KMT5A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KMT5A_MOUSE
• UniProt AC: Q2YDW7
• Protein Name: N-lysine methyltransferase KMT5A {ECO:0000305}
• Gene Name: Kmt5a {ECO:0000250|UniProtKB:Q9NQR1}
• Organism: Mus musculus (Mouse).
• Sequence Length: 349
• Subcellular Localization: Nucleus. Chromosome . Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin (By similarity). Colocalized with SIRT2 at mitotic foci. Associates with chrom
• Protein Description: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration (By similarity)..
• Protein Sequence: MARGRKMCKPRAVEAAAAAVAATAPGPEMVEQRGPGRPRSDGENVFAGQSKIYAYMSPNKCSAMRSPLQEENSVAHHEVKCPGKPLAGIYRKREEKRNTGNVIRSAVKSDEQKSKDTRRGPLAPFPNQKSEAAEPPKTPPPSCDSTNVAVAKQALKKSLKGKQAPRKKSQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKKNELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYVQDPSTGCYMYYFQYLSKTYCVDATQETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAYPWLKH

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
40	Phosphorylation	RGPGRPRSDGENVFA CCCCCCCCCCCCCCC		29514104
55	Phosphorylation	GQSKIYAYMSPNKCS CCCEEEEEECCCCCC		28066266
57	Phosphorylation	SKIYAYMSPNKCSAM CEEEEEECCCCCCCC		26745281
99	Phosphorylation	KREEKRNTGNVIRSA CHHHHCCCHHHHHHH		22345495
129	Acetylation	LAPFPNQKSEAAEPP CCCCCCCCCCCCCCC		-
138	Phosphorylation	EAAEPPKTPPPSCDS CCCCCCCCCCCCCCC		27742792
142	Phosphorylation	PPKTPPPSCDSTNVA CCCCCCCCCCCCHHH		25619855
145	Phosphorylation	TPPPSCDSTNVAVAK CCCCCCCCCHHHHHH		25619855
146	Phosphorylation	PPPSCDSTNVAVAKQ CCCCCCCCHHHHHHH		25619855
231	Methylation	GRGVIATKQFSRGDF CCEEEEEEEECCCCE		-
231	Ubiquitination	GRGVIATKQFSRGDF CCEEEEEEEECCCCE		-

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

Oops, there are no upstream regulatory protein records of KMT5A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
129	K	Acetylation	Acetylated at Lys-129; does not change methyltransferase activity.	-
129	K	Acetylation	Deacetylated at Lys-129 by SIRT2; does not change methyltransferase activity (By similarity).	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KMT5A_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KMT5A_MOUSE !!

Drug and Disease Associations

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