ID ING1_HUMAN Reviewed; 422 AA. AC Q9UK53; O00532; O43658; Q53ZR3; Q5T9G8; Q5T9G9; Q5T9H0; Q5T9H1; Q9H007; AC Q9HD98; Q9HD99; Q9NS83; Q9P0U6; Q9UBC6; Q9UIJ1; Q9UIJ2; Q9UIJ3; Q9UIJ4; AC Q9UK52; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Inhibitor of growth protein 1; GN Name=ING1; 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] (ISOFORMS 1 AND 2), AND VARIANT ARG-125. RX PubMed=8944021; DOI=10.1038/ng1296-415; RA Garkavtsev I.A., Kazarov A.R., Gudkov A.V., Riabowol K.; RT "Suppression of the novel growth inhibitor p33ING1 promotes neoplastic RT transformation."; RL Nat. Genet. 14:415-420(1996). RN [2] RP ERRATUM OF PUBMED:8944021. RA Garkavtsev I.A., Kazarov A.R., Gudkov A.V., Riabowol K.; RL Nat. Genet. 23:373-373(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND TISSUE SPECIFICITY. RC TISSUE=Mammary cancer, and Testis; RX PubMed=10626813; RA Jaeger D., Stockert E., Scanlan M.J., Guere A.O., Jaeger E., Knuth A., RA Old L.J., Chen Y.-T.; RT "Cancer-testis antigens and ING1 tumor suppressor gene product are breast RT cancer antigens: characterization of tissue-specific ING1 transcripts and a RT homologue gene."; RL Cancer Res. 59:6197-6204(1999). RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2). RX PubMed=10779953; RA Baranova A.V., Ivanov D.V., Makeeva N.V., Corcoran M., Nikitin E.A., RA Borodina T.A., Poltaraus A.B., Glinshchikova O.A., Sudarikov A.B., RA Oscier D., Iankovskii N.K.; RT "Genomic organization of the suppressor gene for tumor growth ING1."; RL Mol. Biol. (Mosk.) 34:263-269(2000). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 5), AND VARIANTS RP HNSCC ARG-125; ASP-335; SER-358 AND SER-359. RX PubMed=10866301; RA Gunduz M., Ouchida M., Fukushima K., Hanafusa H., Etani T., Nishioka S., RA Nishizaki K., Shimizu K.; RT "Genomic structure of the human ING1 gene and tumor-specific mutations RT detected in head and neck squamous cell carcinomas."; RL Cancer Res. 60:3143-3146(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP ARG-125. RX PubMed=10807544; DOI=10.1007/s100380050206; RA Saito A., Furukawa T., Fukushige S., Koyama S., Hoshi M., Hayashi Y., RA Horii A.; RT "p24/ING1-ALT1 and p47/ING1-ALT2, distinct alternative transcripts of RT p33/ING1."; RL J. Hum. Genet. 45:177-181(2000). RN [7] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC TISSUE=Brain; RA Nouman G.S., Anderson J.J., Angus B., Lunec J.; RT "Supplement: sequencing of ING1 tumour suppressor gene cDNAs generated from RT mRNA recovered from normal and neoplastic cell lines."; RL J. Pathol. 192:266-266(2000). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2). 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [11] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [13] RP FUNCTION, AND INTERACTION WITH TP53. RX PubMed=9440695; DOI=10.1038/34675; RA Garkavtsev I.A., Grigorian I.A., Ossovskaya V.S., Chernov M.V., RA Chumakov P.M., Gudkov A.V.; RT "The candidate tumour suppressor p33ING1 cooperates with p53 in cell growth RT control."; RL Nature 391:295-298(1998). 