ING5_HUMAN
ID ING5_HUMAN Reviewed; 240 AA.
AC Q8WYH8; A8K1P3; Q53NU6; Q57Z54; Q9BS30;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Inhibitor of growth protein 5;
DE AltName: Full=p28ING5;
GN Name=ING5;
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), FUNCTION, AND INTERACTION WITH
RP EP300 AND 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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX AND THE MOZ/MORF 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 [7]
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 [8]
RP IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18794358; DOI=10.1128/mcb.01297-08;
RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
RA Yang X.-J.;
RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase
RT complexes.";
RL Mol. Cell. Biol. 28:6828-6843(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION, INTERACTION WITH INCA1, AND TISSUE SPECIFICITY.
RX PubMed=21750715; DOI=10.1371/journal.pone.0021505;
RA Zhang F., Baeumer N., Rode M., Ji P., Zhang T., Berdel W.E.,
RA Mueller-Tidow C.;
RT "The inhibitor of growth protein 5 (ING5) depends on INCA1 as a co-factor
RT for its antiproliferative effects.";
RL PLoS ONE 6:E21505-E21505(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE HBO1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24065767; DOI=10.1101/gad.223396.113;
RA Lalonde M.E., Avvakumov N., Glass K.C., Joncas F.H., Saksouk N.,
RA Holliday M., Paquet E., Yan K., Tong Q., Klein B.J., Tan S., Yang X.J.,
RA Kutateladze T.G., Cote J.;
RT "Exchange of associated factors directs a switch in HBO1 acetyltransferase
RT histone tail specificity.";
RL Genes Dev. 27:2009-2024(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 184-236 IN COMPLEX WITH HISTONE
RP H2K4ME3 AND ZINC, AND SUBUNIT.
RX PubMed=18623064; DOI=10.1002/prot.22140;
RA Champagne K.S., Saksouk N., Pena P.V., Johnson K., Ullah M., Yang X.J.,
RA Cote J., Kutateladze T.G.;
RT "The crystal structure of the ING5 PHD finger in complex with an H3K4me3
RT histone peptide.";
RL Proteins 72:1371-1376(2008).
CC -!- FUNCTION: Component of the HBO1 complex, which specifically mediates
CC acetylation of histone H3 at 'Lys-14' (H3K14ac) and, to a lower extent,
CC acetylation of histone H4 (PubMed:24065767). Component of the MOZ/MORF
CC complex which has a histone H3 acetyltransferase activity
CC (PubMed:16387653). Through chromatin acetylation it may regulate DNA
CC replication and may function as a transcriptional coactivator
CC (PubMed:12750254, PubMed:16387653). Inhibits cell growth, induces a
CC delay in S-phase progression and enhances Fas-induced apoptosis in an
CC INCA1-dependent manner (PubMed:21750715). {ECO:0000269|PubMed:12750254,
CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:21750715,
CC ECO:0000269|PubMed:24065767}.
CC -!- SUBUNIT: Component of the HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING5, and one scaffold subunit: complexes containing BRPF scaffold
CC (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards
CC H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2 and
CC JADE3) mediate acetylation of histone H4 (PubMed:16387653,
CC PubMed:24065767). Component of the MOZ/MORF complex composed at least
CC of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3
CC (PubMed:16387653, PubMed:18794358). Interacts with H3K4me3 and to a
CC lesser extent with H3K4me2 (PubMed:16728974, PubMed:18623064).
CC Interacts with EP300 and p53/TP53 (PubMed:12750254). Interacts with
CC INCA1 (PubMed:21750715). {ECO:0000269|PubMed:12750254,
CC ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16728974,
CC ECO:0000269|PubMed:18623064, ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:21750715, ECO:0000269|PubMed:24065767}.
