ING1_HUMAN
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 03-AUG-2022, entry version 181.
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};
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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; 104.
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; Q9UK53; -.
DR PeptideAtlas; Q9UK53; -.
DR PRIDE; 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 Antibodypedia; 4248; 522 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; ENST00000375775.3; 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 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; KMQIVNH; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9UK53; -.
DR TreeFam; TF352014; -.
DR PathwayCommons; Q9UK53; -.
DR SignaLink; Q9UK53; -.
DR SIGNOR; Q9UK53; -.
DR BioGRID-ORCS; 3621; 18 hits in 1095 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 170 other tissues.
DR ExpressionAtlas; Q9UK53; baseline and differential.
DR Genevisible; Q9UK53; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
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; IC: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; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0010941; P:regulation of cell death; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR028643; ING1.
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:SF85; PTHR10333:SF85; 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; 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
