dbPTM

YCCC_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YCCC_SCHPO
UniProt AC	O59776
Protein Name	Uncharacterized protein C1795.12c
Gene Name	SPCC1795.12c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	112
Subcellular Localization	Golgi apparatus membrane Single-pass membrane protein . Endoplasmic reticulum membrane Single-pass membrane protein .
Protein Description
Protein Sequence	MYRPTTTSYSPVYTGNPLYDISASQSDPRQRIRKNVRFQTEVDEFPDFDDSDSDELQFENRDPRKRIDPIKHMLLVQRLKRVSTSSRRLFIFTLSMFLIAFILLIAFVSFRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
51	Phosphorylation	EFPDFDDSDSDELQF CCCCCCCCCCCCCCC	40.64	28889911
53	Phosphorylation	PDFDDSDSDELQFEN CCCCCCCCCCCCCCC	36.62	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 YCCC_SCHPO !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YCCC_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of YCCC_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-51 AND SER-53, AND MASSSPECTROMETRY.	18257517 [Abstract]