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 INTERACTION WITH RSL1D1. RX PubMed=22419112; DOI=10.1038/cddis.2012.22; RA Li N., Zhao G., Chen T., Xue L., Ma L., Niu J., Tong T.; RT "Nucleolar protein CSIG is required for p33ING1 function in UV-induced RT apoptosis."; RL Cell Death Dis. 3:E283-E283(2012). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-278, AND IDENTIFICATION BY MASS RP 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 [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 345-404 IN COMPLEX WITH H3K4ME3 RP AND ZINC, AND MUTAGENESIS OF TRP-378. RX PubMed=18533182; DOI=10.1016/j.jmb.2008.04.061; RA Pena P.V., Hom R.A., Hung T., Lin H., Kuo A.J., Wong R.P., Subach O.M., RA Champagne K.S., Zhao R., Verkhusha V.V., Li G., Gozani O., RA Kutateladze T.G.; RT "Histone H3K4me3 binding is required for the DNA repair and apoptotic RT activities of ING1 tumor suppressor."; RL J. Mol. Biol. 380:303-312(2008). CC -!- FUNCTION: Cooperates with p53/TP53 in the negative regulatory pathway CC of cell growth by modulating p53-dependent transcriptional activation. CC Implicated as a tumor suppressor gene. {ECO:0000269|PubMed:9440695}. CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2. CC Interacts with TP53. Isoform 2 interacts with RSL1D1. CC {ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:18533182, CC ECO:0000269|PubMed:22419112, ECO:0000269|PubMed:9440695}. CC -!- INTERACTION: CC Q9UK53; P15559: NQO1; NbExp=3; IntAct=EBI-399198, EBI-3989435; CC Q9UK53-2; Q96A65-2: EXOC4; NbExp=3; IntAct=EBI-8068204, EBI-17869840; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=p47ING1a, ING1-ALT2; CC IsoId=Q9UK53-1; Sequence=Displayed; CC Name=2; Synonyms=p33ING1b, Variant A; CC IsoId=Q9UK53-2; Sequence=VSP_009126; CC Name=3; Synonyms=p24ING1c, ING1-ALT1, Variant B; CC IsoId=Q9UK53-3; Sequence=VSP_009129; CC Name=4; Synonyms=Variant C; CC IsoId=Q9UK53-4; Sequence=VSP_009127; CC Name=5; CC IsoId=Q9UK53-5; Sequence=VSP_009128; CC -!- TISSUE SPECIFICITY: Isoform 2 was expressed in all normal tissues and CC cells examined, as well as in all breast cancer and melanoma cell lines CC examined. Isoform 3 was expressed in testis, liver, and kidney, weakly CC expressed in colon and brain and not expressed in breast and cultured CC melanocytes. Isoform 4 was highly expressed in testis and weakly CC expressed in brain, but not expressed in breast, colon, kidney, CC melanocytes, breast cancer or melanoma cell lines. CC {ECO:0000269|PubMed:10626813}. 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:0000250|UniProtKB:Q9H160}. 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:10866301}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB60879.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG02579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF181849; AAF07920.1; -; mRNA. DR EMBL; AF181850; AAF07921.1; -; mRNA. DR EMBL; AF001954; AAB60879.1; ALT_FRAME; mRNA. DR EMBL; AF044076; AAC00501.1; -; mRNA. DR EMBL; AF149721; AAF37421.1; -; mRNA. DR EMBL; AF149722; AAF37422.1; -; mRNA. DR EMBL; AF149723; AAF37423.1; -; mRNA. DR EMBL; AF167551; AAG02578.1; -; Genomic_DNA. DR EMBL; AF167550; AAG02578.1; JOINED; Genomic_DNA. DR EMBL; AF167551; AAG02579.