
RP LYS-256, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP STRUCTURE BY NMR OF 362-418.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PHD domain in inhibitor of growth protein 3 (ING3)
RT antigen 7.";
RL Submitted (NOV-2006) to the PDB data bank.
RN [20]
RP VARIANT HNSCC GLY-20.
RX PubMed=12080476; DOI=10.1038/sj.onc.1205540;
RA Gunduz M., Ouchida M., Fukushima K., Ito S., Jitsumori Y., Nakashima T.,
RA Nagai N., Nishizaki K., Shimizu K.;
RT "Allelic loss and reduced expression of the ING3, a candidate tumor
RT suppressor gene at 7q31, in human head and neck cancers.";
RL Oncogene 21:4462-4470(2002).
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 histones 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. This complex may be required for the
CC activation of transcriptional programs associated with oncogene and
CC proto-oncogene mediated growth induction, tumor suppressor mediated
CC growth arrest and replicative senescence, apoptosis, and DNA repair.
CC NuA4 may also play a direct role in DNA repair when directly recruited
CC to sites of DNA damage. Component of a SWR1-like complex that
CC specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC nucleosome. {ECO:0000269|PubMed:12545155, ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:24463511}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC Component of the NuA4 histone acetyltransferase complex which contains
CC the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400,
CC BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin,
CC ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41,
CC VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the
CC adenovirus E1A protein. HTATTIP/TIP60, EPC1, and ING3 together
CC constitute a minimal HAT complex termed Piccolo NuA4. Component of a
CC SWR1-like complex. {ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:19154204,
CC ECO:0000269|PubMed:24463511}.
CC -!- INTERACTION:
CC Q9NXR8; Q93009: USP7; NbExp=2; IntAct=EBI-769503, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NXR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXR8-2; Sequence=VSP_012885, VSP_012886;
CC Name=3;
CC IsoId=Q9NXR8-3; Sequence=VSP_012887, VSP_012888;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC ovaries, placenta, prostate, skeletal muscle, small intestine, spleen,
CC testis and thymus.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:19154204}.
CC -!- DISEASE: Squamous cell carcinoma of the head and neck (HNSCC)
CC [MIM:275355]: A non-melanoma skin cancer affecting the head and neck.
CC The hallmark of cutaneous SCC is malignant transformation of normal
CC epidermal keratinocytes. {ECO:0000269|PubMed:12080476}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28979.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH73865.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF074968; AAG12172.1; -; mRNA.
DR EMBL; AY007790; AAG23285.1; -; mRNA.
DR EMBL; AK000096; BAA90942.1; -; mRNA.
DR EMBL; AK291905; BAF84594.1; -; mRNA.
DR EMBL; AF161419; AAF28979.1; ALT_FRAME; mRNA.
DR EMBL; AL603623; CAC48260.2; -; Transcribed_RNA.
DR EMBL; AC004537; AAQ93373.1; -; Genomic_DNA.
DR EMBL; BC009777; AAH09777.1; -; mRNA.
DR EMBL; BC009777; AAQ93374.1; -; mRNA.
DR EMBL; BC010851; AAH10851.1; -; mRNA.
DR EMBL; BC062634; AAH09776.1; -; mRNA.
DR EMBL; BC062634; AAH62634.1; -; mRNA.
DR EMBL; BC073865; AAH73865.1; ALT_SEQ; mRNA.
DR EMBL; BC093091; AAH93091.1; -; mRNA.
DR EMBL; BC093689; AAH93689.1; -; mRNA.
DR EMBL; BC101609; AAI01610.1; -; mRNA.
DR CCDS; CCDS35497.1; -. [Q9NXR8-2]
DR CCDS; CCDS5778.1; -. [Q9NXR8-1]
DR RefSeq; NP_061944.2; NM_019071.2. [Q9NXR8-1]
DR RefSeq; NP_938008.1; NM_198267.1. [Q9NXR8-2]
DR PDB; 1X4I; NMR; -; A=362-418.
DR PDBsum; 1X4I; -.
DR AlphaFoldDB; Q9NXR8; -.
DR SMR; Q9NXR8; -.
DR BioGRID; 120041; 86.
DR ComplexPortal; CPX-709; Piccolo NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q9NXR8; -.
DR DIP; DIP-34303N; -.
DR IntAct; Q9NXR8; 49.
DR MINT; Q9NXR8; -.
DR STRING; 9606.ENSP00000320566; -.
DR iPTMnet; Q9NXR8; -.
DR PhosphoSitePlus; Q9NXR8; -.
DR BioMuta; ING3; -.
