dbPTM

RL17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL17_HUMAN
UniProt AC	P18621
Protein Name	60S ribosomal protein L17
Gene Name	RPL17
Organism	Homo sapiens (Human).
Sequence Length	184
Subcellular Localization
Protein Description	Component of the large ribosomal subunit..
Protein Sequence	MVRYSLDPENPTKSCKSRGSNLRVHFKNTRETAQAIKGMHIRKATKYLKDVTLQKQCVPFRRYNGGVGRCAQAKQWGWTQGRWPKKSAEFLLHMLKNAESNAELKGLDVDSLVIEHIQVNKAPKMRRRTYRAHGRINPYMSSPCHIEMILTEKEQIVPKPEEEVAQKKKISQKKLKKQKLMARE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MVRYSLDPENP ----CCCEECCCCCC	11.37	30266825
5	Phosphorylation	---MVRYSLDPENPT ---CCCEECCCCCCC	18.74	30266825
12	Phosphorylation	SLDPENPTKSCKSRG ECCCCCCCCCHHCCC	47.36	24732914
13	Ubiquitination	LDPENPTKSCKSRGS CCCCCCCCCHHCCCC	55.93	20639865
13	Malonylation	LDPENPTKSCKSRGS CCCCCCCCCHHCCCC	55.93	26320211
13	Acetylation	LDPENPTKSCKSRGS CCCCCCCCCHHCCCC	55.93	23236377
14	Phosphorylation	DPENPTKSCKSRGSN CCCCCCCCHHCCCCC	29.29	21712546
16	Ubiquitination	ENPTKSCKSRGSNLR CCCCCCHHCCCCCEE	50.72	-
27	Ubiquitination	SNLRVHFKNTRETAQ CCEEEEEECHHHHHH	42.40	-
27	Acetylation	SNLRVHFKNTRETAQ CCEEEEEECHHHHHH	42.40	25953088
34	Ubiquitination	KNTRETAQAIKGMHI ECHHHHHHHHHHHHH	51.55	21890473
37	Methylation	RETAQAIKGMHIRKA HHHHHHHHHHHHHHH	53.87	11923917
37	Ubiquitination	RETAQAIKGMHIRKA HHHHHHHHHHHHHHH	53.87	-
37	Sumoylation	RETAQAIKGMHIRKA HHHHHHHHHHHHHHH	53.87	-
37	Acetylation	RETAQAIKGMHIRKA HHHHHHHHHHHHHHH	53.87	26051181
37	Sumoylation	RETAQAIKGMHIRKA HHHHHHHHHHHHHHH	53.87	-
40	Ubiquitination	AQAIKGMHIRKATKY HHHHHHHHHHHHHHH	25.93	21890473
46	Acetylation	MHIRKATKYLKDVTL HHHHHHHHHHCCCCC	54.14	25953088
47	Phosphorylation	HIRKATKYLKDVTLQ HHHHHHHHHCCCCCC	18.03	28152594
49	Malonylation	RKATKYLKDVTLQKQ HHHHHHHCCCCCCCC	47.24	26320211
49	Acetylation	RKATKYLKDVTLQKQ HHHHHHHCCCCCCCC	47.24	23954790
49	Ubiquitination	RKATKYLKDVTLQKQ HHHHHHHCCCCCCCC	47.24	21890473
49	Ubiquitination	RKATKYLKDVTLQKQ HHHHHHHCCCCCCCC	47.24	21890473
52	Phosphorylation	TKYLKDVTLQKQCVP HHHHCCCCCCCCCCC	33.34	28152594
55	Ubiquitination	LKDVTLQKQCVPFRR HCCCCCCCCCCCCCC	49.10	21890473
55	Ubiquitination	LKDVTLQKQCVPFRR HCCCCCCCCCCCCCC	49.10	21890473
55	Acetylation	LKDVTLQKQCVPFRR HCCCCCCCCCCCCCC	49.10	21466224
57	Glutathionylation	DVTLQKQCVPFRRYN CCCCCCCCCCCCCCC	5.60	22555962
59	Ubiquitination	TLQKQCVPFRRYNGG CCCCCCCCCCCCCCC	25.34	21890473
69	Methylation	RYNGGVGRCAQAKQW CCCCCCCHHHHHHHH	15.36	115491757
71	Ubiquitination	NGGVGRCAQAKQWGW CCCCCHHHHHHHHCC	15.82	21890473
74	Ubiquitination	VGRCAQAKQWGWTQG CCHHHHHHHHCCCCC	34.21	21890473
74	Acetylation	VGRCAQAKQWGWTQG CCHHHHHHHHCCCCC	34.21	26051181
74	Ubiquitination	VGRCAQAKQWGWTQG CCHHHHHHHHCCCCC	34.21	21890473
81	Ubiquitination	KQWGWTQGRWPKKSA HHHCCCCCCCCHHHH	26.67	21890473
85	Acetylation	WTQGRWPKKSAEFLL CCCCCCCHHHHHHHH	53.02	18525475
86	Ubiquitination	TQGRWPKKSAEFLLH CCCCCCHHHHHHHHH	51.31	21890473
86	Sumoylation	TQGRWPKKSAEFLLH CCCCCCHHHHHHHHH	51.31	-
86	Acetylation	TQGRWPKKSAEFLLH CCCCCCHHHHHHHHH	51.31	26051181
86	Ubiquitination	TQGRWPKKSAEFLLH CCCCCCHHHHHHHHH	51.31	21890473
86	Sumoylation	TQGRWPKKSAEFLLH CCCCCCHHHHHHHHH	51.31	-
