RS27A_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27A_SCHPO
• UniProt AC: P0C016
• Protein Name: Ubiquitin-40S ribosomal protein S27a
• Gene Name: ubi3
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 150
• Subcellular Localization: Ubiquitin: Cytoplasm. Nucleus.
• Protein Description: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).; Ribosomal protein S27a is a component of the 40S subunit of the ribosome..
• Protein Sequence: MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEN

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
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEE	31.36	-
27	Ubiquitination	SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC	52.89	-
33	Ubiquitination	VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH	41.27	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24763107
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	28889911
87	Phosphorylation	RKKKTYTTPKKIKHK CCCCCCCCCHHHCCC	23.77	27738172
105	Phosphorylation	VELAVLKYYKVEDDG EEEEEEEEEEECCCC	12.35	25720772
106	Phosphorylation	ELAVLKYYKVEDDGS EEEEEEEEEECCCCC	13.63	25720772
113	Phosphorylation	YKVEDDGSVKRLRRE EEECCCCCEEHHHHH	31.31	25720772

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

Oops, there are no upstream regulatory protein records of RS27A_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27A_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RS27A_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PUB3_SCHPO	pub3	physical	26771498

Drug and Disease Associations

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