DR EPD; Q9NXR8; -.
DR jPOST; Q9NXR8; -.
DR MassIVE; Q9NXR8; -.
DR MaxQB; Q9NXR8; -.
DR PaxDb; Q9NXR8; -.
DR PeptideAtlas; Q9NXR8; -.
DR PRIDE; Q9NXR8; -.
DR ProteomicsDB; 83128; -. [Q9NXR8-1]
DR ProteomicsDB; 83129; -. [Q9NXR8-2]
DR ProteomicsDB; 83130; -. [Q9NXR8-3]
DR Antibodypedia; 31689; 248 antibodies from 32 providers.
DR DNASU; 54556; -.
DR Ensembl; ENST00000315870.10; ENSP00000320566.5; ENSG00000071243.16. [Q9NXR8-1]
DR Ensembl; ENST00000339121.9; ENSP00000341697.5; ENSG00000071243.16. [Q9NXR8-2]
DR Ensembl; ENST00000427726.5; ENSP00000410406.1; ENSG00000071243.16. [Q9NXR8-3]
DR GeneID; 54556; -.
DR KEGG; hsa:54556; -.
DR MANE-Select; ENST00000315870.10; ENSP00000320566.5; NM_019071.3; NP_061944.2.
DR UCSC; uc003vjl.4; human. [Q9NXR8-1]
DR CTD; 54556; -.
DR DisGeNET; 54556; -.
DR GeneCards; ING3; -.
DR HGNC; HGNC:14587; ING3.
DR HPA; ENSG00000071243; Tissue enriched (bone).
DR MalaCards; ING3; -.
DR MIM; 275355; phenotype.
DR MIM; 607493; gene.
DR neXtProt; NX_Q9NXR8; -.
DR OpenTargets; ENSG00000071243; -.
DR PharmGKB; PA29875; -.
DR VEuPathDB; HostDB:ENSG00000071243; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000156619; -.
DR HOGENOM; CLU_031900_0_0_1; -.
DR InParanoid; Q9NXR8; -.
DR OMA; YEWFHWK; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9NXR8; -.
DR TreeFam; TF106497; -.
DR PathwayCommons; Q9NXR8; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9NXR8; -.
DR BioGRID-ORCS; 54556; 370 hits in 1098 CRISPR screens.
DR ChiTaRS; ING3; human.
DR EvolutionaryTrace; Q9NXR8; -.
DR GeneWiki; ING3; -.
DR GenomeRNAi; 54556; -.
DR Pharos; Q9NXR8; Tbio.
DR PRO; PR:Q9NXR8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NXR8; protein.
DR Bgee; ENSG00000071243; Expressed in secondary oocyte and 204 other tissues.
DR ExpressionAtlas; Q9NXR8; baseline and differential.
DR Genevisible; Q9NXR8; HS.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Direct protein sequencing; Disease variant; Growth regulation;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..418
FT /note="Inhibitor of growth protein 3"
FT /id="PRO_0000212665"
FT ZN_FING 360..409
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 127..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 362
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 373
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 377
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 385
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK6"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 90..93
FT /note="VDRH -> DLWN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012887"
FT VAR_SEQ 90..92
FT /note="VDR -> QHF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_012885"
FT VAR_SEQ 93..418
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_012886"
FT VAR_SEQ 94..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012888"
FT VARIANT 20
FT /note="D -> G (in HNSCC)"
FT /evidence="ECO:0000269|PubMed:12080476"
FT /id="VAR_021263"
FT CONFLICT 325
FT /note="C -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="Q -> QV (in Ref. 5; CAC48260)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="Missing (in Ref. 5; CAC48260)"
FT /evidence="ECO:0000305"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:1X4I"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:1X4I"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:1X4I"
SQ SEQUENCE 418 AA; 46743 MW; AA127416912D87F5 CRC64;
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE
QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE
RRSLELDTPS QPVNNHHAHS HTPVEKRKYN PTSHHTTTDH IPEKKFKSEA LLSTLTSDAS
KENTLGCRNN NSTASSNNAY NVNSSQPLGS YNIGSLSSGT GAGAITMAAA QAVQATAQMK
EGRRTSSLKA SYEAFKNNDF QLGKEFSMAR ETVGYSSSSA LMTTLTQNAS SSAADSRSGR
KSKNNNKSSS QQSSSSSSSS SLSSCSSSST VVQEISQQTT VVPESDSNSQ VDWTYDPNEP
RYCICNQVSY GEMVGCDNQD CPIEWFHYGC VGLTEAPKGK WYCPQCTAAM KRRGSRHK