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF167549; AAG02579.1; JOINED; Genomic_DNA. DR EMBL; AB037387; BAB08101.1; -; Genomic_DNA. DR EMBL; AB037387; BAB08102.1; -; Genomic_DNA. DR EMBL; AB037387; BAB08103.1; -; Genomic_DNA. DR EMBL; AB037594; BAB20992.2; -; mRNA. DR EMBL; AB031269; BAA83496.1; -; mRNA. DR EMBL; AB024401; BAA82886.1; -; mRNA. DR EMBL; AB024402; BAA82887.1; -; mRNA. DR EMBL; AB024403; BAA82888.1; -; Genomic_DNA. DR EMBL; AB024404; BAA82889.1; -; Genomic_DNA. DR EMBL; AB024404; BAA83462.1; -; Genomic_DNA. DR EMBL; AB024405; BAA82890.1; -; Genomic_DNA. DR EMBL; AJ310392; CAC38067.1; -; mRNA. DR EMBL; AF078835; AAG12174.1; -; mRNA. DR EMBL; AF078837; AAG12175.1; -; Genomic_DNA. DR EMBL; AF078836; AAG12175.1; JOINED; Genomic_DNA. DR EMBL; AK302353; BAG63679.1; -; mRNA. DR EMBL; AL157820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471085; EAX09127.1; -; Genomic_DNA. DR EMBL; CH471085; EAX09130.1; -; Genomic_DNA. DR EMBL; BC093942; AAH93942.1; -; mRNA. DR EMBL; BC093944; AAH93944.1; -; mRNA. DR CCDS; CCDS9515.1; -. [Q9UK53-4] DR CCDS; CCDS9516.1; -. [Q9UK53-2] DR CCDS; CCDS9517.1; -. [Q9UK53-1] DR CCDS; CCDS9518.1; -. [Q9UK53-3] DR RefSeq; NP_001254657.1; NM_001267728.1. [Q9UK53-5] DR RefSeq; NP_005528.4; NM_005537.5. DR RefSeq; NP_937860.1; NM_198217.2. [Q9UK53-4] DR RefSeq; NP_937861.1; NM_198218.2. [Q9UK53-3] DR RefSeq; NP_937862.1; NM_198219.2. [Q9UK53-2] DR PDB; 2QIC; X-ray; 2.10 A; A=345-404. DR PDBsum; 2QIC; -. DR AlphaFoldDB; Q9UK53; -. DR SMR; Q9UK53; -. DR BioGRID; 109833; 108. 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; Q9UK53; -. DR DIP; DIP-24256N; -. DR DIP; DIP-24257N; -. DR DIP; DIP-24258N; -. DR IntAct; Q9UK53; 37. DR MINT; Q9UK53; -. DR STRING; 9606.ENSP00000364929; -. DR GlyGen; Q9UK53; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UK53; -. DR PhosphoSitePlus; Q9UK53; -. DR BioMuta; ING1; -. DR DMDM; 212276438; -. DR EPD; Q9UK53; -. DR jPOST; Q9UK53; -. DR MassIVE; Q9UK53; -. DR MaxQB; Q9UK53; -. DR PaxDb; 9606-ENSP00000364929; -. DR PeptideAtlas; Q9UK53; -. DR ProteomicsDB; 84718; -. [Q9UK53-1] DR ProteomicsDB; 84719; -. [Q9UK53-2] DR ProteomicsDB; 84720; -. [Q9UK53-3] DR ProteomicsDB; 84721; -. [Q9UK53-4] DR ProteomicsDB; 84722; -. [Q9UK53-5] DR Pumba; Q9UK53; -. DR Antibodypedia; 4248; 558 antibodies from 38 providers. DR DNASU; 3621; -. DR Ensembl; ENST00000333219.9; ENSP00000328436.8; ENSG00000153487.13. [Q9UK53-2] DR Ensembl; ENST00000338450.7; ENSP00000345202.7; ENSG00000153487.13. [Q9UK53-4] DR Ensembl; ENST00000375775.4; ENSP00000364930.3; ENSG00000153487.13. [Q9UK53-3] DR GeneID; 3621; -. DR KEGG; hsa:3621; -. DR MANE-Select; ENST00000333219.9; ENSP00000328436.8; NM_198219.3; NP_937862.1. [Q9UK53-2] DR UCSC; uc001vrf.5; human. [Q9UK53-1] DR AGR; HGNC:6062; -. DR CTD; 3621; -. DR DisGeNET; 3621; -. DR GeneCards; ING1; -. DR HGNC; HGNC:6062; ING1. DR HPA; ENSG00000153487; Low tissue specificity. DR MalaCards; ING1; -. DR MIM; 275355; phenotype. DR MIM; 601566; gene. DR neXtProt; NX_Q9UK53; -. DR OpenTargets; ENSG00000153487; -. DR Orphanet; 500481; Squamous cell carcinoma of salivary glands. DR Orphanet; 494547; Squamous cell carcinoma of the hypopharynx. DR Orphanet; 494550; Squamous cell carcinoma of the