ING1_DICDI
ID ING1_DICDI Reviewed; 324 AA.
AC Q54PN9; Q5H7A8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Inhibitor of growth protein 1 homolog {ECO:0000305};
GN Name=dng1 {ECO:0000303|PubMed:16003496};
GN ORFNames=DDB_G0284411 {ECO:0000312|dictyBase:DDB_G0284411};
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=16003496; DOI=10.1007/s00018-005-4570-0;
RA Mayanagi T., Amagai A., Maeda Y.;
RT "DNG1, a Dictyostelium homologue of tumor suppressor ING1 regulates
RT differentiation of Dictyostelium cells.";
RL Cell. Mol. Life Sci. 62:1734-1743(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in regulation of the growth and differentiation
CC transition (GDT) process, probably by regulating gene expression via
CC histone modification. {ECO:0000269|PubMed:16003496}.
CC -!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000255|RuleBase:RU361213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU361213,
CC ECO:0000269|PubMed:16003496}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed at low level throughout
CC development (at protein level). {ECO:0000269|PubMed:16003496}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000255|RuleBase:RU361213}.
CC -!- DISRUPTION PHENOTYPE: Cells provided with nutrients proliferate slower
CC than normal. Upon starvation, the progression of differentiation is
CC delayed in a cell density-dependent manner. Cells form tiny aggregates
CC and more aggregation centers compared to wild-type cells, resulting in
CC a higher number of tiny migrating slugs. Cells form complete tiny
CC fruiting bodies 3-4 h faster than wild-type. In a similar manner to
CC wild-type, most cells remain as non-aggregated single cells in the
CC presence of caffeine, which is an inhibitor of adenylate cyclase
CC activation. Decreased expression of cyclic AMP receptor carA gene and
CC of csaA, a contact site A gene, both of which are expressed early in
CC development. Cells exhibit a disordered change of histone H2B
CC modification compared to wild-type, in which the modification level of
CC histone H2B appears to increase in response to cell differentiation.
CC Adequate histone H1 and H3 modifications are also impaired. Normal
CC uniform distribution of starved cells in aggregation streams, but
CC abnormal distribution of cells in subsequent multicellular structures.
CC {ECO:0000269|PubMed:16003496}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000255|RuleBase:RU361213,
CC ECO:0000305}.
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DR EMBL; AB194261; BAD89149.1; -; mRNA.
DR EMBL; AAFI01000106; EAL65254.1; -; Genomic_DNA.
DR RefSeq; XP_638615.1; XM_633523.1.
DR AlphaFoldDB; Q54PN9; -.
DR SMR; Q54PN9; -.
DR STRING; 44689.DDB0220706; -.
DR PaxDb; Q54PN9; -.
DR GeneID; 8624586; -.
DR KEGG; ddi:DDB_G0284411; -.
DR dictyBase; DDB_G0284411; dng1.
DR eggNOG; KOG1973; Eukaryota.
DR HOGENOM; CLU_031900_5_1_1; -.
DR InParanoid; Q54PN9; -.
DR OMA; QPKGKWF; -.
DR PhylomeDB; Q54PN9; -.
DR Reactome; R-DDI-3214847; HATs acetylate histones.
DR Reactome; R-DDI-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DDI-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DDI-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:Q54PN9; -.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0032991; C:protein-containing complex; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016570; P:histone modification; IMP:dictyBase.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:dictyBase.
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; 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 Chromatin regulator; Growth regulation; Metal-binding; Nucleus;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..324
FT /note="Inhibitor of growth protein 1 homolog"
FT /id="PRO_0000445438"
FT ZN_FING 271..320
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 120..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 273
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 284
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 288
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT SITE 296
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UK53"
FT CONFLICT 130..131
FT /note="Missing (in Ref. 1; BAD89149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34963 MW; 81E3A7DD42676698 CRC64;
MYQGKGTYLE NYLDSISTLP SELGRNFALI RELDYRTSDL VEKIEKLKSN LLVTTNGTRR
AVHELTDERA SKHIKLEMKQ VIEYSDEKVE LSNQTYELID KHIRKLDIDL KKFETELESA
EEEKKKKKSK QSQNNSTVES STTSSSSSSS SSSLSLSSST NNTSSLNSSS GGGGGGSGGG
GGGGGHSSHS TGNKKGKARD SLTSSSSSGN INGMSSSSSS SSSSSSLSSR KQKSMAAQDI
ASITGNNGDA DVRVFNANPN DLDLAIDPNE PTYCFCNRVS FGEMVGCENP DCKIEWFHFE
CVGLTSTPKG KWYCPDCTRI KVKK
