MO4L2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MO4L2_MOUSE
• UniProt AC: Q9R0Q4
• Protein Name: Mortality factor 4-like protein 2
• Gene Name: Morf4l2
• Organism: Mus musculus (Mouse).
• Sequence Length: 288
• Subcellular Localization: Nucleus .
• Protein Description: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. Also component of the MSIN3A complex which acts to repress transcription by deacetylation of nucleosomal histones (By similarity)..
• Protein Sequence: MSSRKQASQTRGQQSAEEDNFKKPTRSNMQRSKMRGAASGKKSAGSQPKNLDPALPGRWGGRSAENPPSGSVRKTRKNKQKAPGNGDGGSTSEVPQPPRKKRARADPTVESEEAFKSRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAILEEYANCKKSQGNVDNKEYAVNEVVGGIKEYFNVMLGTQLLYKFERPQYAEILLAHPDAPMSQIYGAPHLLRLFVRIGAMLAYTPLDEKSLALLLGYLHDFLKYLAKNSASLFTASDYKVASADYHRKAL

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
15	Phosphorylation	SQTRGQQSAEEDNFK HHHHCCHHHHHCCCC	29.75	25266776
69	Phosphorylation	RSAENPPSGSVRKTR CCCCCCCCCCCCCCC	44.98	29899451
71	Phosphorylation	AENPPSGSVRKTRKN CCCCCCCCCCCCCCC	24.08	26824392
74	Ubiquitination	PPSGSVRKTRKNKQK CCCCCCCCCCCCCCC	50.99	-
116	Ubiquitination	VESEEAFKSRMEVKV CCCHHHHHHCCEEEE	44.17	-
144	Ubiquitination	WDLVTRQKQLFQLPA CCHHHHHHHHHCCCC	45.75	27667366
152	Ubiquitination	QLFQLPAKKNVDAIL HHHCCCCCCCHHHHH	42.83	27667366
175	Ubiquitination	SQGNVDNKEYAVNEV HHCCCCCHHHHHHHH	47.87	-
262	Phosphorylation	YLHDFLKYLAKNSAS HHHHHHHHHHHCCCC	17.65	19367708
267	Phosphorylation	LKYLAKNSASLFTAS HHHHHHCCCCCCCHH	20.66	22817900
269	Phosphorylation	YLAKNSASLFTASDY HHHHCCCCCCCHHHH	24.68	22817900
277	Ubiquitination	LFTASDYKVASADYH CCCHHHHHHCCHHHH	35.99	-

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

Oops, there are no upstream regulatory protein records of MO4L2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MO4L2_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 MO4L2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of MO4L2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-262 AND SER-267, ANDMASS SPECTROMETRY.
PubMed: 19367708