ID2_RAT
ID ID2_RAT Reviewed; 134 AA.
AC P41137;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA-binding protein inhibitor ID-2;
DE AltName: Full=Inhibitor of DNA binding 2;
DE AltName: Full=Inhibitor of differentiation 2;
GN Name=Id2; Synonyms=Id-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7908517; DOI=10.1006/bbrc.1994.1380;
RA Nagata Y., Todokoro K.;
RT "Activation of helix-loop-helix proteins Id1, Id2 and Id3 during neural
RT differentiation.";
RL Biochem. Biophys. Res. Commun. 199:1355-1362(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
RN [3]
RP PHOSPHORYLATION.
RX PubMed=7864897; DOI=10.1006/bbrc.1995.1273;
RA Nagata Y., Shoji W., Obinata M., Todokoro K.;
RT "Phosphorylation of helix-loop-helix proteins ID1, ID2 and ID3.";
RL Biochem. Biophys. Res. Commun. 207:916-926(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Restricts the CLOCK and ARNTL/BMAL1 localization to the
CC cytoplasm. Plays a role in both the input and output pathways of the
CC circadian clock: in the input component, is involved in modulating the
CC magnitude of photic entrainment and in the output component,
CC contributes to the regulation of a variety of liver clock-controlled
CC genes involved in lipid metabolism (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GATA4, IFI204, NR0B2 and NKX2-5. Interacts with
CC CLOCK and ARNTL/BMAL1 (By similarity). Heterodimer with other HLH
CC proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41136}. Nucleus
CC {ECO:0000250|UniProtKB:P41136}.
CC -!- DOMAIN: The bHLH domain is essential for its repressor activity towards
CC the CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by CDK1, PKA and PKC.
CC {ECO:0000269|PubMed:7864897}.
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DR EMBL; D10863; BAA01634.1; -; mRNA.
DR EMBL; BC086391; AAH86391.1; -; mRNA.
DR PIR; JC2112; JC2112.
DR RefSeq; NP_037192.1; NM_013060.3.
DR AlphaFoldDB; P41137; -.
DR SMR; P41137; -.
DR BioGRID; 247617; 3.
DR STRING; 10116.ENSRNOP00000009491; -.
DR iPTMnet; P41137; -.
DR PhosphoSitePlus; P41137; -.
DR PaxDb; P41137; -.
DR Ensembl; ENSRNOT00000009491; ENSRNOP00000009491; ENSRNOG00000007237.
DR GeneID; 25587; -.
DR KEGG; rno:25587; -.
DR CTD; 3398; -.
DR RGD; 2859; Id2.
DR eggNOG; ENOG502RZP5; Eukaryota.
DR GeneTree; ENSGT00940000156464; -.
DR HOGENOM; CLU_116790_2_1_1; -.
DR InParanoid; P41137; -.
DR OMA; SFRKNGA; -.
DR OrthoDB; 1624054at2759; -.
DR PRO; PR:P41137; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007237; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; P41137; baseline and differential.
DR Genevisible; P41137; RN.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0003166; P:bundle of His development; ISO:RGD.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; ISO:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0009649; P:entrainment of circadian clock; ISO:RGD.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISO:RGD.
DR GO; GO:0061030; P:epithelial cell differentiation involved in mammary gland alveolus development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0002521; P:leukocyte differentiation; ISO:RGD.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0060749; P:mammary gland alveolus development; ISS:UniProtKB.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0003149; P:membranous septum morphogenesis; ISO:RGD.
DR GO; GO:0001656; P:metanephros development; ISO:RGD.
DR GO; GO:0001779; P:natural killer cell differentiation; ISO:RGD.
DR GO; GO:0045578; P:negative regulation of B cell differentiation; ISO:RGD.
DR GO; GO:1904797; P:negative regulation of core promoter binding; ISO:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; ISO:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; ISO:RGD.
DR GO; GO:0048541; P:Peyer's patch development; ISO:RGD.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0001966; P:thigmotaxis; ISO:RGD.
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 Biological rhythms; Cytoplasm; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..134
FT /note="DNA-binding protein inhibitor ID-2"
FT /id="PRO_0000127244"
FT DOMAIN 23..75
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT MOTIF 106..115
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41136"
SQ SEQUENCE 134 AA; 14989 MW; A0D98D54EFDEB7B5 CRC64;
MKAFSPVRSV RKNSLSDHSL GISRSKTPVD DPMSLLYNMN DCYSKLKELV PSIPQNKKVT
KMEILQHVID YILDLQIALD SHPTIVSLHH QRPGQNQTSR TPLTTLNTDI SILSLQASEF
PSELMSNDSK VLCG
