RS27A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27A_RAT
• UniProt AC: P62982
• Protein Name: Ubiquitin-40S ribosomal protein S27a
• Gene Name: Rps27a
• Organism: Rattus norvegicus (Rat).
• 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: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMGSHFDRHYCGKCCLTYCFNKPEDK

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	-
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	25575281
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	25575281
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	22673903
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	23984901
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	22673903
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25575281
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27097102
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	29779826
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHH	15.70	27097102
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	28432305
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	28432305
76	ADP-ribosylation	LVLRLRGGAKKRKKK HHHHHCCCCHHCCCC	27.99	-
104	Acetylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	22902405
107	Acetylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	22902405
113	Ubiquitination	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	-
113	Acetylation	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	22902405
152	Acetylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	25786129
156	Acetylation	CFNKPEDK------- HCCCCCCC-------	61.65	26302492

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	B5DFG1	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
65	S	Phosphorylation	[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.	-
65	S	ubiquitylation	[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.	-

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RS27A_RAT !!

Drug and Disease Associations

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