CC -!- INTERACTION:
CC Q8WYH8; P53365: ARFIP2; NbExp=3; IntAct=EBI-488533, EBI-638194;
CC Q8WYH8; Q00994: BEX3; NbExp=3; IntAct=EBI-488533, EBI-741753;
CC Q8WYH8; P55201-2: BRPF1; NbExp=3; IntAct=EBI-488533, EBI-12065306;
CC Q8WYH8; Q6ZUJ4: C3orf62; NbExp=3; IntAct=EBI-488533, EBI-2837036;
CC Q8WYH8; Q8NA61-2: CBY2; NbExp=6; IntAct=EBI-488533, EBI-11524851;
CC Q8WYH8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-488533, EBI-10175300;
CC Q8WYH8; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-488533, EBI-5278764;
CC Q8WYH8; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-488533, EBI-744115;
CC Q8WYH8; Q05D60: DEUP1; NbExp=3; IntAct=EBI-488533, EBI-748597;
CC Q8WYH8; Q9UJY5-4: GGA1; NbExp=3; IntAct=EBI-488533, EBI-12108696;
CC Q8WYH8; Q4V328: GRIPAP1; NbExp=6; IntAct=EBI-488533, EBI-717919;
CC Q8WYH8; O14964: HGS; NbExp=6; IntAct=EBI-488533, EBI-740220;
CC Q8WYH8; Q05084: ICA1; NbExp=3; IntAct=EBI-488533, EBI-1046751;
CC Q8WYH8; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-488533, EBI-747204;
CC Q8WYH8; Q0VD86: INCA1; NbExp=4; IntAct=EBI-488533, EBI-6509505;
CC Q8WYH8; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-488533, EBI-12094820;
CC Q8WYH8; Q9NQC1: JADE2; NbExp=4; IntAct=EBI-488533, EBI-2796167;
CC Q8WYH8; Q6A162: KRT40; NbExp=3; IntAct=EBI-488533, EBI-10171697;
CC Q8WYH8; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-488533, EBI-10172290;
CC Q8WYH8; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-488533, EBI-739657;
CC Q8WYH8; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-488533, EBI-10182361;
CC Q8WYH8; Q8IVL1: NAV2; NbExp=4; IntAct=EBI-488533, EBI-741200;
CC Q8WYH8; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-488533, EBI-9090919;
CC Q8WYH8; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-488533, EBI-1504830;
CC Q8WYH8; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-488533, EBI-455078;
CC Q8WYH8; P51687: SUOX; NbExp=3; IntAct=EBI-488533, EBI-3921347;
CC Q8WYH8; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-488533, EBI-3925505;
CC Q8WYH8; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-488533, EBI-11059915;
CC Q8WYH8; Q92558: WASF1; NbExp=3; IntAct=EBI-488533, EBI-1548747;
CC Q8WYH8-2; Q53GS7: GLE1; NbExp=3; IntAct=EBI-21602071, EBI-1955541;
CC Q8WYH8-2; P42858: HTT; NbExp=18; IntAct=EBI-21602071, EBI-466029;
CC Q8WYH8-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-21602071, EBI-10975473;
CC Q8WYH8-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-21602071, EBI-5235340;
CC Q8WYH8-2; O76024: WFS1; NbExp=3; IntAct=EBI-21602071, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18794358}. Chromosome
CC {ECO:0000269|PubMed:24065767}. Note=Localizes to transcription start
CC sites. {ECO:0000269|PubMed:24065767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WYH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WYH8-2; Sequence=VSP_012528;
CC -!- TISSUE SPECIFICITY: Down-regulated in bone marrow cells in acute
CC myeloid leukemia patients as compared with normal bone marrow cells.
CC {ECO:0000269|PubMed:21750715}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:16728974}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; AF189286; AAL68979.1; -; mRNA.
DR EMBL; AK074422; BAB85078.1; -; mRNA.
DR EMBL; AK289958; BAF82647.1; -; mRNA.
DR EMBL; AC114730; AAX82019.1; -; Genomic_DNA.
DR EMBL; AC133528; AAY14921.1; -; Genomic_DNA.
DR EMBL; BC005370; AAH05370.1; -; mRNA.
DR EMBL; BC071899; AAH71899.1; -; mRNA.
DR CCDS; CCDS33425.1; -. [Q8WYH8-1]
DR CCDS; CCDS82586.1; -. [Q8WYH8-2]
DR RefSeq; NP_001317091.1; NM_001330162.1. [Q8WYH8-2]
DR RefSeq; NP_115705.2; NM_032329.5. [Q8WYH8-1]
DR PDB; 3C6W; X-ray; 1.75 A; A/C=184-236.
DR PDB; 5ME8; X-ray; 3.20 A; A/B=1-105.
DR PDB; 5MTO; X-ray; 3.10 A; A/B=1-105.
DR PDBsum; 3C6W; -.
DR PDBsum; 5ME8; -.
DR PDBsum; 5MTO; -.
DR AlphaFoldDB; Q8WYH8; -.
DR SMR; Q8WYH8; -.
DR BioGRID; 124016; 108.
DR ComplexPortal; CPX-721; HBO1-5.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-722; HBO1-5.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-723; HBO1-5.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-727; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-733; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-736; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-738; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-739; MORF2 histone acetyltransferase complex.
