CPLM-011560

Genbank Nucleotide ID

Amino-terminal enhancer of split

Protein Synonyms/Alias

Amino enhancer of split; Gp130-associated protein GAM; Protein ESP1; Protein GRG

Homo sapiens (Human)

Position	Peptide	Type	References
19	SHLPQQLKFTTSDSC	ubiquitination	[1, 2, 3, 4, 5]
30	SDSCDRIKDEFQLLQ	ubiquitination	[1, 4, 5, 6]
44	QAQYHSLKLECDKLA	ubiquitination	[4]
49	SLKLECDKLASEKSE	ubiquitination	[4]
54	CDKLASEKSEMQRHY	ubiquitination	[4, 6]
112	LGAIERAKQVTAPEL	ubiquitination	[2, 4, 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] 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]
[3] 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]
[4] 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]
[5] 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]
[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

Acts as dominant repressor towards other family members. Inhibits NF-kappa-B-regulated gene expression. May be required for the initiation and maintenance of the differentiated state.

REGION 166 197 CCN domain.
MOD_RES 196 196 Phosphoserine.

Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation; Wnt signaling pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO:0031668; P:cellular response to extracellular stimulus; IEA:Compara.
GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB.
GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
GO:0060761; P:negative regulation of response to cytokine stimulus; IMP:BHF-UCL.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO:0009887; P:organ morphogenesis; TAS:ProtInc.
GO:2000210; P:positive regulation of anoikis; IMP:UniProtKB.
GO:0040008; P:regulation of growth; IEA:Compara.
GO:0070555; P:response to interleukin-1; IDA:BHF-UCL.
GO:0001501; P:skeletal system development; IEA:Compara.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.

IPR005617; Groucho/TLE_N.