larynx. DR Orphanet; 502366; Squamous cell carcinoma of the lip. DR Orphanet; 500464; Squamous cell carcinoma of the nasal cavity and paranasal sinuses. DR Orphanet; 502363; Squamous cell carcinoma of the oral cavity. DR Orphanet; 500478; Squamous cell carcinoma of the oropharynx. DR PharmGKB; PA29872; -. DR VEuPathDB; HostDB:ENSG00000153487; -. DR eggNOG; KOG1973; Eukaryota. DR GeneTree; ENSGT00940000155401; -. DR HOGENOM; CLU_031900_5_1_1; -. DR InParanoid; Q9UK53; -. DR OMA; MREQGNQ; -. DR OrthoDB; 3140066at2759; -. DR PhylomeDB; Q9UK53; -. DR TreeFam; TF352014; -. DR PathwayCommons; Q9UK53; -. DR SignaLink; Q9UK53; -. DR SIGNOR; Q9UK53; -. DR BioGRID-ORCS; 3621; 19 hits in 1176 CRISPR screens. DR ChiTaRS; ING1; human. DR EvolutionaryTrace; Q9UK53; -. DR GeneWiki; ING1; -. DR GenomeRNAi; 3621; -. DR Pharos; Q9UK53; Tbio. DR PRO; PR:Q9UK53; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9UK53; Protein. DR Bgee; ENSG00000153487; Expressed in stromal cell of endometrium and 172 other cell types or tissues. DR ExpressionAtlas; Q9UK53; baseline and differential. DR GO; GO:0005634; C:nucleus; 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:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; NAS:ComplexPortal. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl. DR GO; GO:0043067; P:regulation of programmed cell death; IEA:Ensembl. DR CDD; cd16860; ING_ING1; 1. DR CDD; cd15584; PHD_ING1_2; 1. DR Gene3D; 6.10.140.1740; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR028643; ING1_PHD_Znf. 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; INHIBITOR OF GROWTH PROTEIN; 1. DR PANTHER; PTHR10333:SF85; INHIBITOR OF GROWTH PROTEIN 1; 1. DR Pfam; PF12998; ING; 1. DR SMART; SM01408; ING; 1. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9UK53; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Disease variant; KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; KW Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..422 FT /note="Inhibitor of growth protein 1" FT /id="PRO_0000212661" FT ZN_FING 353..402 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 261..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 405..422 FT /note="PBR" FT /evidence="ECO:0000250|UniProtKB:Q9H160" FT COMPBIAS 280..322 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 356 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 369 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 374 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 380 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 383 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 396 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT BINDING 399 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT SITE 355 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT SITE 366 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT SITE 370 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT SITE 378 FT /note="Histone H3K4me3 binding" FT /evidence="ECO:0000269|PubMed:18533182, FT ECO:0007744|PDB:2QIC" FT CROSSLNK 278 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..212 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10626813, FT