dbPTM

RL35_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL35_HUMAN
UniProt AC	P42766
Protein Name	60S ribosomal protein L35
Gene Name	RPL35
Organism	Homo sapiens (Human).
Sequence Length	123
Subcellular Localization
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MAKIKARDLRGKKKEELLKQLDDLKVELSQLRVAKVTGGAASKLSKIRVVRKSIARVLTVINQTQKENLRKFYKGKKYKPLDLRPKKTRAMRRRLNKHEENLKTKKQQRKERLYPLRKYAVKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Acetylation	ARDLRGKKKEELLKQ HHHCCCHHHHHHHHH	69.14	23749302
13	Ubiquitination	ARDLRGKKKEELLKQ HHHCCCHHHHHHHHH	69.14	25015289
14	Ubiquitination	RDLRGKKKEELLKQL HHCCCHHHHHHHHHH	60.96	-
19	Ubiquitination	KKKEELLKQLDDLKV HHHHHHHHHHHHHHH	62.53	23000965
19	Acetylation	KKKEELLKQLDDLKV HHHHHHHHHHHHHHH	62.53	19608861
25	2-Hydroxyisobutyrylation	LKQLDDLKVELSQLR HHHHHHHHHHHHHHH	40.43	-
25	Ubiquitination	LKQLDDLKVELSQLR HHHHHHHHHHHHHHH	40.43	23000965
25	Sumoylation	LKQLDDLKVELSQLR HHHHHHHHHHHHHHH	40.43	28112733
25	Succinylation	LKQLDDLKVELSQLR HHHHHHHHHHHHHHH	40.43	23954790
25	Acetylation	LKQLDDLKVELSQLR HHHHHHHHHHHHHHH	40.43	26822725
29	Phosphorylation	DDLKVELSQLRVAKV HHHHHHHHHHHHHHH	17.42	30266825
32	Methylation	KVELSQLRVAKVTGG HHHHHHHHHHHHHCC	20.79	-
35	Ubiquitination	LSQLRVAKVTGGAAS HHHHHHHHHHCCHHH	37.16	23000965
37	Phosphorylation	QLRVAKVTGGAASKL HHHHHHHHCCHHHHH	29.23	22985185
42	Phosphorylation	KVTGGAASKLSKIRV HHHCCHHHHHHHHHH	33.33	24670416
43	Ubiquitination	VTGGAASKLSKIRVV HHCCHHHHHHHHHHH	52.64	23000965
43	Acetylation	VTGGAASKLSKIRVV HHCCHHHHHHHHHHH	52.64	19608861
43	2-Hydroxyisobutyrylation	VTGGAASKLSKIRVV HHCCHHHHHHHHHHH	52.64	-
45	Phosphorylation	GGAASKLSKIRVVRK CCHHHHHHHHHHHHH	29.76	25159151
46	Ubiquitination	GAASKLSKIRVVRKS CHHHHHHHHHHHHHH	44.99	23000965
46	Acetylation	GAASKLSKIRVVRKS CHHHHHHHHHHHHHH	44.99	19814843
53	Phosphorylation	KIRVVRKSIARVLTV HHHHHHHHHHHHHHH	15.77	29514088
59	Phosphorylation	KSIARVLTVINQTQK HHHHHHHHHHHHHHH	19.24	29514088
64	Phosphorylation	VLTVINQTQKENLRK HHHHHHHHHHHHHHH	36.80	21712546
66	Ubiquitination	TVINQTQKENLRKFY HHHHHHHHHHHHHHH	52.54	23000965
66	2-Hydroxyisobutyrylation	TVINQTQKENLRKFY HHHHHHHHHHHHHHH	52.54	-
66	Succinylation	TVINQTQKENLRKFY HHHHHHHHHHHHHHH	52.54	23954790
66	Acetylation	TVINQTQKENLRKFY HHHHHHHHHHHHHHH	52.54	26051181
71	Ubiquitination	TQKENLRKFYKGKKY HHHHHHHHHHCCCCC	57.10	23000965
74	Ubiquitination	ENLRKFYKGKKYKPL HHHHHHHCCCCCCCC	68.34	22817900
76	Ubiquitination	LRKFYKGKKYKPLDL HHHHHCCCCCCCCCC	49.10	22817900
77	Ubiquitination	RKFYKGKKYKPLDLR HHHHCCCCCCCCCCC	68.15	29967540
78	Phosphorylation	KFYKGKKYKPLDLRP HHHCCCCCCCCCCCC	22.71	28152594
79	Ubiquitination	FYKGKKYKPLDLRPK HHCCCCCCCCCCCCH	48.24	22817900
79	Acetylation	FYKGKKYKPLDLRPK HHCCCCCCCCCCCCH	48.24	26051181
84	Methylation	KYKPLDLRPKKTRAM CCCCCCCCCHHHHHH	40.43	115492137
86	Ubiquitination	KPLDLRPKKTRAMRR CCCCCCCHHHHHHHH	61.41	32015554
86	2-Hydroxyisobutyrylation	KPLDLRPKKTRAMRR CCCCCCCHHHHHHHH	61.41	-
97	Ubiquitination	AMRRRLNKHEENLKT HHHHHHHHHHHHHHH	57.92	33845483
97	Acetylation	AMRRRLNKHEENLKT HHHHHHHHHHHHHHH	57.92	25825284
103	Ubiquitination	NKHEENLKTKKQQRK HHHHHHHHHHHHHHH	70.63	33845483
103	2-Hydroxyisobutyrylation	NKHEENLKTKKQQRK HHHHHHHHHHHHHHH	70.63	-
106	Ubiquitination	EENLKTKKQQRKERL HHHHHHHHHHHHHHH	57.82	24816145
117	Methylation	KERLYPLRKYAVKA- HHHHHHHHHHHHCC-	25.99	115492121

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 RL35_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL35_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 RL35_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBB2B_HUMAN	TUBB2B	physical	21900206
SGSM3_HUMAN	SGSM3	physical	21900206
RS8_HUMAN	RPS8	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL36_HUMAN	RPL36	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
EIFCL_HUMAN	EIF3CL	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
KPRA_HUMAN	PRPSAP1	physical	22863883
RL17_HUMAN	RPL17	physical	22863883
RS11_HUMAN	RPS11	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
SND1_HUMAN	SND1	physical	22863883
PABP1_HUMAN	PABPC1	physical	26344197
RNPS1_HUMAN	RNPS1	physical	26344197
RL10_HUMAN	RPL10	physical	26344197
RL10A_HUMAN	RPL10A	physical	26344197
RL10L_HUMAN	RPL10L	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL13_HUMAN	RPL13	physical	26344197
RL13A_HUMAN	RPL13A	physical	26344197
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL27A_HUMAN	RPL27A	physical	26344197
RL35A_HUMAN	RPL35A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL38_HUMAN	RPL38	physical	26344197
RL4_HUMAN	RPL4	physical	26344197
RL8_HUMAN	RPL8	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS2_HUMAN	RPS2	physical	26344197
RS23_HUMAN	RPS23	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RSSA_HUMAN	RPSA	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 RL35_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-19 AND LYS-43, AND MASSSPECTROMETRY.	19608861 [Abstract]