RS27A_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27A_BOVIN
• UniProt AC: P62992
• Protein Name: Ubiquitin-40S ribosomal protein S27a
• Gene Name: RPS27A
• Organism: Bos taurus (Bovine).
• 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-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, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. 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).; 40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome..
• Protein Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK

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	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
29	Acetylation	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	-
76	ADP-ribosylation	LVLRLRGGAKKRKKK HHHHHCCCCHHCCCC	27.99	-
104	Acetylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	-
113	Acetylation	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	-
152	Acetylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	-

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
65	S	Phosphorylation	Kinase	PINK1	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27A_BOVIN !!

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_BOVIN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS27A_BOVIN	RPS27A	physical	26171660

Drug and Disease Associations

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