ID A5WVS7_DANRE Unreviewed; 242 AA.
AC A5WVS7; A0A0H2UKX2;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Inhibitor of growth protein {ECO:0000256|RuleBase:RU361213};
GN Name=ing5a {ECO:0000313|Ensembl:ENSDARP00000040700,
GN ECO:0000313|RefSeq:NP_001093519.1,
GN ECO:0000313|ZFIN:ZDB-GENE-031016-1};
GN Synonyms=LOC792168 {ECO:0000313|EMBL:AAI62372.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI62372.1};
RN [1] {ECO:0000313|RefSeq:NP_001093519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15356280;
RA He G.H., Helbing C.C., Wagner M.J., Sensen C.W., Riabowol K.;
RT "Phylogenetic analysis of the ING family of PHD finger proteins.";
RL Mol. Biol. Evol. 22:104-116(2005).
RN [2] {ECO:0000313|EMBL:AAI62372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001093519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24240475;
RA Huang H.T., Kathrein K.L., Barton A., Gitlin Z., Huang Y.H., Ward T.P.,
RA Hofmann O., Dibiase A., Song A., Tyekucheva S., Hide W., Zhou Y., Zon L.I.;
RT "A network of epigenetic regulators guides developmental haematopoiesis in
RT vivo.";
RL Nat. Cell Biol. 15:1516-1525(2013).
RN [4] {ECO:0000313|Ensembl:ENSDARP00000040700, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000040700};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000040700}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000040700};
RG Ensembl;
RL Submitted (AUG-2013) to UniProtKB.
RN [6] {ECO:0000313|RefSeq:NP_001093519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24732281;
RA Garcia de la Serrana D., Mareco E.A., Johnston I.A.;
RT "Systematic variation in the pattern of gene paralog retention between the
RT teleost superorders Ostariophysi and Acanthopterygii.";
RL Genome Biol. Evol. 6:981-987(2014).
RN [7] {ECO:0000313|RefSeq:NP_001093519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [8] {ECO:0000313|RefSeq:NP_001093519.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [9] {ECO:0000313|RefSeq:NP_001093519.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of an histone acetyltransferase complex.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SUBUNIT: Component of an histone acetyltransferase complex. Interacts
CC with H3K4me3 and to a lesser extent with H3K4me2.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU361213}.
CC -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC {ECO:0000256|RuleBase:RU361213}.
CC -!- SIMILARITY: Belongs to the ING family. {ECO:0000256|ARBA:ARBA00010210,
CC ECO:0000256|RuleBase:RU361213}.
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DR EMBL; CABZ01006771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01006772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01006773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01006774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01078511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01078514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT027565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO704722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO017843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; LO018478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC162372; AAI62372.1; -; mRNA.
DR EMBL; BC162642; AAI62642.1; -; mRNA.
DR RefSeq; NP_001093519.1; NM_001100049.2.
DR STRING; 7955.ENSDARP00000040700; -.
DR PaxDb; 7955-ENSDARP00000040700; -.
DR Ensembl; ENSDART00000040701.8; ENSDARP00000040700.6; ENSDARG00000022413.9.
DR Ensembl; ENSDART00000157620.2; ENSDARP00000141310.1; ENSDARG00000022413.9.
DR GeneID; 792168; -.
DR KEGG; dre:792168; -.
DR AGR; ZFIN:ZDB-GENE-031016-1; -.
DR CTD; 792168; -.
DR ZFIN; ZDB-GENE-031016-1; ing5a.
DR eggNOG; KOG1973; Eukaryota.
DR HOGENOM; CLU_031900_5_1_1; -.
DR OMA; QPKGKWF; -.
DR OrthoDB; 3140066at2759; -.
DR TreeFam; TF352014; -.
DR Reactome; R-DRE-3214847; HATs acetylate histones.
DR Reactome; R-DRE-6804758; Regulation of TP53 Activity through Acetylation.
DR Proteomes; UP000000437; Chromosome 22.
DR Bgee; ENSDARG00000022413; Expressed in spleen and 20 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd16863; ING_ING5; 1.
DR CDD; cd15685; PHD_ING5; 1.
DR Gene3D; 6.10.140.1740; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; INHIBITOR OF GROWTH PROTEIN; 1.
DR PANTHER; PTHR10333:SF41; INHIBITOR OF GROWTH PROTEIN 5; 1.
DR Pfam; PF12998; ING; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|RuleBase:RU361213};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR628651-51};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361213};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR628651-51};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 189..238
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 118..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..117
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-51"
FT SITE 191
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 202
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 206
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
FT SITE 214
FT /note="Histone H3K4me3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR628651-50"
SQ SEQUENCE 242 AA; 28281 MW; A8CD5E2B5A1610D9 CRC64;
MATAIYLEHY LDSIENLPCE LQRNFTLMRE LDNRAEEKKC EIDKLAEEYI ANVRNLAPDQ
RVEHLQKIQN GFSKCKEYSD DKVQLAMQTY EMVDKHIRRL DADLARFENE LKEKLDVSGY
ESPDNRTHKK VTGRGNLKEK RRPKGRGRKS SDDESPRKKK MKNSPEFPES ILPVHPSDVL
DMPVDPNEPT YCLCHQVSYG EMIGCDNPDC PIEWFHFACV DLTTKPKGKW FCPRCTQDRK
KK
//