DR ComplexPortal; CPX-740; MORF3 histone acetyltransferase complex.
DR CORUM; Q8WYH8; -.
DR DIP; DIP-32511N; -.
DR IntAct; Q8WYH8; 63.
DR MINT; Q8WYH8; -.
DR STRING; 9606.ENSP00000322142; -.
DR iPTMnet; Q8WYH8; -.
DR PhosphoSitePlus; Q8WYH8; -.
DR BioMuta; ING5; -.
DR DMDM; 57012960; -.
DR EPD; Q8WYH8; -.
DR jPOST; Q8WYH8; -.
DR MassIVE; Q8WYH8; -.
DR MaxQB; Q8WYH8; -.
DR PaxDb; Q8WYH8; -.
DR PeptideAtlas; Q8WYH8; -.
DR PRIDE; Q8WYH8; -.
DR ProteomicsDB; 75158; -. [Q8WYH8-1]
DR ProteomicsDB; 75159; -. [Q8WYH8-2]
DR Antibodypedia; 34573; 237 antibodies from 31 providers.
DR DNASU; 84289; -.
DR Ensembl; ENST00000313552.11; ENSP00000322142.7; ENSG00000168395.16. [Q8WYH8-1]
DR Ensembl; ENST00000406941.5; ENSP00000385937.1; ENSG00000168395.16. [Q8WYH8-2]
DR GeneID; 84289; -.
DR KEGG; hsa:84289; -.
DR MANE-Select; ENST00000313552.11; ENSP00000322142.7; NM_032329.6; NP_115705.2.
DR UCSC; uc002wcd.4; human. [Q8WYH8-1]
DR CTD; 84289; -.
DR DisGeNET; 84289; -.
DR GeneCards; ING5; -.
DR HGNC; HGNC:19421; ING5.
DR HPA; ENSG00000168395; Low tissue specificity.
DR MIM; 608525; gene.
DR neXtProt; NX_Q8WYH8; -.
DR OpenTargets; ENSG00000168395; -.
DR PharmGKB; PA134935441; -.
DR VEuPathDB; HostDB:ENSG00000168395; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000158159; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q8WYH8; -.
DR OMA; QPKGKWF; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q8WYH8; -.
DR TreeFam; TF352014; -.
DR PathwayCommons; Q8WYH8; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR SignaLink; Q8WYH8; -.
DR BioGRID-ORCS; 84289; 23 hits in 1082 CRISPR screens.
DR EvolutionaryTrace; Q8WYH8; -.
DR GeneWiki; ING5; -.
DR GenomeRNAi; 84289; -.
DR Pharos; Q8WYH8; Tbio.
DR PRO; PR:Q8WYH8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WYH8; protein.
DR Bgee; ENSG00000168395; Expressed in sural nerve and 178 other tissues.
DR ExpressionAtlas; Q8WYH8; baseline and differential.
DR Genevisible; Q8WYH8; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:ComplexPortal.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:ComplexPortal.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:ComplexPortal.
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:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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:0001558; P:regulation of cell growth; IDA:ComplexPortal.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
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; Activator; Alternative splicing;
KW Chromatin regulator; Chromosome; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..240
FT /note="Inhibitor of growth protein 5"
FT /id="PRO_0000212671"
FT ZN_FING 186..235
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 116..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT SITE 188
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT SITE 199
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT SITE 203
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT SITE 211
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:18623064,
FT ECO:0007744|PDB:3C6W"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 126
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 227..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012528"
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:5MTO"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:5ME8"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5MTO"
FT HELIX 19..52
FT /evidence="ECO:0007829|PDB:5MTO"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:5MTO"
FT HELIX 58..100
FT /evidence="ECO:0007829|PDB:5MTO"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3C6W"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3C6W"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3C6W"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3C6W"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:3C6W"
SQ SEQUENCE 240 AA; 27751 MW; B66DA23209EE9B9E CRC64;
MATAMYLEHY LDSIENLPCE LQRNFQLMRE LDQRTEDKKA EIDILAAEYI STVKTLSPDQ
RVERLQKIQN AYSKCKEYSD DKVQLAMQTY EMVDKHIRRL DADLARFEAD LKDKMEGSDF
ESSGGRGLKK GRGQKEKRGS RGRGRRTSEE DTPKKKKHKG GSEFTDTILS VHPSDVLDMP
VDPNEPTYCL CHQVSYGEMI GCDNPDCPIE WFHFACVDLT TKPKGKWFCP RCVQEKRKKK
