RS27A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27A_MOUSE
• UniProt AC: P62983
• Protein Name: Ubiquitin-40S ribosomal protein S27a
• Gene Name: Rps27a
• Organism: Mus musculus (Mouse).
• 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.; 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	22790023
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Malonylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	26320211
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	27600695
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	22790023
11	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	27180971
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	27742792
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	26745281
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	26745281
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	22790023
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	22790023
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	22790023
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	22790023
48	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHH	15.70	24925903
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	22790023
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	26320211
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	26824392
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	22324799
76	ADP-ribosylation	LVLRLRGGAKKRKKK HHHHHCCCCHHCCCC	27.99	-
104	Succinylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	23954790
104	Malonylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	26320211
104	Ubiquitination	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	-
104	Acetylation	KVKLAVLKYYKVDEN HEEEEEEEEEEECCC	39.68	23806337
107	Malonylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	26320211
107	Acetylation	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	23864654
107	Ubiquitination	LAVLKYYKVDENGKI EEEEEEEEECCCCCE	39.87	-
113	Malonylation	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	26320211
113	Acetylation	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	23201123
113	Ubiquitination	YKVDENGKISRLRRE EEECCCCCEEEHHHH	49.44	-
115	Phosphorylation	VDENGKISRLRRECP ECCCCCEEEHHHHCC	28.84	29514104
121	Glutathionylation	ISRLRRECPSDECGA EEEHHHHCCCCCCCC	3.57	24333276
123	Phosphorylation	RLRRECPSDECGAGV EHHHHCCCCCCCCCC	58.67	26525534
126	Glutathionylation	RECPSDECGAGVFMG HHCCCCCCCCCCCCC	5.63	24333276
143	Acetylation	FDRHYCGKCCLTYCF CCCCCCCCEEHHHHC	20.43	22826441
143	Ubiquitination	FDRHYCGKCCLTYCF CCCCCCCCEEHHHHC	20.43	-
144	S-nitrosylation	DRHYCGKCCLTYCFN CCCCCCCEEHHHHCC	1.08	20925432
144	S-nitrosocysteine	DRHYCGKCCLTYCFN CCCCCCCEEHHHHCC	1.08	-
145	S-nitrosylation	RHYCGKCCLTYCFNK CCCCCCEEHHHHCCC	3.47	24926564
145	S-nitrosocysteine	RHYCGKCCLTYCFNK CCCCCCEEHHHHCCC	3.47	-
147	Phosphorylation	YCGKCCLTYCFNKPE CCCCEEHHHHCCCCC	12.34	-
148	Phosphorylation	CGKCCLTYCFNKPED CCCEEHHHHCCCCCC	5.10	-
149	S-nitrosylation	GKCCLTYCFNKPEDK CCEEHHHHCCCCCCC	2.27	20925432
149	S-nitrosocysteine	GKCCLTYCFNKPEDK CCEEHHHHCCCCCCC	2.27	-
152	Malonylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	26320211
152	Acetylation	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	23806337
152	Ubiquitination	CLTYCFNKPEDK--- EHHHHCCCCCCC---	29.54	-
156	Ubiquitination	CFNKPEDK------- HCCCCCCC-------	61.65	-

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	Q99MQ3	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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RS27A_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASSSPECTROMETRY.
PubMed: 17242355