CPLM-010957

Genbank Nucleotide ID

DNA-binding protein inhibitor ID-3

Protein Synonyms/Alias

Class B basic helix-loop-helix protein 25; bHLHb25; Helix-loop-helix protein HEIR-1; ID-like protein inhibitor HLH 1R21; Inhibitor of DNA binding 3

1R21; BHLHB25; HEIR1

Homo sapiens (Human)

Position	Peptide	Type	References
2	******MKALSPVRG	ubiquitination	[1, 2]
30	AIARGRGKGPAAEEP	ubiquitination	[1, 2, 3, 4, 5]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

Functional Description

ID (inhibitor of DNA binding) HLH proteins lack a basic DNA-binding domain but are able to form heterodimers with other HLH proteins, thereby inhibiting DNA binding. Involved in myogenesis by inhibiting skeletal muscle and cardiac myocyte differentiation and promoting muscle precursor cells proliferation. Inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. May inhibit other transcription factors.

3D-structure; Complete proteome; Myogenesis; Nucleus; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:Compara.
GO:0005634; C:nucleus; IC:GDB.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO:0007417; P:central nervous system development; IEA:Compara.
GO:0030855; P:epithelial cell differentiation; IEA:Compara.
GO:0007507; P:heart development; IEA:Compara.
GO:0001656; P:metanephros development; IEA:Compara.
GO:0007275; P:multicellular organismal development; TAS:ProtInc.
GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Compara.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:GDB.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:GDB.
GO:0030182; P:neuron differentiation; IEA:Compara.
GO:0030903; P:notochord development; IEA:Compara.
GO:0042476; P:odontogenesis; IEA:Compara.
GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
GO:0051726; P:regulation of cell cycle; IEA:Compara.
GO:0006275; P:regulation of DNA replication; IEA:Compara.
GO:0009611; P:response to wounding; IEA:Compara.
GO:0006351; P:transcription, DNA-dependent; IEA:Compara.

IPR011598; bHLH_dom.
IPR026052; DNA-bd_prot-inh.