RS27A_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27A_DROME
• UniProt AC: P15357
• Protein Name: Ubiquitin-40S ribosomal protein S27a
• Gene Name: RpS27A
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 156
• 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-48-linked is involved in protein degradation via the proteasome. 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: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKNYSTPKKIKHKRKKVKLAVLKYYKVDENGKIHRLRRECPGENCGAGVFMAAHEDRHYCGKCNLTFVFSKPEEK

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
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	27794539
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27794539
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	19429919
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	19429919
104	Acetylation	KVKLAVLKYYKVDEN HHEEEEEEEEEECCC	39.68	21791702
107	Acetylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	21791702
113	Acetylation	YKVDENGKIHRLRRE EEECCCCCEEEEEEC	47.09	21791702

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

Oops, there are no upstream regulatory protein records of RS27A_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27A_DROME !!

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_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DORS_DROME	dl	physical	14605208
GRIM_DROME	grim	physical	23940367
KLD10_DROME	slim	physical	25242320

Drug and Disease Associations

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