dbPTM

RL36_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL36_HUMAN
UniProt AC	Q9Y3U8
Protein Name	60S ribosomal protein L36
Gene Name	RPL36
Organism	Homo sapiens (Human).
Sequence Length	105
Subcellular Localization	Cytoplasm, cytosol . Cytoplasm . Detected on cytosolic polysomes (PubMed:25957688).
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MALRYPMAVGLNKGHKVTKNVSKPRHSRRRGRLTKHTKFVRDMIREVCGFAPYERRAMELLKVSKDKRALKFIKKRVGTHIRAKRKREELSNVLAAMRKAAAKKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Methylation	----MALRYPMAVGL ----CCCCCCCEECC	24.78	115492161
5	Nitration	---MALRYPMAVGLN ---CCCCCCCEECCC	9.75	-
7	Sulfoxidation	-MALRYPMAVGLNKG -CCCCCCCEECCCCC	3.32	21406390
13	Acetylation	PMAVGLNKGHKVTKN CCEECCCCCCCCCCC	68.39	25953088
13	2-Hydroxyisobutyrylation	PMAVGLNKGHKVTKN CCEECCCCCCCCCCC	68.39	-
13	Ubiquitination	PMAVGLNKGHKVTKN CCEECCCCCCCCCCC	68.39	23000965
16	Ubiquitination	VGLNKGHKVTKNVSK ECCCCCCCCCCCCCC	61.34	23000965
18	Phosphorylation	LNKGHKVTKNVSKPR CCCCCCCCCCCCCCC	23.00	22817900
19	Acetylation	NKGHKVTKNVSKPRH CCCCCCCCCCCCCCH	59.34	26051181
19	Ubiquitination	NKGHKVTKNVSKPRH CCCCCCCCCCCCCCH	59.34	23000965
23	Acetylation	KVTKNVSKPRHSRRR CCCCCCCCCCHHHHC	41.61	26051181
27	Phosphorylation	NVSKPRHSRRRGRLT CCCCCCHHHHCCCCC	28.85	-
35	Ubiquitination	RRRGRLTKHTKFVRD HHCCCCCHHHHHHHH	54.60	24816145
38	Acetylation	GRLTKHTKFVRDMIR CCCCHHHHHHHHHHH	41.40	26051181
38	Sumoylation	GRLTKHTKFVRDMIR CCCCHHHHHHHHHHH	41.40	-
48	S-palmitoylation	RDMIREVCGFAPYER HHHHHHHHCCCCHHH	2.96	29575903
48	Glutathionylation	RDMIREVCGFAPYER HHHHHHHHCCCCHHH	2.96	22555962
53	Phosphorylation	EVCGFAPYERRAMEL HHHCCCCHHHHHHHH	20.73	28152594
62	Acetylation	RRAMELLKVSKDKRA HHHHHHHHHCCCHHH	58.02	19608861
62	2-Hydroxyisobutyrylation	RRAMELLKVSKDKRA HHHHHHHHHCCCHHH	58.02	-
62	Malonylation	RRAMELLKVSKDKRA HHHHHHHHHCCCHHH	58.02	26320211
62	Ubiquitination	RRAMELLKVSKDKRA HHHHHHHHHCCCHHH	58.02	23000965
65	Ubiquitination	MELLKVSKDKRALKF HHHHHHCCCHHHHHH	70.97	23000965
67	Ubiquitination	LLKVSKDKRALKFIK HHHHCCCHHHHHHHH	43.22	23000965
71	Ubiquitination	SKDKRALKFIKKRVG CCCHHHHHHHHHHHH	44.02	27667366
71	Acetylation	SKDKRALKFIKKRVG CCCHHHHHHHHHHHH	44.02	26051181
79	Phosphorylation	FIKKRVGTHIRAKRK HHHHHHHHHHHHHHH	15.98	21406692
86	Ubiquitination	THIRAKRKREELSNV HHHHHHHHHHHHHHH	64.55	24816145
86	Acetylation	THIRAKRKREELSNV HHHHHHHHHHHHHHH	64.55	26051181
91	Phosphorylation	KRKREELSNVLAAMR HHHHHHHHHHHHHHH	28.33	21712546
97	Sulfoxidation	LSNVLAAMRKAAAKK HHHHHHHHHHHHHCC	3.62	21406390

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 RL36_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL36_HUMAN !!

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 RL36_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RL4_HUMAN	RPL4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS15_HUMAN	RPS15	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
AIMP1_HUMAN	AIMP1	physical	22863883
SYK_HUMAN	KARS	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL17_HUMAN	RPL17	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
IF6_HUMAN	EIF6	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL28_HUMAN	RPL28	physical	26344197
RL3_HUMAN	RPL3	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL3L_HUMAN	RPL3L	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RL7_HUMAN	RPL7	physical	26344197
RL7A_HUMAN	RPL7A	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15A_HUMAN	RPS15A	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS20_HUMAN	RPS20	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
RL40_HUMAN	UBA52	physical	26344197
WDR12_HUMAN	WDR12	physical	26344197

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.

Regulatory Network of RL36_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND MASS SPECTROMETRY.	19608861 [Abstract]