ING4_HUMAN
ID ING4_HUMAN Reviewed; 249 AA.
AC Q9UNL4; A4KYM4; A4KYM6; D3DUR8; Q0EF62; Q0EF63; Q4VBQ6; Q96E15; Q9H3J0;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Inhibitor of growth protein 4;
DE AltName: Full=p29ING4;
GN Name=ING4; ORFNames=My036;
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 INTERACTION WITH EP300 AND
RP TP53.
RC TISSUE=Placenta;
RX PubMed=12750254;
RA Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K.,
RA Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.;
RT "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.";
RL Cancer Res. 63:2373-2378(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5; 6 AND 7), SUBCELLULAR
RP LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=16973615; DOI=10.1074/jbc.m606296200;
RA Unoki M., Shen J.C., Zheng Z.M., Harris C.C.;
RT "Novel splice variants of ING4 and their possible roles in the regulation
RT of cell growth and motility.";
RL J. Biol. Chem. 281:34677-34686(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 8), AND ALTERNATIVE SPLICING
RP (ISOFORM 8).
RX PubMed=17325660; DOI=10.1038/sj.onc.1210335;
RA Raho G., Miranda C., Tamborini E., Pierotti M.A., Greco A.;
RT "Detection of novel mRNA splice variants of human ING4 tumor suppressor
RT gene.";
RL Oncogene 26:5247-5257(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=B-cell, Lung, and Pituitary;
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 FUNCTION.
RX PubMed=15251430; DOI=10.1016/j.febslet.2004.06.010;
RA Zhang X., Xu L.-S., Wang Z.-Q., Wang K.-S., Li N., Cheng Z.-H.,
RA Huang S.-Z., Wei D.-Z., Han Z.-G.;
RT "ING4 induces G2/M cell cycle arrest and enhances the chemosensitivity to
RT DNA-damage agents in HepG2 cells.";
RL FEBS Lett. 570:7-12(2004).
RN [9]
RP FUNCTION, INTERACTION WITH RELA, AND SUBCELLULAR LOCATION.
RX PubMed=15029197; DOI=10.1038/nature02329;
RA Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E.,
RA Barnett G.H., Jain R.K.;
RT "The candidate tumour suppressor protein ING4 regulates brain tumour growth
RT and angiogenesis.";
RL Nature 428:328-332(2004).
RN [10]
RP FUNCTION.
RX PubMed=15528276; DOI=10.1073/pnas.0407158101;
RA Kim S., Chin K., Gray J.W., Bishop J.M.;
RT "A screen for genes that suppress loss of contact inhibition:
RT Identification of ING4 as a candidate tumor suppressor gene in human
RT cancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16251-16256(2004).
RN [11]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=15882981; DOI=10.1016/j.bbrc.2005.04.023;
RA Zhang X., Wang K.S., Wang Z.Q., Xu L.S., Wang Q.W., Chen F., Wei D.Z.,
RA Han Z.G.;
RT "Nuclear localization signal of ING4 plays a key role in its binding to
RT p53.";
RL Biochem. Biophys. Res. Commun. 331:1032-1038(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH EGLN1.
RX PubMed=15897452; DOI=10.1073/pnas.0502716102;
RA Ozer A., Wu L.C., Bruick R.K.;
RT "The candidate tumor suppressor ING4 represses activation of the hypoxia
RT inducible factor (HIF).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7481-7486(2005).
RN [13]
RP FUNCTION IN HISTONE ACETYLATION, FUNCTION IN DNA REPLICATION, FUNCTION IN
RP TP53-MEDIATED TRANSCRIPTION, AND IDENTIFICATION IN THE HBO1 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 [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112; LYS-127; LYS-146; LYS-148
RP AND LYS-156, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-127
RP (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP CITRULLINATION AT ARG-133 AND ARG-166, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=21454715; DOI=10.1074/jbc.m111.230961;
RA Guo Q., Fast W.;
RT "Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine
RT deminase 4 (PAD4) disrupts the interaction between ING4 and p53.";
RL J. Biol. Chem. 286:17069-17078(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 188-245 IN COMPLEX WITH H3K4ME3,
RP DOMAIN PHD, AND SUBUNIT.
