SUV91_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUV91_MOUSE
• UniProt AC: O54864
• Protein Name: Histone-lysine N-methyltransferase SUV39H1
• Gene Name: Suv39h1
• Organism: Mus musculus (Mouse).
• Sequence Length: 412
• Subcellular Localization: Nucleus. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Associates with centromeric constitutive heterochromatin.
• Protein Description: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation..
• Protein Sequence: MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCIRVLKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYDLCIFRTNDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
159	Phosphorylation	DLDGPPRSFVYINEY CCCCCCCEEEEEEEE	25.49	28066266
214	Ubiquitination	DQGQVRLKAGQPIYE CCCCEEEECCCEEEE	39.65	-
266	Acetylation	RTLEKIRKNSFVMEY CCHHHHHCCCCHHHE	61.49	-
391	Phosphorylation	GLAGLPGSPKKRVRI CCCCCCCCCCCCEEE	31.44	27087446
409	Acetylation	CGTTACRKYLF---- CCCHHHHHHCC----	46.30	6566757

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SUV91_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
266	K	Acetylation	Acetylated at Lys-266, leading to inhibition of enzyme activity.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SUV91_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX1_MOUSE	Cbx1	physical	28059589
CBX5_MOUSE	Cbx5	physical	28059589

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.