BYST_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BYST_MOUSE
• UniProt AC: O54825
• Protein Name: Bystin
• Gene Name: Bysl
• Organism: Mus musculus (Mouse).
• Sequence Length: 436
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus . Associated with 40S ribosomal subunits.
• Protein Description: Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits..
• Protein Sequence: MPKFKVTRGASNREKHAPLAEQILAGNAVRAGTREKRRGREVEEEEEYVGPRLSRRILQQARQQQEELETDHGAGDRSAPPRERATRLGPGLPQDGSDEEDEEWPTLEKAAKMAGVDHQAEVIVDPEDERAIEMFMNKNPPVRRTLADIIMEKLTEKQTEVETVMSEVSGFPMPQLDPRVLEVYRGVREVLCKYRSGKLPKAFKVIPALSNWEQILYVTEPEAWTAAAMYQATRIFASNLKERMAQRFYNLVLLPRVRDDIAEYKRLNFHLYMALKKALFKPGAWFKGILIPLCESGTCTLREAIIVGSIITKCSIPVLHSSAAMLKIAEMEYSGANSIFLRLLLDKKYALPYRVLDALVFHFLAFRTEKRQLPVLWHQCLLTLAQRYKADLATEQKEALLELLRLQPHPQLSPEIRRELQSAVPRDVEDGGVTME

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	Methylation	TREKRRGREVEEEEE CCCHHCCCCCCCHHH	42.87	-
48	Phosphorylation	EVEEEEEYVGPRLSR CCCCHHHCCCHHHHH	17.62	25159016
54	Phosphorylation	EYVGPRLSRRILQQA HCCCHHHHHHHHHHH	22.31	-
97	Phosphorylation	PGLPQDGSDEEDEEW CCCCCCCCCCCCCCC	50.57	24925903
106	Phosphorylation	EEDEEWPTLEKAAKM CCCCCCCHHHHHHHH	48.93	25619855
155	Phosphorylation	DIIMEKLTEKQTEVE HHHHHHHHCCCHHHH	52.80	22006019
159	Phosphorylation	EKLTEKQTEVETVMS HHHHCCCHHHHHHHH	53.73	23649490
163	Phosphorylation	EKQTEVETVMSEVSG CCCHHHHHHHHHHCC	27.04	23649490
166	Phosphorylation	TEVETVMSEVSGFPM HHHHHHHHHHCCCCC	30.43	26745281
169	Phosphorylation	ETVMSEVSGFPMPQL HHHHHHHCCCCCCCC	30.57	26745281
230	Phosphorylation	AWTAAAMYQATRIFA HHHHHHHHHHHHHHH	7.11	22817900
264	Phosphorylation	VRDDIAEYKRLNFHL CCCCHHHHHHHCHHH	7.74	20531401
388	Phosphorylation	LLTLAQRYKADLATE HHHHHHHHHCCCHHH	9.84	18779572
413	Phosphorylation	LQPHPQLSPEIRREL HCCCCCCCHHHHHHH	18.42	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BYST_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 BYST_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BYST_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.
PubMed: 19131326

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.
PubMed: 19144319

"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.
PubMed: 18630941