SUV92_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUV92_MOUSE
• UniProt AC: Q9EQQ0
• Protein Name: Histone-lysine N-methyltransferase SUV39H2
• Gene Name: Suv39h2
• Organism: Mus musculus (Mouse).
• Sequence Length: 477
• Subcellular Localization: Nucleus. Chromosome. Chromosome, centromere. Associates with centromeric constitutive heterochromatin during most stages of spermato- and spermiogenesis. Predominantly accumulates at the sex chromosomes present at the XY body.
• 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 cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher-order chromatin organization during spermatogenesis. Recruited by the large 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: MATARAKARGSEAGARCHRAPGPPPRPKARRTARRRRAETLTARRSRPSAGERRAGSQRAWSGAPRAAVFGDECARGALFKAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVAKGVEYYLVKWKGWPDSTNTWEPLRNLRCPQLLRQFSDDKKTYLAQERKCKAVNSKSLQPAIAEYIVQKAKQRIALQRWQDYLNRRKNHKGMIFVENTVDLEGPPLDFYYINEYRPAPGISINSEATFGCSCTDCFFDKCCPAEAGVVLAYNKKQQIKIQPGTPIYECNSRCRCGPECPNRIVQKGTQYSLCIFKTSNGCGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFSVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGEASSDSIDHSPAKKRVRTQCKCGAETCRGYLN

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
138	Acetylation	GVEYYLVKWKGWPDS CCEEEEEEECCCCCC	40.36	7713507
165	Phosphorylation	PQLLRQFSDDKKTYL HHHHHHCCCCHHHHH	36.24	29514104
444	Phosphorylation	FDYQMKGSGEASSDS EEEEECCCCCCCCCC	28.13	21149613
448	Phosphorylation	MKGSGEASSDSIDHS ECCCCCCCCCCCCCC	30.31	21149613
449	Phosphorylation	KGSGEASSDSIDHSP CCCCCCCCCCCCCCH	42.28	21149613
451	Phosphorylation	SGEASSDSIDHSPAK CCCCCCCCCCCCHHH	31.68	21149613
455	Phosphorylation	SSDSIDHSPAKKRVR CCCCCCCCHHHHHHH	23.86	23375375

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

Oops, there are no upstream regulatory protein records of SUV92_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUV92_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SUV92_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SUV92_MOUSE !!

Drug and Disease Associations

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