CPLM-023101

Genbank Nucleotide ID

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
119	VPDFDPAKLARRSQE	ubiquitination	[1, 2]
156	YIAIAKEKHGYNMEQ	ubiquitination	[2]
294	TETVPQVKKEKHSTQ	sumoylation	[3]
418	NKSVVQVKNFFVNYR	ubiquitination	[4, 5, 6]

[1] 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]
[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] Sumoylation of CoREST modulates its function as a transcriptional repressor.
Muraoka A, Maeda A, Nakahara N, Yokota M, Nishida T, Maruyama T, Ohshima T.
Biochem Biophys Res Commun. 2008 Dec 26;377(4):1031-5. [PMID: 18854179]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation.

DOMAIN 100 186 ELM2.
DOMAIN 187 238 SANT 1.
DOMAIN 378 429 SANT 2.
REGION 75 254 Interaction with HDAC1.
REGION 293 381 Interaction with KDM1A.
MOD_RES 124 124 Phosphoserine.
MOD_RES 257 257 Phosphoserine.
MOD_RES 457 457 Phosphoserine.

3D-structure; Chromatin regulator; Coiled coil; Complete proteome; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO:0003682; F:chromatin binding; IEA:InterPro.
GO:0001078; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:UniProtKB.
GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO:0007596; P:blood coagulation; TAS:Reactome.
GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.

IPR000949; ELM2_dom.
IPR009057; Homeodomain-like.
IPR001005; SANT/Myb.
IPR017884; SANT_dom.

PF01448; ELM2
PF00249; Myb_DNA-binding

PS51156; ELM2
PS51293; SANT