RX PubMed=18381289; DOI=10.1074/jbc.m710020200;
RA Palacios A., Munoz I.G., Pantoja-Uceda D., Marcaida M.J., Torres D.,
RA Martin-Garcia J.M., Luque I., Montoya G., Blanco F.J.;
RT "Molecular basis of histone H3K4me3 recognition by ING4.";
RL J. Biol. Chem. 283:15956-15964(2008).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 194-246, AND SUBUNIT.
RX PubMed=19187765; DOI=10.1016/j.molcel.2008.12.016;
RA Hung T., Binda O., Champagne K.S., Kuo A.J., Johnson K., Chang H.Y.,
RA Simon M.D., Kutateladze T.G., Gozani O.;
RT "ING4 mediates crosstalk between histone H3 K4 trimethylation and H3
RT acetylation to attenuate cellular transformation.";
RL Mol. Cell 33:248-256(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 2-105, COILED-COIL DOMAIN, AND
RP SUBUNIT.
RX PubMed=22334692; DOI=10.1074/jbc.m111.330001;
RA Culurgioni S., Munoz I.G., Moreno A., Palacios A., Villate M., Palmero I.,
RA Montoya G., Blanco F.J.;
RT "Crystal structure of inhibitor of growth 4 (ING4) dimerization domain
RT reveals functional organization of ING family of chromatin-binding
RT proteins.";
RL J. Biol. Chem. 287:10876-10884(2012).
CC -!- FUNCTION: Component of HBO1 complexes, which specifically mediate
CC acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced
CC activity toward histone H4 (PubMed:16387653). Through chromatin
CC acetylation it may function in DNA replication (PubMed:16387653). May
CC inhibit tumor progression by modulating the transcriptional output of
CC signaling pathways which regulate cell proliferation (PubMed:15251430,
CC PubMed:15528276). Can suppress brain tumor angiogenesis through
CC transcriptional repression of RELA/NFKB3 target genes when complexed
CC with RELA (PubMed:15029197). May also specifically suppress loss of
CC contact inhibition elicited by activated oncogenes such as MYC
CC (PubMed:15029197). Represses hypoxia inducible factor's (HIF) activity
CC by interacting with HIF prolyl hydroxylase 2 (EGLN1) (PubMed:15897452).
CC Can enhance apoptosis induced by serum starvation in mammary epithelial
CC cell line HC11 (By similarity). {ECO:0000250|UniProtKB:Q8C0D7,
CC ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:15251430,
CC ECO:0000269|PubMed:15528276, ECO:0000269|PubMed:15897452,
CC ECO:0000269|PubMed:16387653}.
CC -!- SUBUNIT: Homodimer (PubMed:19187765, PubMed:22334692). Component of the
CC HBO1 complex composed of KAT7/HBO1, MEAF6, ING4 or ING5, and one
CC scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2
CC or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes
CC containing JADE scaffold (JADE1, JADE2 and JADE3) mediate acetylation
CC of histone H4 (PubMed:16387653). Interacts with H3K4me3 and to a lesser
CC extent with H3K4me2, the interaction augments KAT7/HBO1 acetylation
CC activity on H3 tails (PubMed:16728974, PubMed:18381289). Interacts with
CC EP300, RELA and TP53; these interactions may be indirect
CC (PubMed:12750254, PubMed:15029197). Interacts with EGLN1
CC (PubMed:15897452). Interacts with BCL2A1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8C0D7, ECO:0000269|PubMed:12750254,
CC ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:15897452,
CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16728974,
CC ECO:0000269|PubMed:18381289, ECO:0000269|PubMed:19187765,
CC ECO:0000269|PubMed:22334692}.