87	Phosphorylation	QGRWPKKSAEFLLHM CCCCCHHHHHHHHHH	38.87	28450419
90	Ubiquitination	WPKKSAEFLLHMLKN CCHHHHHHHHHHHHH	9.83	21890473
94	Sulfoxidation	SAEFLLHMLKNAESN HHHHHHHHHHHCHHC	6.02	21406390
96	Acetylation	EFLLHMLKNAESNAE HHHHHHHHHCHHCHH	46.68	23236377
96	Ubiquitination	EFLLHMLKNAESNAE HHHHHHHHHCHHCHH	46.68	21890473
96	Ubiquitination	EFLLHMLKNAESNAE HHHHHHHHHCHHCHH	46.68	21890473
100	Phosphorylation	HMLKNAESNAELKGL HHHHHCHHCHHHCCC	38.64	29514088
105	Ubiquitination	AESNAELKGLDVDSL CHHCHHHCCCCHHHH	49.27	21890473
105	Ubiquitination	AESNAELKGLDVDSL CHHCHHHCCCCHHHH	49.27	21890473
106	Ubiquitination	ESNAELKGLDVDSLV HHCHHHCCCCHHHHH	39.47	21890473
111	Phosphorylation	LKGLDVDSLVIEHIQ HCCCCHHHHHEEEEE	25.12	29514088
121	Ubiquitination	IEHIQVNKAPKMRRR EEEEECCCCHHHCCH	68.18	21890473
121	Ubiquitination	IEHIQVNKAPKMRRR EEEEECCCCHHHCCH	68.18	21890473
121	Acetylation	IEHIQVNKAPKMRRR EEEEECCCCHHHCCH	68.18	25953088
129	Phosphorylation	APKMRRRTYRAHGRI CHHHCCHHHHHCCCC	18.62	-
139	Phosphorylation	AHGRINPYMSSPCHI HCCCCCCCCCCCCEE	12.73	30266825
141	Phosphorylation	GRINPYMSSPCHIEM CCCCCCCCCCCEEEE	25.86	30266825
142	Phosphorylation	RINPYMSSPCHIEMI CCCCCCCCCCEEEEE	18.28	22167270
144	Glutathionylation	NPYMSSPCHIEMILT CCCCCCCCEEEEEEE	5.65	22555962
151	Phosphorylation	CHIEMILTEKEQIVP CEEEEEEECHHHCCC	33.80	23927012
153	Acetylation	IEMILTEKEQIVPKP EEEEEECHHHCCCCC	50.08	26051181
159	Ubiquitination	EKEQIVPKPEEEVAQ CHHHCCCCCHHHHHH	54.92	-
159	Sumoylation	EKEQIVPKPEEEVAQ CHHHCCCCCHHHHHH	54.92	-
159	Sumoylation	EKEQIVPKPEEEVAQ CHHHCCCCCHHHHHH	54.92	-
159	Acetylation	EKEQIVPKPEEEVAQ CHHHCCCCCHHHHHH	54.92	26051181
167	Sumoylation	PEEEVAQKKKISQKK CHHHHHHHHCCCHHH	46.42	-
167	Succinylation	PEEEVAQKKKISQKK CHHHHHHHHCCCHHH	46.42	23954790
167	Acetylation	PEEEVAQKKKISQKK CHHHHHHHHCCCHHH	46.42	23236377
167	Ubiquitination	PEEEVAQKKKISQKK CHHHHHHHHCCCHHH	46.42	-
171	Phosphorylation	VAQKKKISQKKLKKQ HHHHHCCCHHHHHHH	44.84	-
179	Acetylation	QKKLKKQKLMARE-- HHHHHHHHHHHCC--	49.46	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
Oops, there are no upstream regulatory protein records of RL17_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL17_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 RL17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL21_HUMAN	RPL21	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RLA0_HUMAN	RPLP0	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS25_HUMAN	RPS25	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
RL38_HUMAN	RPL38	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
SYK_HUMAN	KARS	physical	22863883
SAHH3_HUMAN	AHCYL2	physical	26344197
RRF2M_HUMAN	GFM2	physical	26344197
RT07_HUMAN	MRPS7	physical	26344197
RS15_HUMAN	RPS15	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS6_HUMAN	RPS6	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
RL40_HUMAN	UBA52	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 RL17_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASSSPECTROMETRY.	18691976 [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 SER-5, AND MASSSPECTROMETRY.	19007248 [Abstract]