ID ID4_HUMAN Reviewed; 161 AA.
AC P47928; Q13005;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 24-JAN-2024, entry version 192.
DE RecName: Full=DNA-binding protein inhibitor ID-4;
DE AltName: Full=Class B basic helix-loop-helix protein 27;
DE Short=bHLHb27;
DE AltName: Full=Inhibitor of DNA binding 4;
DE AltName: Full=Inhibitor of differentiation 4;
GN Name=ID4; Synonyms=BHLHB27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Abdominal adipose tissue;
RA Kiesling T.L., Christy B.A.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9872455; DOI=10.1093/dnares/5.5.309;
RA Rigolet M., Rich T., Gross-Morand M.S., Molina-Gomes D.,
RA Viegas-Pequignot E., Junien C.;
RT "cDNA cloning, tissue distribution and chromosomal localization of the
RT human ID4 gene.";
RL DNA Res. 5:309-313(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7665172; DOI=10.1006/geno.1995.1026;
RA Pagliuca A., Bartoli P.C., Saccone S., Della Valle G., Lania L.;
RT "Molecular cloning of ID4, a novel dominant negative helix-loop-helix human
RT gene on chromosome 6p21.3-p22.";
RL Genomics 27:200-203(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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).
CC -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC transcription factors by forming heterodimers and inhibiting their DNA
CC binding and transcriptional activity. Implicated in regulating a
CC variety of cellular processes, including cellular growth, senescence,
CC differentiation, apoptosis, angiogenesis, and neoplastic transformation
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with other HLH proteins.
CC -!- INTERACTION:
CC P47928; P16333: NCK1; NbExp=3; IntAct=EBI-1754719, EBI-389883;
CC P47928; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1754719, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/40916/ID4";
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DR EMBL; U28368; AAA73923.1; -; mRNA.
DR EMBL; Y07958; CAA69255.1; -; mRNA.
DR EMBL; U16153; AAA82882.1; -; mRNA.
DR EMBL; AL022726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014941; AAH14941.1; -; mRNA.
DR CCDS; CCDS4544.1; -.
DR PIR; G01855; G01855.
DR PIR; JE0306; JE0306.
DR RefSeq; NP_001537.1; NM_001546.3.
DR AlphaFoldDB; P47928; -.
DR SMR; P47928; -.
DR BioGRID; 109626; 19.
DR IntAct; P47928; 14.
DR MINT; P47928; -.
DR STRING; 9606.ENSP00000367972; -.
DR GlyGen; P47928; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P47928; -.
DR PhosphoSitePlus; P47928; -.
DR BioMuta; ID4; -.
DR DMDM; 1352422; -.
DR EPD; P47928; -.
DR MassIVE; P47928; -.
DR MaxQB; P47928; -.
DR PaxDb; 9606-ENSP00000367972; -.
DR PeptideAtlas; P47928; -.
DR ProteomicsDB; 55823; -.
DR Pumba; P47928; -.
DR Antibodypedia; 10414; 425 antibodies from 32 providers.
DR DNASU; 3400; -.
DR Ensembl; ENST00000378700.8; ENSP00000367972.3; ENSG00000172201.12.
DR GeneID; 3400; -.
DR KEGG; hsa:3400; -.
DR MANE-Select; ENST00000378700.8; ENSP00000367972.3; NM_001546.4; NP_001537.1.
DR UCSC; uc003ncw.5; human.
DR AGR; HGNC:5363; -.
DR CTD; 3400; -.
DR DisGeNET; 3400; -.
DR GeneCards; ID4; -.
DR HGNC; HGNC:5363; ID4.
DR HPA; ENSG00000172201; Tissue enhanced (thyroid).
DR MIM; 600581; gene.
DR neXtProt; NX_P47928; -.
DR OpenTargets; ENSG00000172201; -.
DR PharmGKB; PA29611; -.
DR VEuPathDB; HostDB:ENSG00000172201; -.
DR eggNOG; ENOG502S1WX; Eukaryota.
DR GeneTree; ENSGT00940000162435; -.
DR HOGENOM; CLU_116790_2_0_1; -.
DR InParanoid; P47928; -.
DR OMA; NIDHHQR; -.
DR OrthoDB; 4206554at2759; -.
DR PhylomeDB; P47928; -.
DR TreeFam; TF326217; -.
DR PathwayCommons; P47928; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P47928; -.
DR SIGNOR; P47928; -.
DR BioGRID-ORCS; 3400; 14 hits in 1169 CRISPR screens.
DR ChiTaRS; ID4; human.
DR GeneWiki; ID4; -.
DR GenomeRNAi; 3400; -.
DR Pharos; P47928; Tbio.
DR PRO; PR:P47928; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P47928; Protein.
DR Bgee; ENSG00000172201; Expressed in blood vessel layer and 197 other cell types or tissues.
DR Genevisible; P47928; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ARUK-UCL.
DR GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:GDB.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR GO; GO:0060741; P:prostate gland stromal morphogenesis; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0061682; P:seminal vesicle morphogenesis; IEA:Ensembl.
DR CDD; cd19694; bHLH_dnHLH_ID4; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR026052; DNA-bd_prot-inh.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR11723; DNA-BINDING PROTEIN INHIBITOR; 1.
DR PANTHER; PTHR11723:SF6; DNA-BINDING PROTEIN INHIBITOR ID-4; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..161
FT /note="DNA-binding protein inhibitor ID-4"
FT /id="PRO_0000127250"
FT DOMAIN 52..104
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 117..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 10..14
FT /note="SGRKA -> RPLR (in Ref. 3; AAA82882)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..40
FT /note="AA -> Q (in Ref. 3; AAA82882)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..79
FT /note="RLV -> WL (in Ref. 3; AAA82882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 16622 MW; 5B14847AE7337339 CRC64;
MKAVSPVRPS GRKAPSGCGG GELALRCLAE HGHSLGGSAA AAAAAAAARC KAAEAAADEP
ALCLQCDMND CYSRLRRLVP TIPPNKKVSK VEILQHVIDY ILDLQLALET HPALLRQPPP
PAPPHHPAGT CPAAPPRTPL TALNTDPAGA VNKQGDSILC R
//