CC -!- INTERACTION:
CC Q9UNL4; Q00994: BEX3; NbExp=3; IntAct=EBI-2866661, EBI-741753;
CC Q9UNL4; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-2866661, EBI-717919;
CC Q9UNL4; P28799: GRN; NbExp=3; IntAct=EBI-2866661, EBI-747754;
CC Q9UNL4; P68431: H3C12; NbExp=3; IntAct=EBI-2866661, EBI-79722;
CC Q9UNL4; Q14103: HNRNPD; NbExp=9; IntAct=EBI-2866661, EBI-299674;
CC Q9UNL4; Q14103-4: HNRNPD; NbExp=2; IntAct=EBI-2866661, EBI-432545;
CC Q9UNL4; P42858: HTT; NbExp=3; IntAct=EBI-2866661, EBI-466029;
CC Q9UNL4; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-2866661, EBI-12094820;
CC Q9UNL4; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-2866661, EBI-741200;
CC Q9UNL4; O43933: PEX1; NbExp=3; IntAct=EBI-2866661, EBI-988601;
CC Q9UNL4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2866661, EBI-396669;
CC Q9UNL4; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2866661, EBI-5235340;
CC Q9UNL4; O76024: WFS1; NbExp=3; IntAct=EBI-2866661, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15029197,
CC ECO:0000269|PubMed:16973615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=ING4_v1;
CC IsoId=Q9UNL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UNL4-2; Sequence=VSP_012518, VSP_012519;
CC Name=3; Synonyms=deltaEx2;
CC IsoId=Q9UNL4-3; Sequence=VSP_041288;
CC Name=4; Synonyms=ING4_v4;
CC IsoId=Q9UNL4-4; Sequence=VSP_041291;
CC Name=5;
CC IsoId=Q9UNL4-5; Sequence=VSP_041289;
CC Name=6; Synonyms=ING4_v2;
CC IsoId=Q9UNL4-6; Sequence=VSP_041292;
CC Name=7; Synonyms=ING4_v3;
CC IsoId=Q9UNL4-7; Sequence=VSP_041290;
CC Name=8; Synonyms=deltaEx6A;
CC IsoId=Q9UNL4-8; Sequence=VSP_041293;
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:18381289}.
CC -!- DOMAIN: The N-terminal coiled-coil domain mediates homodimerization.
CC {ECO:0000269|PubMed:22334692}.
CC -!- PTM: Citrullination by PADI4 within the nuclear localization signal
CC disrupts the interaction with p53 and increases susceptibility to
CC degradation. {ECO:0000269|PubMed:21454715}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Lacks the nuclear localization signal
CC (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Lacks the nuclear localization signal
CC (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Lacks the nuclear localization signal
CC (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43153.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ING4ID40978ch12p13.html";
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DR EMBL; AF156552; AAL79773.1; -; mRNA.
DR EMBL; AB197695; BAF30477.1; -; mRNA.
DR EMBL; AB197696; BAF30478.1; -; mRNA.
DR EMBL; AB197697; BAF30479.1; -; mRNA.
DR EMBL; EF152349; ABO61139.1; -; mRNA.
DR EMBL; EF152351; ABO61141.1; -; mRNA.
DR EMBL; AF063594; AAG43153.1; ALT_FRAME; mRNA.
DR EMBL; AF110645; AAD48585.1; -; mRNA.
DR EMBL; CH471116; EAW88763.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88768.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88770.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88772.1; -; Genomic_DNA.
DR EMBL; BC007781; AAH07781.1; -; mRNA.
DR EMBL; BC013038; AAH13038.2; -; mRNA.
DR EMBL; BC095434; AAH95434.1; -; mRNA.
