dbPTM

RL26_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL26_HUMAN
UniProt AC	P61254
Protein Name	60S ribosomal protein L26
Gene Name	RPL26
Organism	Homo sapiens (Human).
Sequence Length	145
Subcellular Localization
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MKFNPFVTSDRSKNRKRHFNAPSHIRRKIMSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEETIEKMQE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Sulfoxidation	-------MKFNPFVT -------CCCCCCCC	11.45	28183972
2	Acetylation	------MKFNPFVTS ------CCCCCCCCC	54.57	133641
2	Methylation	------MKFNPFVTS ------CCCCCCCCC	54.57	133641
2	Sumoylation	------MKFNPFVTS ------CCCCCCCCC	54.57	-
2	Sumoylation	------MKFNPFVTS ------CCCCCCCCC	54.57	-
2	Ubiquitination	------MKFNPFVTS ------CCCCCCCCC	54.57	23000965
8	Phosphorylation	MKFNPFVTSDRSKNR CCCCCCCCCCCCCCC	25.86	21815630
9	Phosphorylation	KFNPFVTSDRSKNRK CCCCCCCCCCCCCCC	26.23	21815630
11	Methylation	NPFVTSDRSKNRKRH CCCCCCCCCCCCCCC	49.66	-
12	Phosphorylation	PFVTSDRSKNRKRHF CCCCCCCCCCCCCCC	38.99	25159151
13	Acetylation	FVTSDRSKNRKRHFN CCCCCCCCCCCCCCC	62.76	20167786
16	Acetylation	SDRSKNRKRHFNAPS CCCCCCCCCCCCCCH	60.67	7935065
17	Methylation	DRSKNRKRHFNAPSH CCCCCCCCCCCCCHH	36.07	115491925
23	Phosphorylation	KRHFNAPSHIRRKIM CCCCCCCHHHHHHHH	29.18	29214152
26	Methylation	FNAPSHIRRKIMSSP CCCCHHHHHHHHCCC	28.54	115491917
28	Ubiquitination	APSHIRRKIMSSPLS CCHHHHHHHHCCCCC	32.67	33845483
30	Sulfoxidation	SHIRRKIMSSPLSKE HHHHHHHHCCCCCHH	3.49	30846556
31	Phosphorylation	HIRRKIMSSPLSKEL HHHHHHHCCCCCHHH	32.07	23911959
32	Phosphorylation	IRRKIMSSPLSKELR HHHHHHCCCCCHHHH	16.69	25159151
35	Phosphorylation	KIMSSPLSKELRQKY HHHCCCCCHHHHHHH	27.71	30206219
36	Acetylation	IMSSPLSKELRQKYN HHCCCCCHHHHHHHC	69.33	26051181
36	2-Hydroxyisobutyrylation	IMSSPLSKELRQKYN HHCCCCCHHHHHHHC	69.33	-
36	Ubiquitination	IMSSPLSKELRQKYN HHCCCCCHHHHHHHC	69.33	23000965
41	Ubiquitination	LSKELRQKYNVRSMP CCHHHHHHHCCCCCC	32.15	23000965
46	Phosphorylation	RQKYNVRSMPIRKDD HHHHCCCCCCCCCCC	25.32	29214152
51	Acetylation	VRSMPIRKDDEVQVV CCCCCCCCCCCEEEE	70.96	23236377
51	Ubiquitination	VRSMPIRKDDEVQVV CCCCCCCCCCCEEEE	70.96	21906983
59	Methylation	DDEVQVVRGHYKGQQ CCCEEEEECEECCCC	27.58	-
63	Ubiquitination	QVVRGHYKGQQIGKV EEEECEECCCCCCCE	44.56	23000965
63	Acetylation	QVVRGHYKGQQIGKV EEEECEECCCCCCCE	44.56	26051181
63	Succinylation	QVVRGHYKGQQIGKV EEEECEECCCCCCCE	44.56	23954790
69	Acetylation	YKGQQIGKVVQVYRK ECCCCCCCEEEEEEE	40.64	23236377
69	2-Hydroxyisobutyrylation	YKGQQIGKVVQVYRK ECCCCCCCEEEEEEE	40.64	-
69	Malonylation	YKGQQIGKVVQVYRK ECCCCCCCEEEEEEE	40.64	26320211
69	Ubiquitination	YKGQQIGKVVQVYRK ECCCCCCCEEEEEEE	40.64	23000965
76	Ubiquitination	KVVQVYRKKYVIYIE CEEEEEEECEEEEEE	30.67	-
76	Acetylation	KVVQVYRKKYVIYIE CEEEEEEECEEEEEE	30.67	25953088
77	Acetylation	VVQVYRKKYVIYIER EEEEEEECEEEEEEE	35.43	25825284
77	2-Hydroxyisobutyrylation	VVQVYRKKYVIYIER EEEEEEECEEEEEEE	35.43	-
77	Ubiquitination	VVQVYRKKYVIYIER EEEEEEECEEEEEEE	35.43	33845483
84	Methylation	KYVIYIERVQREKAN CEEEEEEEEHHHHCC	21.95	-
89	Acetylation	IERVQREKANGTTVH EEEEHHHHCCCCEEE	49.71	26051181
89	Ubiquitination	IERVQREKANGTTVH EEEEHHHHCCCCEEE	49.71	33845483
103	Acetylation	HVGIHPSKVVITRLK EEEECHHHEEEEEEE	45.00	26051181
103	Ubiquitination	HVGIHPSKVVITRLK EEEECHHHEEEEEEE	45.00	23000965
103	Methylation	HVGIHPSKVVITRLK EEEECHHHEEEEEEE	45.00	-
110	Acetylation	KVVITRLKLDKDRKK HEEEEEEECCHHHHH	51.88	25953088
113	Ubiquitination	ITRLKLDKDRKKILE EEEEECCHHHHHHHH	70.62	-
113	Acetylation	ITRLKLDKDRKKILE EEEEECCHHHHHHHH	70.62	26051181
134	Ubiquitination	QVGKEKGKYKEETIE HHHHHHCCCCHHHHH	65.30	29967540
134	Acetylation	QVGKEKGKYKEETIE HHHHHHCCCCHHHHH	65.30	23749302
135	Phosphorylation	VGKEKGKYKEETIEK HHHHHCCCCHHHHHH	32.09	28152594
136	Sumoylation	GKEKGKYKEETIEKM HHHHCCCCHHHHHHH	53.19	28112733
136	Ubiquitination	GKEKGKYKEETIEKM HHHHCCCCHHHHHHH	53.19	24816145
136	Sumoylation	GKEKGKYKEETIEKM HHHHCCCCHHHHHHH	53.19	-
136	Acetylation	GKEKGKYKEETIEKM HHHHCCCCHHHHHHH	53.19	26051181
139	Phosphorylation	KGKYKEETIEKMQE- HCCCCHHHHHHHHC-	35.21	25159151
142	2-Hydroxyisobutyrylation	YKEETIEKMQE---- CCHHHHHHHHC----	41.87	-
142	Ubiquitination	YKEETIEKMQE---- CCHHHHHHHHC----	41.87	21906983
142	Acetylation	YKEETIEKMQE---- CCHHHHHHHHC----	41.87	25953088

