dbPTM

ORN_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ORN_SCHPO
UniProt AC	O94626
Protein Name	Probable oligoribonuclease
Gene Name	rex2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	252
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	3'-to-5' exoribonuclease specific for small oligoribonucleotides..
Protein Sequence	MQGAFLNNRIILQSYHIKKRLYSKRTSSLHSRFLQPTYRKNICQISKPIFQQDLSTNTNFISKLKSPFSNLKMSNLKQPLVWIDCEMTGLEVGKHVLMEVAAIITDGNLRPVEEKFDAVIKLDEKQLSEMNDWCIEQHGKSGLTERCRQSNLTVKDVENQLLAYIKKYIPKKREALIAGNSVHADVRFLSVEMPKIIEHLHYRIIDVSTIKELAKRWCPDIPAYDKKGDHRALSDILESIGELQHYRSYWLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
Oops, there are no PTM records of ORN_SCHPO !!

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 ORN_SCHPO !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RENT1_SCHPO	upf1	genetic	23619768

Drug and Disease Associations

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

Regulatory Network of ORN_SCHPO

Related Literatures of Post-Translational Modification