ING3_MOUSE
ID ING3_MOUSE Reviewed; 421 AA.
AC Q8VEK6; Q99JS6; Q9ERB2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Inhibitor of growth protein 3;
DE AltName: Full=p47ING3;
GN Name=Ing3;
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 [MRNA].
RA Zenklusen J.C., Green E.D.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-181 AND LYS-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase (HAT) complex
CC which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A. This
CC modification may both alter nucleosome - DNA interactions and promote
CC interaction of the modified histones with other proteins which
CC positively regulate transcription. This complex may be required for the
CC activation of transcriptional programs associated with oncogene and
CC proto-oncogene mediated growth induction, tumor suppressor mediated
CC growth arrest and replicative senescence, apoptosis, and DNA repair.
CC NuA4 may also play a direct role in DNA repair when directly recruited
CC to sites of DNA damage. Component of a SWR1-like complex that
CC specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC nucleosome (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2 (By
CC similarity). Component of the NuA4 histone acetyltransferase complex
CC which contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC.
CC HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex
CC termed Piccolo NuA4. Component of a SWR1-like complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH18342.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY007791; AAG23286.1; ALT_INIT; mRNA.
DR EMBL; AK080787; BAC38021.1; ALT_INIT; mRNA.
DR EMBL; BC005721; AAH05721.1; -; mRNA.
DR EMBL; BC018342; AAH18342.1; ALT_INIT; mRNA.
DR CCDS; CCDS39434.1; -.
DR RefSeq; NP_001297990.1; NM_001311061.1.
DR RefSeq; NP_076115.3; NM_023626.4.
DR AlphaFoldDB; Q8VEK6; -.
DR SMR; Q8VEK6; -.
DR BioGRID; 214920; 3.
DR ComplexPortal; CPX-747; Piccolo NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR IntAct; Q8VEK6; 4.
DR MINT; Q8VEK6; -.
DR STRING; 10090.ENSMUSP00000031680; -.
DR iPTMnet; Q8VEK6; -.
DR PhosphoSitePlus; Q8VEK6; -.
DR EPD; Q8VEK6; -.
DR MaxQB; Q8VEK6; -.
DR PaxDb; Q8VEK6; -.
DR PRIDE; Q8VEK6; -.
DR ProteomicsDB; 267337; -.
DR Antibodypedia; 31689; 248 antibodies from 32 providers.
DR DNASU; 71777; -.
DR Ensembl; ENSMUST00000031680; ENSMUSP00000031680; ENSMUSG00000029670.
DR GeneID; 71777; -.
DR KEGG; mmu:71777; -.
DR UCSC; uc009bat.1; mouse.
DR CTD; 54556; -.
DR MGI; MGI:1919027; Ing3.
DR VEuPathDB; HostDB:ENSMUSG00000029670; -.
DR eggNOG; KOG1973; Eukaryota.
DR GeneTree; ENSGT00940000156619; -.
DR InParanoid; Q8VEK6; -.
DR OMA; YEWFHWK; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q8VEK6; -.
DR TreeFam; TF106497; -.
DR BioGRID-ORCS; 71777; 19 hits in 77 CRISPR screens.
DR PRO; PR:Q8VEK6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VEK6; protein.
DR Bgee; ENSMUSG00000029670; Expressed in animal zygote and 256 other tissues.
DR ExpressionAtlas; Q8VEK6; baseline and differential.
DR Genevisible; Q8VEK6; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; ISO:MGI.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:1902275; P:regulation of chromatin organization; IC:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd15585; PHD_ING3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038004; ING3.
DR InterPro; IPR042020; ING3_PHD.
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:SF99; PTHR10333:SF99; 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 Acetylation; Chromatin regulator; Growth regulation; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..421
FT /note="Inhibitor of growth protein 3"
FT /id="PRO_0000212666"
FT ZN_FING 363..412
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 129..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 365
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 376
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 380
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 388
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR8"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR8"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR8"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NXR8"
FT CONFLICT 257
FT /note="N -> T (in Ref. 1; AAG23286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 46847 MW; E786062A26E3BF96 CRC64;
MLYLEDYLEM IEQLPMDLRD RFTEMREMDL QVQNAMDQLE QRVSEFFMNA KKNKPEWREE
QMASIKKDYY KALEDADEKV QLANQIYDLV DRHLRKLDQE LAKFKMELEA DNAGITEILE
RRSLELDAPS QPVNNHHAHS HTPVEKRKYN PTSHHAAADH IPEKKFKSEA LLSTLTSDAS
KENTLGCRNN NSTASCNNAY NVNSSQPLAS YNIGSLSSGA GAGAITMAAA QAVQATAQMK
EGRRTSSLKA SYEAFKNNDF QLGKEFSIPR ETAGYSSSSA LMTTLTQNAS SSATDSRSGR
KSKNNTKSSS QQSSSSSSSS SSSSLSLCSS SSTVVQEVSQ QATVVPESDS NSQVDWTYDP
NEPRYCICNQ VSYGEMVGCD NQDCPIEWFH YGCVGLTEAP KGKWFCPQCT AAMKRRGSRH
K
