dbPTM

RL40_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL40_MOUSE
UniProt AC	P62984
Protein Name	Ubiquitin-60S ribosomal protein L40
Gene Name	Uba52
Organism	Mus musculus (Mouse).
Sequence Length	128
Subcellular Localization	Ubiquitin: Cytoplasm. Nucleus. 60S ribosomal protein L40: Cytoplasm.
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.; 60S ribosomal protein L40: Component of the 60S subunit of the ribosome..
Protein Sequence	MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	27600695
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
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	-
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	17242355
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHH	15.70	24925903
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHHHHHH	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	27742792
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	22324799
76	ADP-ribosylation	LVLRLRGGIIEPSLR HHHHHCCCCCCHHHH	15.97	-
88	Acetylation	SLRQLAQKYNCDKMI HHHHHHHHCCCCHHH	32.59	22826441
93	Ubiquitination	AQKYNCDKMICRKCY HHHCCCCHHHHHHHH	32.15	-
93	Acetylation	AQKYNCDKMICRKCY HHHCCCCHHHHHHHH	32.15	22826441
98	"N6,N6,N6-trimethyllysine"	CDKMICRKCYARLHP CCHHHHHHHHHHHCH	27.47	-
98	Methylation	CDKMICRKCYARLHP CCHHHHHHHHHHHCH	27.47	-
115	S-nitrosocysteine	VNCRKKKCGHTNNLR HCCCHHCCCCCCCCC	7.11	-
115	Glutathionylation	VNCRKKKCGHTNNLR HCCCHHCCCCCCCCC	7.11	24333276
115	S-nitrosylation	VNCRKKKCGHTNNLR HCCCHHCCCCCCCCC	7.11	21278135
124	Acetylation	HTNNLRPKKKVK--- CCCCCCCCCCCC---	59.81	23864654

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	Q9BXM7	PSP
65	S	Phosphorylation	Kinase	PINK1	Q99MQ3	Uniprot
66	T	Phosphorylation	Kinase	PINK1	Q9BXM7	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RL40_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
FOXP3_MOUSE	Foxp3	physical	22579476
WRIP1_HUMAN	WRNIP1	physical	27062441

Drug and Disease Associations

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

Regulatory Network of RL40_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	17242355 [Abstract]

show

show