DR CCDS; CCDS44812.1; -. [Q9UNL4-3]
DR CCDS; CCDS44813.1; -. [Q9UNL4-1]
DR CCDS; CCDS44814.1; -. [Q9UNL4-5]
DR CCDS; CCDS44815.1; -. [Q9UNL4-4]
DR CCDS; CCDS44816.1; -. [Q9UNL4-8]
DR CCDS; CCDS8555.1; -. [Q9UNL4-2]
DR RefSeq; NP_001121054.1; NM_001127582.1. [Q9UNL4-1]
DR RefSeq; NP_001121055.1; NM_001127583.1. [Q9UNL4-5]
DR RefSeq; NP_001121056.1; NM_001127584.1. [Q9UNL4-4]
DR RefSeq; NP_001121057.1; NM_001127585.1. [Q9UNL4-3]
DR RefSeq; NP_001121058.1; NM_001127586.1. [Q9UNL4-8]
DR RefSeq; NP_057246.2; NM_016162.3. [Q9UNL4-2]
DR PDB; 2K1J; NMR; -; A=188-249.
DR PDB; 2M1R; NMR; -; A=188-249.
DR PDB; 2PNX; X-ray; 1.80 A; A/C=194-246.
DR PDB; 2VNF; X-ray; 1.76 A; A/C=188-246.
DR PDB; 4AFL; X-ray; 2.28 A; A/B/C/D/E/F=2-105.
DR PDBsum; 2K1J; -.
DR PDBsum; 2M1R; -.
DR PDBsum; 2PNX; -.
DR PDBsum; 2VNF; -.
DR PDBsum; 4AFL; -.
DR AlphaFoldDB; Q9UNL4; -.
DR BMRB; Q9UNL4; -.
DR SMR; Q9UNL4; -.
DR BioGRID; 119331; 77.
DR ComplexPortal; CPX-718; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-719; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-720; HBO1-4.3 histone acetyltransferase complex.
DR CORUM; Q9UNL4; -.
DR DIP; DIP-42222N; -.
DR IntAct; Q9UNL4; 51.
DR MINT; Q9UNL4; -.
DR STRING; 9606.ENSP00000380024; -.
DR iPTMnet; Q9UNL4; -.
DR PhosphoSitePlus; Q9UNL4; -.
DR BioMuta; ING4; -.
DR DMDM; 57012981; -.
DR EPD; Q9UNL4; -.
DR jPOST; Q9UNL4; -.
DR MassIVE; Q9UNL4; -.
DR MaxQB; Q9UNL4; -.
DR PaxDb; Q9UNL4; -.
DR PeptideAtlas; Q9UNL4; -.
DR PRIDE; Q9UNL4; -.
DR ProteomicsDB; 85303; -. [Q9UNL4-1]
DR ProteomicsDB; 85304; -. [Q9UNL4-2]
DR ProteomicsDB; 85305; -. [Q9UNL4-3]
DR ProteomicsDB; 85306; -. [Q9UNL4-4]
DR ProteomicsDB; 85307; -. [Q9UNL4-5]
DR ProteomicsDB; 85308; -. [Q9UNL4-6]
DR ProteomicsDB; 85309; -. [Q9UNL4-7]
DR ProteomicsDB; 85310; -. [Q9UNL4-8]
DR Antibodypedia; 22581; 267 antibodies from 32 providers.
DR DNASU; 51147; -.
DR Ensembl; ENST00000341550.9; ENSP00000343396.4; ENSG00000111653.20. [Q9UNL4-2]
DR Ensembl; ENST00000396807.8; ENSP00000380024.4; ENSG00000111653.20. [Q9UNL4-1]
DR Ensembl; ENST00000412586.6; ENSP00000412705.2; ENSG00000111653.20. [Q9UNL4-5]
DR Ensembl; ENST00000423703.6; ENSP00000414008.2; ENSG00000111653.20. [Q9UNL4-8]
DR Ensembl; ENST00000444704.5; ENSP00000397343.2; ENSG00000111653.20. [Q9UNL4-3]
DR Ensembl; ENST00000446105.6; ENSP00000415903.2; ENSG00000111653.20. [Q9UNL4-4]
DR GeneID; 51147; -.
DR KEGG; hsa:51147; -.
DR MANE-Select; ENST00000341550.9; ENSP00000343396.4; NM_016162.4; NP_057246.2. [Q9UNL4-2]
DR UCSC; uc001qpv.5; human. [Q9UNL4-1]
DR CTD; 51147; -.
DR DisGeNET; 51147; -.