ECO:0000303|PubMed:10807544" FT /id="VSP_009129" FT VAR_SEQ 1..189 FT /note="MSFVECPYHSPAERLVAEADEGGPSAITGMGLCFRCLLFSFSGRSGVEGGRV FT DLNVFGSLGLQPWIGSSRCWGGPCSSALRCGWFSSWPPPSKSAIPIGGGSRGAGRVSRW FT PPPHWLEAWRVSPLPLSPLSPATFGRGFIAVAVIPGLWARGRGCSSDRLPRPAGPARRQ FT FQAASLLTRGWGRAWPWKQ -> MLSPANGEQLHLVNYVEDYLDSIESLPFDLQRNVSL FT MREIDAKYQE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10626813, FT ECO:0000303|PubMed:10807544, ECO:0000303|PubMed:11481424, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8944021" FT /id="VSP_009126" FT VAR_SEQ 1..189 FT /note="MSFVECPYHSPAERLVAEADEGGPSAITGMGLCFRCLLFSFSGRSGVEGGRV FT DLNVFGSLGLQPWIGSSRCWGGPCSSALRCGWFSSWPPPSKSAIPIGGGSRGAGRVSRW FT PPPHWLEAWRVSPLPLSPLSPATFGRGFIAVAVIPGLWARGRGCSSDRLPRPAGPARRQ FT FQAASLLTRGWGRAWPWKQ -> ME (in isoform 4)" FT /evidence="ECO:0000303|PubMed:10626813, FT ECO:0000303|PubMed:14702039" FT /id="VSP_009127" FT VAR_SEQ 1..189 FT /note="MSFVECPYHSPAERLVAEADEGGPSAITGMGLCFRCLLFSFSGRSGVEGGRV FT DLNVFGSLGLQPWIGSSRCWGGPCSSALRCGWFSSWPPPSKSAIPIGGGSRGAGRVSRW FT PPPHWLEAWRVSPLPLSPLSPATFGRGFIAVAVIPGLWARGRGCSSDRLPRPAGPARRQ FT FQAASLLTRGWGRAWPWKQ -> MSFVECPYHSPAERLVAEADEGGPSAITE (in FT isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_009128" FT VARIANT 125 FT /note="L -> R (in dbSNP:rs7338333)" FT /evidence="ECO:0000269|PubMed:10807544, FT ECO:0000269|PubMed:10866301, ECO:0000269|PubMed:8944021" FT /id="VAR_047097" FT VARIANT 335 FT /note="A -> D (in HNSCC)" FT /evidence="ECO:0000269|PubMed:10866301" FT /id="VAR_017420" FT VARIANT 358 FT /note="C -> S (in HNSCC)" FT /evidence="ECO:0000269|PubMed:10866301" FT /id="VAR_017421" FT VARIANT 359 FT /note="N -> S (in HNSCC)" FT /evidence="ECO:0000269|PubMed:10866301" FT /id="VAR_017422" FT MUTAGEN 378 FT /note="W->A: Unable to stimulate DNA repair after UV FT irradiation or promote DNA-damage-induced apoptosis." FT /evidence="ECO:0000269|PubMed:18533182" FT CONFLICT 266 FT /note="A -> V (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="A -> V (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="K -> N (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT CONFLICT 280 FT /note="E -> D (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="A -> V (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT CONFLICT 285 FT /note="A -> S (in Ref. 1; AAC00501/AAB60879, 3 and 6)" FT /evidence="ECO:0000305" FT TURN 356..359 FT /evidence="ECO:0007829|PDB:2QIC" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:2QIC" FT STRAND 378..380 FT /evidence="ECO:0007829|PDB:2QIC" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:2QIC" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:2QIC" SQ SEQUENCE 422 AA; 46738 MW; 03D6AEEAA6E39090 CRC64; MSFVECPYHS PAERLVAEAD EGGPSAITGM GLCFRCLLFS FSGRSGVEGG RVDLNVFGSL GLQPWIGSSR CWGGPCSSAL RCGWFSSWPP PSKSAIPIGG GSRGAGRVSR WPPPHWLEAW RVSPLPLSPL SPATFGRGFI AVAVIPGLWA RGRGCSSDRL PRPAGPARRQ FQAASLLTRG WGRAWPWKQI LKELDECYER FSRETDGAQK RRMLHCVQRA LIRSQELGDE KIQIVSQMVE LVENRTRQVD SHVELFEAQQ ELGDTAGNSG KAGADRPKGE AAAQADKPNS KRSRRQRNNE NRENASSNHD HDDGASGTPK EKKAKTSKKK KRSKAKAERE ASPADLPIDP NEPTYCLCNQ VSYGEMIGCD NDECPIEWFH FSCVGLNHKP KGKWYCPKCR GENEKTMDKA LEKSKKERAY NR //