Search by BoMiProt ID - Bomi7542


Primary Information

BoMiProt ID Bomi7542
Protein Name Non-histone chromosomal protein HMG-17
Organism Bos taurus
Uniprot IdP02313
Milk Fractionwhey
Ref Sequence Id NP_001092415.1
Aminoacid Length 90
Molecular Weight 9380
Fasta Sequence https://www.uniprot.org/uniprot/P02313.fasta
Gene Name HMGN2
Gene Id 512161
Protein Existence Status Reviewed

Secondary Information

Protein Function It is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair.Acts as a positive modulator of nuclear factor kappaB signalling to promote lipopolysaccharide-induced beta-defensin-2 expression.
Biochemical Properties Contains NBD and RRSARLSA motif.NBD is a highly conserved 30-amino acid region spanning from amino acids 17 to 47 of HMGN2, and the RRSARLSA motif (amino acids 22 to 29) is responsible for direct interaction with the nucleosome.SUMOylation sites of Lys-17 and Lys-35 are both located near the RRSARLSA motif, which is known as a nucleosomal binding site present in all HMGN proteins.
PTMs Acetylation,succinylation,Phosphorylation,Ubl conjugation,ADP-ribosylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P02313|HMGN2_BOVIN Non-histone chromosomal protein HMG-17 OS=Bos taurus OX=9913 GN=HMGN2 PE=1 SV=2 MPKRKAEGDAEGDKAKVKDEPQRRS*25ARLS*29AKPAPPKPEPKPKKAPAKKGEKVPKGKKGKA DAGKDGNNPAENGDAKTDQAQKAEGAGDAK
Predicted Disorder Regions (1-90)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association.Phosphorylation of HMGN2 also serves to abolish the interaction of HMGN2 with its chromatin targets.Acetylated HMGN2 has lower binding affinity for nucleosomes, suggesting that acetylation may function to loosen the interaction between HMGN2 and nucleosomes.SUMOylation by the SUMO E3 Ligase PIAS1 decreases the binding affinity to nucleosome core particles.DeSUMOylated by SENP. Lys-17 and Lys-35 are major SUMO sites in HMGN2 located in the NBD.
Bibliography 1.Wu, J., Kim, S., Kwak, M. S., Jeong, J. B., Min, H. J., Yoon, H. G., Ahn, J. H., & Shin, J. S. (2014). High mobility group nucleosomal binding domain 2 (HMGN2) SUMOylation by the SUMO E3 ligase PIAS1 decreases the binding affinity to nucleosome core particles. The Journal of biological chemistry, 289(29), 20000–20011. https://doi.org/10.1074/jbc.M114.555425 2.Jing Y, Tian G, Qin X, Liu Z, Li XD. Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2-nucleosome association. RSC Chem Biol. 2021 May 27;2(4):1257-1262. doi: 10.1039/d1cb00070e. PMID: 34458839; PMCID: PMC8341127.