DR GeneCards; ING4; -.
DR HGNC; HGNC:19423; ING4.
DR HPA; ENSG00000111653; Low tissue specificity.
DR MIM; 608524; gene.
DR neXtProt; NX_Q9UNL4; -.
DR OpenTargets; ENSG00000111653; -.
DR PharmGKB; PA134976283; -.
DR VEuPathDB; HostDB:ENSG00000111653; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000159033; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q9UNL4; -.
DR OMA; SHGQMIM; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9UNL4; -.
DR TreeFam; TF352014; -.
DR PathwayCommons; Q9UNL4; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9UNL4; -.
DR SIGNOR; Q9UNL4; -.
DR BioGRID-ORCS; 51147; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; ING4; human.
DR EvolutionaryTrace; Q9UNL4; -.
DR GeneWiki; ING4; -.
DR GenomeRNAi; 51147; -.
DR Pharos; Q9UNL4; Tbio.
DR PRO; PR:Q9UNL4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UNL4; protein.
DR Bgee; ENSG00000111653; Expressed in cortical plate and 186 other tissues.
DR ExpressionAtlas; Q9UNL4; baseline and differential.
DR Genevisible; Q9UNL4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; 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:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1902164; P:positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IDA:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR DisProt; DP01347; -.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028638; ING4/ING5.
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:SF41; PTHR10333:SF41; 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; Apoptosis; Cell cycle;
KW Chromatin regulator; Citrullination; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..249
FT /note="Inhibitor of growth protein 4"
FT /id="PRO_0000212668"
FT ZN_FING 196..245
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 115..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..118
FT /evidence="ECO:0000269|PubMed:22334692"
FT MOTIF 127..148
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 223
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="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 198
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 209
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 213
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 221
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0D7"
FT MOD_RES 133
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:21454715"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 166
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:21454715"
FT VAR_SEQ 13..37
FT /note="SIENLPFELQRNFQLMRDLDQRTED -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17325660"
FT /id="VSP_041288"
FT VAR_SEQ 128..131
FT /note="GKKK -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16973615"
FT /id="VSP_041289"
FT VAR_SEQ 128..130
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16973615"
FT /id="VSP_041290"
FT VAR_SEQ 129..132
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16973615"
FT /id="VSP_041291"
FT VAR_SEQ 131
FT /note="K -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16973615, ECO:0000303|Ref.4"
FT /id="VSP_012518"
FT VAR_SEQ 131
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16973615"
FT /id="VSP_041292"
FT VAR_SEQ 132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16973615, ECO:0000303|Ref.4"
FT /id="VSP_012519"
FT VAR_SEQ 168..249
FT /note="SPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSI
FT EWFHFACVGLTTKPRGKWFCPRCSQERKKK -> VPLSGSILPVWG (in isoform
FT 8)"
FT /evidence="ECO:0000303|PubMed:17325660"
FT /id="VSP_041293"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:4AFL"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4AFL"
FT HELIX 17..50
FT /evidence="ECO:0007829|PDB:4AFL"
FT HELIX 58..103
FT /evidence="ECO:0007829|PDB:4AFL"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:2VNF"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2VNF"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2VNF"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2VNF"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:2VNF"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2M1R"
FT MOD_RES Q9UNL4-4:114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES Q9UNL4-4:127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 249 AA; 28530 MW; CE3FD9CC9F0CE949 CRC64;
MAAGMYLEHY LDSIENLPFE LQRNFQLMRD LDQRTEDLKA EIDKLATEYM SSARSLSSEE
KLALLKQIQE AYGKCKEFGD DKVQLAMQTY EMVDKHIRRL DTDLARFEAD LKEKQIESSD
YDSSSSKGKK KGRTQKEKKA ARARSKGKNS DEEAPKTAQK KLKLVRTSPE YGMPSVTFGS
VHPSDVLDMP VDPNEPTYCL CHQVSYGEMI GCDNPDCSIE WFHFACVGLT TKPRGKWFCP
RCSQERKKK
