ING5_MOUSE
ID ING5_MOUSE Reviewed; 240 AA.
AC Q9D8Y8; Q3UL57; Q6P292; Q9CV64; Q9D9V8;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Inhibitor of growth protein 5;
GN Name=Ing5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Component of the MOZ/MORF complex which has
CC a histone H3 acetyltransferase activity. Through chromatin acetylation
CC it may regulate DNA replication and may function as a transcriptional
CC coactivator. Inhibits cell growth, induces a delay in S-phase
CC progression and enhances Fas-induced apoptosis in an INCA1-dependent
CC manner. {ECO:0000250|UniProtKB:Q8WYH8}.
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. Component of the MOZ/MORF
CC complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of
CC BRPF1, BRD1/BRPF2 and BRPF3. Interacts with H3K4me3 and to a lesser
CC extent with H3K4me2. Interacts with EP300 and p53/TP53. Interacts with
CC INCA1. {ECO:0000250|UniProtKB:Q8WYH8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WYH8}.
CC Chromosome {ECO:0000250|UniProtKB:Q8WYH8}. Note=Localizes to
CC transcription start sites. {ECO:0000250|UniProtKB:Q8WYH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D8Y8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8Y8-2; Sequence=VSP_012529;
CC Name=3;
CC IsoId=Q9D8Y8-3; Sequence=VSP_012530;
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250|UniProtKB:Q8WYH8}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ING family. {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; AK006421; BAB24580.1; -; mRNA.
DR EMBL; AK007536; BAB25095.1; -; mRNA.
DR EMBL; AK009312; BAB26210.1; -; mRNA.
DR EMBL; AK028010; BAC25697.1; -; mRNA.
DR EMBL; AK145695; BAE26593.1; -; mRNA.
DR EMBL; BC064674; AAH64674.1; -; mRNA.
DR CCDS; CCDS35673.1; -. [Q9D8Y8-1]
DR RefSeq; NP_079730.1; NM_025454.2. [Q9D8Y8-1]
DR AlphaFoldDB; Q9D8Y8; -.
DR SMR; Q9D8Y8; -.
DR BioGRID; 211337; 4.
DR ComplexPortal; CPX-797; HBO1-5.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-798; HBO1-5.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-799; HBO1-5.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-800; MOZ1 histone acetyltransferase complex.
DR ComplexPortal; CPX-801; MOZ2 histone acetyltransferase complex.
DR ComplexPortal; CPX-802; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-803; MORF1 histone acetyltransferase complex.
DR ComplexPortal; CPX-804; MORF3 histone acetyltransferase complex.
DR ComplexPortal; CPX-805; MORF2 histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000027505; -.
DR iPTMnet; Q9D8Y8; -.
DR PhosphoSitePlus; Q9D8Y8; -.
DR EPD; Q9D8Y8; -.
DR jPOST; Q9D8Y8; -.
DR MaxQB; Q9D8Y8; -.
DR PaxDb; Q9D8Y8; -.
DR PeptideAtlas; Q9D8Y8; -.
DR PRIDE; Q9D8Y8; -.
DR ProteomicsDB; 269482; -. [Q9D8Y8-1]
DR ProteomicsDB; 269483; -. [Q9D8Y8-2]
DR ProteomicsDB; 269484; -. [Q9D8Y8-3]
DR Antibodypedia; 34573; 237 antibodies from 31 providers.
DR DNASU; 66262; -.
DR Ensembl; ENSMUST00000027505; ENSMUSP00000027505; ENSMUSG00000026283. [Q9D8Y8-1]
DR Ensembl; ENSMUST00000190476; ENSMUSP00000140498; ENSMUSG00000026283. [Q9D8Y8-2]
DR GeneID; 66262; -.
DR KEGG; mmu:66262; -.
DR UCSC; uc007cen.1; mouse. [Q9D8Y8-1]
DR CTD; 84289; -.
DR MGI; MGI:1922816; Ing5.
DR VEuPathDB; HostDB:ENSMUSG00000026283; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000158159; -.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q9D8Y8; -.
DR OMA; QPKGKWF; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9D8Y8; -.
DR TreeFam; TF352014; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 66262; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q9D8Y8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D8Y8; protein.
DR Bgee; ENSMUSG00000026283; Expressed in metanephric ureteric bud and 222 other tissues.
DR ExpressionAtlas; Q9D8Y8; baseline and differential.
DR Genevisible; Q9D8Y8; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0048144; P:fibroblast proliferation; IGI:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISO:MGI.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISO:MGI.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISO:MGI.
DR GO; GO:0016570; P:histone modification; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IGI:MGI.
DR GO; GO:0045926; P:negative regulation of growth; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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 Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..240
FT /note="Inhibitor of growth protein 5"
FT /id="PRO_0000212672"
FT ZN_FING 186..235
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 115..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..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:0000250|UniProtKB:Q8WYH8"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT SITE 188
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT SITE 199
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT SITE 203
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT SITE 211
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYH8"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012530"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012529"
SQ SEQUENCE 240 AA; 27799 MW; FE8A0BACC503E480 CRC64;
MATAMYLEHY LDSIENLPCE LQRNFQLMRE LDQRTEDKKA EIDILAAEYI STVKTLSSAQ
RVEHLQKIQS AYSKCKEYSD DKVQLAMQTY EMVDKHIRRL DADLARFEAD LKDRMDGSDF
ESTGARSLKK GRSQKEKRSS RGRGRRTSEE DTPKKKKHKS GSEFTDSILS VHPSDVLDMP
VDPNEPTYCL CHQVSYGEMI GCDNPDCPIE WFHFACVDLT TKPKGKWFCP RCVQEKRKKK
