dbPTM

RL23A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL23A_MOUSE
UniProt AC	P62751
Protein Name	60S ribosomal protein L23a
Gene Name	Rpl23a
Organism	Mus musculus (Mouse).
Sequence Length	156
Subcellular Localization
Protein Description	Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA (By similarity). May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination (By similarity)..
Protein Sequence	MAPKAKKEAPAPPKAEAKAKALKAKKAVLKGVHSHKKKKIRTSPTFRRPKTLRLRRQPKYPRKSAPRRNKLDHYAIIKFPLTTESAMKKIEDNNTLVFIVDVKANKHQIKQAVKKLYDIDVAKVNTLIRPDGEKKAYVRLAPDYDALDVANKIGII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MAPKAKKEA ------CCCHHCCCC	17.82	20668449
7	Malonylation	-MAPKAKKEAPAPPK -CCCHHCCCCCCCCH	65.06	26320211
14	Ubiquitination	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	-
14	Malonylation	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	26320211
14	Acetylation	KEAPAPPKAEAKAKA CCCCCCCHHHHHHHH	58.77	23201123
30	Ubiquitination	KAKKAVLKGVHSHKK HHHHHHHHHHHHCCC	52.90	-
41	Citrullination	SHKKKKIRTSPTFRR HCCCCCCCCCCCCCC	37.72	-
41	Citrullination	SHKKKKIRTSPTFRR HCCCCCCCCCCCCCC	37.72	24463520
42	Phosphorylation	HKKKKIRTSPTFRRP CCCCCCCCCCCCCCC	42.40	23684622
43	Phosphorylation	KKKKIRTSPTFRRPK CCCCCCCCCCCCCCC	16.46	25521595
45	Phosphorylation	KKIRTSPTFRRPKTL CCCCCCCCCCCCCHH	29.55	22942356
70	Ubiquitination	KSAPRRNKLDHYAII CCCCCCCCCCEEEEE	54.18	-
70	Acetylation	KSAPRRNKLDHYAII CCCCCCCCCCEEEEE	54.18	23806337
78	Acetylation	LDHYAIIKFPLTTES CCEEEEEECEECCHH	34.51	22826441
85	Phosphorylation	KFPLTTESAMKKIED ECEECCHHHHHHHCC	31.41	29514104
115	Malonylation	QIKQAVKKLYDIDVA HHHHHHHHHHCCCHH	45.76	26320211
115	Ubiquitination	QIKQAVKKLYDIDVA HHHHHHHHHHCCCHH	45.76	-
126	Phosphorylation	IDVAKVNTLIRPDGE CCHHHCCEEECCCCC	26.92	28725479
134	Acetylation	LIRPDGEKKAYVRLA EECCCCCCEEEEEEC	48.51	23201123
137	Phosphorylation	PDGEKKAYVRLAPDY CCCCCEEEEEECCCC	8.59	26239621
152	Ubiquitination	DALDVANKIGII--- CHHHHHHHHCCC---	32.35	-

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
Oops, there are no upstream regulatory protein records of RL23A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL23A_MOUSE !!

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 RL23A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RL23A_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RL23A_MOUSE

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"NRMT is an alpha-N-methyltransferase that methylates RCC1 andretinoblastoma protein."; Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; Nature 466:1125-1128(2010). Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT ALA-2.	20668449 [Abstract]