Search by BoMiProt ID - Bomi6738


Primary Information

BoMiProt ID Bomi6738
Protein Name Lethal(3)malignant brain tumor-like protein 2/L(3)mbt-like protein 2
Organism Bos taurus
Uniprot IDQ1JQD9
Milk FractionWhey
Ref Sequence ID NP_001069078.1
Aminoacid Length 706
Molecular Weight 79081
FASTA Sequence Download
Gene Name L3MBTL2
Gene ID 513297
Protein Existence Status reviewed

Secondary Information

Protein Function L3MBTL2 plays important roles in chromatin remodeling during meiosis and spermiogenesis.Maintain the transcriptionally repressive state of genes. binds and compacts nucleosomes independently of histone modifications.negatively regulates p21.
Biochemical Properties Contain atypical C2/C2 type Zn finger in the N-terminal portion of the protein followed by four MBT-domain.
PTMs Isopeptide bond formation, Phosphorylation, Ubl conjugation,SUMOylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q1JQD9|LMBL2_BOVIN Lethal(3)malignant brain tumor-like protein 2 OS=Bos taurus OX=9913 GN=L3MBTL2 PE=2 SV=1 MEKPRGVEETPSS*13EPMEEEEEDDDLELFGGYDSFRSYNSSAGSESSSYLEESSEAEHEDR EAGELPTS*68PLHLLSPGT*77PRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYS SNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHSQGTGQLADGTPTGQDALVLGF DWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIASVIQAA GYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKGYLMK RLVGSRTLPVDFHIKMVESMKYPFRQGMRLEVVDKSQVS*339RTRMAVVDTVIGGRLRLLYED GDSDDDFWCHMWSPLIHPVGWSRRVGHGIKLSERRSDMAHHPTFRKIYCDAVPYLFKKVR AVYTEGGWFEEGMKLEAIDPLNLGNICVATICKVLLDGYLMICVDGGPSTDGSDWFCYHA SSHAIFPANFCQKNDIELTPPKGYEAHTFSWEAYLEKTKAKAAPSRLFNMDCPNHGFKVG MKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGY QLQPPVATEPTTPLKAKEATKKKKKQFGKKRKRIPPAKTRPLRQGSKKALLEEDLQAAAK APSEPAPDEIITVRVKEEHLDVATADKALS*690PELPVPVENIKQETDD
Predicted Disorder Regions 1-85, 119-148, 613-644, 658-706
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs SUMOylation of L3MBTL2 facilitates repression of these PRC1.6-target genes by balancing the local H2Aub1 levels established by the ubiquitinating enzyme RING2 and the de-ubiquitinating PR–DUB complex.
Bibliography 1.Stielow C, Stielow B, Finkernagel F, Scharfe M, Jarek M, Suske G. SUMOylation of the polycomb group protein L3MBTL2 facilitates repression of its target genes. Nucleic Acids Res. 2014 Mar;42(5):3044-58. doi: 10.1093/nar/gkt1317. Epub 2013 Dec 24. PMID: 24369422; PMCID: PMC3950706. 2.Trojer, P., Cao, A. R., Gao, Z., Li, Y., Zhang, J., Xu, X., Li, G., Losson, R., Erdjument-Bromage, H., Tempst, P., Farnham, P. J., & Reinberg, D. (2011). L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure. Molecular cell, 42(4), 438–450. https://doi.org/10.1016/j.molcel.2011.04.004 2.Meng C, Liao J, Zhao D, Huang H, Qin J, Lee TL, Chen D, Chan WY, Xia Y. L3MBTL2 regulates chromatin remodeling during spermatogenesis. Cell Death Differ. 2019 Nov;26(11):2194-2207. doi: 10.1038/s41418-019-0283-z. Epub 2019 Feb 13. PMID: 30760872; PMCID: PMC6889272.