RS27L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RS27L_HUMAN
• UniProt AC: Q71UM5
• Protein Name: 40S ribosomal protein S27-like
• Gene Name: RPS27L {ECO:0000312|HGNC:HGNC:18476}
• Organism: Homo sapiens (Human).
• Sequence Length: 84
• Protein Sequence: MPLARDLLHPSLEEEKKKHKKKRLVQSPNSYFMDVKCPGCYKITTVFSHAQTVVLCVGCSTVLCQPTGGKARLTEGCSFRRKQH

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
11	Phosphorylation	ARDLLHPSLEEEKKK HHHHCCCCHHHHHHH	37.35	30266825
16	Ubiquitination	HPSLEEEKKKHKKKR CCCHHHHHHHHHHHH	71.10	21906983
17	Ubiquitination	PSLEEEKKKHKKKRL CCHHHHHHHHHHHHH	64.49	2190698
20	Ubiquitination	EEEKKKHKKKRLVQS HHHHHHHHHHHHCCC	69.72	24816145
22	Sumoylation	EKKKHKKKRLVQSPN HHHHHHHHHHCCCCC	56.63	-
22	Sumoylation	EKKKHKKKRLVQSPN HHHHHHHHHHCCCCC	56.63	-
27	Phosphorylation	KKKRLVQSPNSYFMD HHHHHCCCCCCCCCC	20.69	29255136
30	Phosphorylation	RLVQSPNSYFMDVKC HHCCCCCCCCCCCCC	24.11	21945579
31	Phosphorylation	LVQSPNSYFMDVKCP HCCCCCCCCCCCCCC	15.01	29255136
31	Nitration	LVQSPNSYFMDVKCP HCCCCCCCCCCCCCC	15.01	-
36	Ubiquitination	NSYFMDVKCPGCYKI CCCCCCCCCCCEEEE	30.37	16196087
70	Ubiquitination	LCQPTGGKARLTEGC EECCCCCCEECCCCC	31.51	-
72	Methylation	QPTGGKARLTEGCSF CCCCCCEECCCCCCC	45.70	-
74	Phosphorylation	TGGKARLTEGCSFRR CCCCEECCCCCCCCC	25.44	24702127
77	Glutathionylation	KARLTEGCSFRRKQH CEECCCCCCCCCCCC	2.57	22555962
77	Carbamidation	KARLTEGCSFRRKQH CEECCCCCCCCCCCC	2.57	17322306
77	S-palmitoylation	KARLTEGCSFRRKQH CEECCCCCCCCCCCC	2.57	29575903
78	Phosphorylation	ARLTEGCSFRRKQH- EECCCCCCCCCCCC-	32.42	29255136

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
27	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RS27L_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RS27L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	21170087
RS3_HUMAN	RPS3	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
SMD3_HUMAN	SNRPD3	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
G3BP1_HUMAN	G3BP1	physical	22863883
RACK1_HUMAN	GNB2L1	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
PA2G4_HUMAN	PA2G4	physical	22863883
RANB9_HUMAN	RANBP9	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
RS15A_HUMAN	RPS15A	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
HNRPQ_HUMAN	SYNCRIP	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.
PubMed: 19690332