ING1_ARATH
ID ING1_ARATH Reviewed; 234 AA.
AC Q9LIQ6; Q84WD2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=PHD finger protein ING1;
DE AltName: Full=Protein INHIBITOR OF GROWTH 1;
DE Short=Protein AtING1;
GN Name=ING1; OrderedLocusNames=At3g24010; ORFNames=F14O13.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-234.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP GENE FAMILY, DOMAIN PHD-TYPE ZINC-FINGER, SUBCELLULAR LOCATION, INTERACTION
RP WITH HISTONES H3K4ME3 AND H3K4ME2, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP MET-191; ASP-195 AND TRP-203.
RX PubMed=19154204; DOI=10.1111/j.1365-313x.2009.03795.x;
RA Lee W.Y., Lee D., Chung W.I., Kwon C.S.;
RT "Arabidopsis ING and Alfin1-like protein families localize to the nucleus
RT and bind to H3K4me3/2 via plant homeodomain fingers.";
RL Plant J. 58:511-524(2009).
CC -!- FUNCTION: Histone-binding component that specifically recognizes H3
CC tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription
CC start sites of virtually all active genes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000269|PubMed:19154204}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19154204}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:19154204}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000269|PubMed:19154204}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
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DR EMBL; AP001297; BAB03019.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76844.1; -; Genomic_DNA.
DR EMBL; BT024927; ABD94083.1; -; mRNA.
DR EMBL; AB493630; BAH30468.1; -; mRNA.
DR EMBL; AY088805; AAM67115.1; -; mRNA.
DR EMBL; BT003957; AAO42002.1; -; mRNA.
DR RefSeq; NP_566742.1; NM_113306.4.
DR AlphaFoldDB; Q9LIQ6; -.
DR SMR; Q9LIQ6; -.
DR BioGRID; 7318; 3.
DR IntAct; Q9LIQ6; 3.
DR STRING; 3702.AT3G24010.1; -.
DR PaxDb; Q9LIQ6; -.
DR PRIDE; Q9LIQ6; -.
DR ProteomicsDB; 228866; -.
DR EnsemblPlants; AT3G24010.1; AT3G24010.1; AT3G24010.
DR GeneID; 821986; -.
DR Gramene; AT3G24010.1; AT3G24010.1; AT3G24010.
DR KEGG; ath:AT3G24010; -.
DR Araport; AT3G24010; -.
DR TAIR; locus:2076141; AT3G24010.
DR eggNOG; KOG1973; Eukaryota.
DR HOGENOM; CLU_031900_4_0_1; -.
DR InParanoid; Q9LIQ6; -.
DR OMA; QPKGKWF; -.
DR OrthoDB; 1434088at2759; -.
DR PhylomeDB; Q9LIQ6; -.
DR PRO; PR:Q9LIQ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIQ6; baseline and differential.
DR Genevisible; Q9LIQ6; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 1.
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; 2.
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 Chromatin regulator; Growth regulation; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..234
FT /note="PHD finger protein ING1"
FT /id="PRO_0000412979"
FT ZN_FING 178..227
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 129..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 180
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 191
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:19154204"
FT SITE 195
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:19154204"
FT SITE 203
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 191
FT /note="M->A: Abolishes binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 195
FT /note="D->A: Abolishes binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 195
FT /note="D->E: Does not affect binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT MUTAGEN 203
FT /note="W->A: Abolishes binding to H3K4me2/3."
FT /evidence="ECO:0000269|PubMed:19154204"
FT CONFLICT 111
FT /note="D -> G (in Ref. 6; AAO42002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26098 MW; B24DADAA6FE12549 CRC64;
MSFAEEFEAN LVSLAHVLQK KYALLRDLDK SLQENQRQNE QRCEKEIEDI RRGRAGNITP
NTSLTKFSEE ALDEQKHSVR IADEKVTLAM QAYDLVDMHV QQLDQYMKKS DEVIRKEKEA
AAATLELENN GKAGNAGEGG RGGRKKTRLA TAASTAAAST GMTSSNMDLD LPVDPNEPTY
CICNQVSFGE MVACDNNACK IEWFHFGCVG LKEQPKGKWY CPECATVKKS RKGR