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
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:18951086

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL26_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 RL26_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDM2_HUMAN	MDM2	physical	18951086
MDM2_HUMAN	MDM2	physical	20542919
P53_HUMAN	TP53	physical	20542919
RL17_HUMAN	RPL17	physical	22863883
RL35_HUMAN	RPL35	physical	22863883
RL36_HUMAN	RPL36	physical	22863883
RL14_HUMAN	RPL14	physical	26344197
RL15_HUMAN	RPL15	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL27_HUMAN	RPL27	physical	26344197
RL30_HUMAN	RPL30	physical	26344197
RL34_HUMAN	RPL34	physical	26344197
RL35_HUMAN	RPL35	physical	26344197
RL36_HUMAN	RPL36	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL5_HUMAN	RPL5	physical	26344197
RL6_HUMAN	RPL6	physical	26344197
RLA0_HUMAN	RPLP0	physical	26344197
RLA2_HUMAN	RPLP2	physical	26344197
RS11_HUMAN	RPS11	physical	26344197
RS14_HUMAN	RPS14	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS25_HUMAN	RPS25	physical	26344197
RS26_HUMAN	RPS26	physical	26344197
RS29_HUMAN	RPS29	physical	26344197
RS3A_HUMAN	RPS3A	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
RS8_HUMAN	RPS8	physical	26344197
RS9_HUMAN	RPS9	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614900	Diamond-Blackfan anemia 11 (DBA11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RL26_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-77, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-139, AND MASSSPECTROMETRY.	19007248 [Abstract]