dbPTM

MU123_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MU123_SCHPO
UniProt AC	O74461
Protein Name	Meiotically up-regulated gene 123 protein
Gene Name	mug123
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	235
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Involved in sporulation and has a role in meiosis..
Protein Sequence	MERLATRSSHDDPYSRSSLPTSNAINSNHESNGSTFSYVQSLRRAKATVWSDIGRVAPLHSSPSIKSSSQNGKSSSKGLGGMRSRVFSSQHHGVYHTRPASLHSRTMAPQHTILTPRLSATEGKDDDEDELVISTSNTAPTYISMIESSRASSTHSGTAPSIMGMSIHSRADSRAETTQSDGFESRSGSPTHDIQSYLVNRRSSSSESSDEDSAEEGMKRLVITNMGDNDEFDSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MERLATRSSHDDP --CCCCCCCCCCCCC	35.36	28889911
8	Phosphorylation	MERLATRSSHDDPYS CCCCCCCCCCCCCCC	27.89	29996109
9	Phosphorylation	ERLATRSSHDDPYSR CCCCCCCCCCCCCCC	27.87	29996109
48	Phosphorylation	SLRRAKATVWSDIGR HHHHHCCEEECCCCC	23.08	21712547
61	Phosphorylation	GRVAPLHSSPSIKSS CCCCCCCCCCCCCCC	52.18	29996109
62	Phosphorylation	RVAPLHSSPSIKSSS CCCCCCCCCCCCCCC	16.36	24763107
64	Phosphorylation	APLHSSPSIKSSSQN CCCCCCCCCCCCCCC	44.59	24763107
67	Phosphorylation	HSSPSIKSSSQNGKS CCCCCCCCCCCCCCC	33.29	21712547
68	Phosphorylation	SSPSIKSSSQNGKSS CCCCCCCCCCCCCCC	30.82	21712547
69	Phosphorylation	SPSIKSSSQNGKSSS CCCCCCCCCCCCCCC	34.45	21712547
173	Phosphorylation	SIHSRADSRAETTQS EEECCCCCCCCCCCC	32.19	25720772
177	Phosphorylation	RADSRAETTQSDGFE CCCCCCCCCCCCCCC	29.20	25720772
178	Phosphorylation	ADSRAETTQSDGFES CCCCCCCCCCCCCCC	19.99	25720772
180	Phosphorylation	SRAETTQSDGFESRS CCCCCCCCCCCCCCC	37.29	28889911
185	Phosphorylation	TQSDGFESRSGSPTH CCCCCCCCCCCCCCH	29.50	25720772
187	Phosphorylation	SDGFESRSGSPTHDI CCCCCCCCCCCCHHH	53.56	28889911
189	Phosphorylation	GFESRSGSPTHDIQS CCCCCCCCCCHHHHH	28.07	28889911
191	Phosphorylation	ESRSGSPTHDIQSYL CCCCCCCCHHHHHHH	33.60	28889911
196	Phosphorylation	SPTHDIQSYLVNRRS CCCHHHHHHHHHCCC	22.29	25720772
197	Phosphorylation	PTHDIQSYLVNRRSS CCHHHHHHHHHCCCC	9.78	25720772
234	Phosphorylation	GDNDEFDSD------ CCCCCCCCC------	51.01	28889911

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of MU123_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MU123_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MU123_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PIL1_SCHPO	pil1	physical	26771498

Drug and Disease Associations

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

Regulatory Network of MU123_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-187; SER-189AND THR-191, AND MASS SPECTROMETRY.	18257517 [Abstract]