CPLM-008705

Genbank Nucleotide ID

CCAAT/enhancer-binding protein gamma

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
113	AKIKLLTKELSVLKD	ubiquitination	[1, 2, 3, 4, 5]
119	TKELSVLKDLFLEHA	ubiquitination	[6]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] 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]
[4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[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]
[6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]

Functional Description

Transcription factor that binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene. Might change the DNA-binding specificity of other transcription factors and recruit them to unusual DNA sites.

DOMAIN 62 125 bZIP.
REGION 66 93 Basic motif (By similarity).
REGION 97 118 Leucine-zipper (By similarity).

Activator; Complete proteome; DNA-binding; Nucleus; Reference proteome; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; ISS:UniProtKB.
GO:0003690; F:double-stranded DNA binding; IEA:Compara.
GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO:0043353; P:enucleate erythrocyte differentiation; ISS:UniProtKB.
GO:0001889; P:liver development; ISS:UniProtKB.
GO:0016071; P:mRNA metabolic process; IEA:Compara.
GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
GO:0043388; P:positive regulation of DNA binding; TAS:UniProtKB.
GO:0045739; P:positive regulation of DNA repair; IEP:UniProtKB.
GO:0045078; P:positive regulation of interferon-gamma biosynthetic process; ISS:UniProtKB.
GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; TAS:UniProtKB.
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

PS50217; BZIP
PS00036; BZIP_BASIC