ID1_MOUSE
ID ID1_MOUSE Reviewed; 168 AA.
AC P20067; Q61101; Q9D897;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=DNA-binding protein inhibitor ID-1;
DE AltName: Full=Inhibitor of DNA binding 1;
DE AltName: Full=Inhibitor of differentiation 1;
GN Name=Id1; Synonyms=Id, Id-1, Idb1;
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] (ISOFORM SHORT).
RX PubMed=2156629; DOI=10.1016/0092-8674(90)90214-y;
RA Benezra R., Davis R.L., Lockshon D., Turner D.L., Weintraub H.;
RT "The protein Id: a negative regulator of helix-loop-helix DNA binding
RT proteins.";
RL Cell 61:49-59(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Swiss albino; TISSUE=Brain;
RX PubMed=8765747; DOI=10.1016/0167-4781(96)00092-9;
RA Hernandez M.-C., Andres-Barquin P.J., Israel M.A.;
RT "Molecular cloning of the cDNA encoding a helix-loop-helix protein, mouse
RT ID1B: tissue-specific expression of ID1A and ID1B genes.";
RL Biochim. Biophys. Acta 1308:28-30(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [4]
RP INTERACTION WITH IFI204.
RX PubMed=11940648; DOI=10.1128/mcb.22.9.2893-2905.2002;
RA Liu C.-J., Ding B., Wang H., Lengyel P.;
RT "The MyoD-inducible p204 protein overcomes the inhibition of myoblast
RT differentiation by Id proteins.";
RL Mol. Cell. Biol. 22:2893-2905(2002).
RN [5]
RP INTERACTION WITH COPS5.
RX PubMed=15451666; DOI=10.1016/j.jmb.2004.08.043;
RA Berse M., Bounpheng M., Huang X., Christy B., Pollmann C., Dubiel W.;
RT "Ubiquitin-dependent degradation of Id1 and Id3 is mediated by the COP9
RT signalosome.";
RL J. Mol. Biol. 343:361-370(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=16516211; DOI=10.1016/j.febslet.2006.02.038;
RA Makita J., Kurooka H., Mori K., Akagi Y., Yokota Y.;
RT "Identification of the nuclear export signal in the helix-loop-helix
RT inhibitor Id1.";
RL FEBS Lett. 580:1812-1816(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH GATA4 AND NKX2-5.
RX PubMed=16556596; DOI=10.1074/jbc.m511748200;
RA Ding B., Liu C.-J., Huang Y., Yu J., Kong W., Lengyel P.;
RT "p204 protein overcomes the inhibition of the differentiation of P19 murine
RT embryonal carcinoma cells to beating cardiac myocytes by Id proteins.";
RL J. Biol. Chem. 281:14893-14906(2006).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=19217292; DOI=10.1016/j.cub.2008.12.052;
RA Duffield G.E., Watson N.P., Mantani A., Peirson S.N., Robles-Murguia M.,
RA Loros J.J., Israel M.A., Dunlap J.C.;
RT "A role for Id2 in regulating photic entrainment of the mammalian circadian
RT system.";
RL Curr. Biol. 19:297-304(2009).
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
CC transformation. Inhibits skeletal muscle and cardiac myocyte
CC differentiation. Regulates the circadian clock by repressing the
CC transcriptional activator activity of the CLOCK-ARNTL/BMAL1
CC heterodimer. {ECO:0000269|PubMed:16556596,
CC ECO:0000269|PubMed:19217292}.
CC -!- SUBUNIT: Heterodimer with other HLH proteins. Interacts with CLOCK and
CC ARNTL/BMAL1 (By similarity). Interacts with COPS5, IFI204, GATA4 and
CC NKX2-5. {ECO:0000250, ECO:0000269|PubMed:11940648,
CC ECO:0000269|PubMed:15451666, ECO:0000269|PubMed:16556596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16516211}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16516211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P20067-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P20067-2; Sequence=VSP_002109;
CC -!- INDUCTION: Expressed in a circadian manner in the suprachiasmatic
CC nucleus (SCN) of the brain and heart with peak levels seen between CT16
CC and CT20 in the SCN and between CT8 and CT12 in the heart.
CC {ECO:0000269|PubMed:19217292}.
CC -!- PTM: Polyubiquitinated; which is favored by Ifi204 and leads to
CC proteasomal degradation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37879.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M31885; AAA37879.1; ALT_INIT; mRNA.
DR EMBL; U43884; AAC52760.1; -; mRNA.
DR EMBL; AK008264; BAB25564.1; -; mRNA.
DR CCDS; CCDS16897.1; -. [P20067-2]
DR CCDS; CCDS89567.1; -. [P20067-1]
DR PIR; A34690; A34690.
DR PIR; S72171; S72171.
DR PDB; 6MGM; X-ray; 1.79 A; A/B=52-104.
DR PDB; 6MGN; X-ray; 1.90 A; B=58-104.
DR PDB; 6U2U; X-ray; 1.50 A; A/B=59-104.
DR PDBsum; 6MGM; -.
DR PDBsum; 6MGN; -.
DR PDBsum; 6U2U; -.
DR AlphaFoldDB; P20067; -.
DR SMR; P20067; -.
DR IntAct; P20067; 3.
DR MINT; P20067; -.
DR STRING; 10090.ENSMUSP00000092019; -.
DR iPTMnet; P20067; -.
DR PhosphoSitePlus; P20067; -.
DR MaxQB; P20067; -.
DR PaxDb; P20067; -.
DR PRIDE; P20067; -.
DR ProteomicsDB; 267189; -. [P20067-1]
DR ProteomicsDB; 267190; -. [P20067-2]
DR Antibodypedia; 25205; 396 antibodies from 37 providers.
DR Ensembl; ENSMUST00000038368; ENSMUSP00000092019; ENSMUSG00000042745. [P20067-2]
DR MGI; MGI:96396; Id1.
DR VEuPathDB; HostDB:ENSMUSG00000042745; -.
DR eggNOG; ENOG502RZP5; Eukaryota.
DR GeneTree; ENSGT00940000161109; -.
DR HOGENOM; CLU_116790_0_0_1; -.
DR InParanoid; P20067; -.
DR OMA; QMNVFLQ; -.
DR PhylomeDB; P20067; -.
DR TreeFam; TF326217; -.
DR Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR ChiTaRS; Id1; mouse.
DR PRO; PR:P20067; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P20067; protein.
DR Bgee; ENSMUSG00000042745; Expressed in mucous cell of stomach and 361 other tissues.
DR ExpressionAtlas; P20067; baseline and differential.
DR Genevisible; P20067; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070628; F:proteasome binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; IDA:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0060426; P:lung vasculature development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IDA:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR GO; GO:1901342; P:regulation of vasculature development; ISO:MGI.
DR GO; GO:0046677; P:response to antibiotic; IMP:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR026052; DNA-bd_prot-inh.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR11723; PTHR11723; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cytoplasm;
KW Developmental protein; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..168
FT /note="DNA-binding protein inhibitor ID-1"
FT /id="PRO_0000127237"
FT DOMAIN 46..98
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 53..106
FT /note="Interaction with IFI204"
FT /evidence="ECO:0000250"
FT MOTIF 91..104
FT /note="Nuclear export signal"
FT VAR_SEQ 136..168
FT /note="VRSESEYYIILQWETEATGGGCPPSLLFRRIAI -> AACVPADDRILCR
FT (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:2156629"
FT /id="VSP_002109"
FT CONFLICT 140
FT /note="S -> A (in Ref. 3; BAB25564)"
FT /evidence="ECO:0000305"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:6U2U"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6U2U"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:6U2U"
SQ SEQUENCE 168 AA; 17914 MW; 7F7EF0177358F516 CRC64;
MKVASGSAAA AAGPSCSLKA GRTAGEVVLG LSEQSVAISR CAGTRLPALL DEQQVNVLLY
DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT TGGRGLPVRA
PLSTLNGEIS ALAAEVRSES EYYIILQWET EATGGGCPPS LLFRRIAI
