dbPTM

RL15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RL15_HUMAN
UniProt AC	P61313
Protein Name	60S ribosomal protein L15
Gene Name	RPL15
Organism	Homo sapiens (Human).
Sequence Length	204
Subcellular Localization	Membrane Lipid-anchor .
Protein Description
Protein Sequence	MGAYKYIQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRIRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSVAEERAGRHCGALRVLNSYWVGEDSTYKFFEVILIDPFHKAIRRNPDTQWITKPVHKHREMRGLTSAGRKSRGLGKGHKFHHTIGGSRRAAWRRRNTLQLHRYR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGAYKYIQE ------CCHHHHHHH	37.30	25255805
5	Ubiquitination	---MGAYKYIQELWR ---CCHHHHHHHHHH	35.03	-
5	Acetylation	---MGAYKYIQELWR ---CCHHHHHHHHHH	35.03	25825284
6	Phosphorylation	--MGAYKYIQELWRK --CCHHHHHHHHHHH	8.65	28152594
14	2-Hydroxyisobutyrylation	IQELWRKKQSDVMRF HHHHHHHCHHHHHHH	46.60	-
34	Phosphorylation	CWQYRQLSALHRAPR HHHHHHHHHHHCCCC	22.05	23401153
47	Ubiquitination	PRPTRPDKARRLGYK CCCCCCCHHHHHCCE	46.61	-
47	2-Hydroxyisobutyrylation	PRPTRPDKARRLGYK CCCCCCCHHHHHCCE	46.61	-
54	Ubiquitination	KARRLGYKAKQGYVI HHHHHCCEECCCEEE	47.51	-
54	Methylation	KARRLGYKAKQGYVI HHHHHCCEECCCEEE	47.51	23748837
56	2-Hydroxyisobutyrylation	RRLGYKAKQGYVIYR HHHCCEECCCEEEEE	39.85	-
56	Ubiquitination	RRLGYKAKQGYVIYR HHHCCEECCCEEEEE	39.85	21890473
56	Ubiquitination	RRLGYKAKQGYVIYR HHHCCEECCCEEEEE	39.85	21890473
56	Ubiquitination	RRLGYKAKQGYVIYR HHHCCEECCCEEEEE	39.85	21890473
59	Phosphorylation	GYKAKQGYVIYRIRV CCEECCCEEEEEEEE	4.91	20007894
62	Phosphorylation	AKQGYVIYRIRVRRG ECCCEEEEEEEECCC	7.02	28152594
77	Ubiquitination	GRKRPVPKGATYGKP CCCCCCCCCCCCCCC	62.50	-
80	Phosphorylation	RPVPKGATYGKPVHH CCCCCCCCCCCCCCC	41.28	28152594
81	Phosphorylation	PVPKGATYGKPVHHG CCCCCCCCCCCCCCH	23.71	28152594
83	Ubiquitination	PKGATYGKPVHHGVN CCCCCCCCCCCCHHH	33.19	21890473
83	Sumoylation	PKGATYGKPVHHGVN CCCCCCCCCCCCHHH	33.19	28112733
83	Ubiquitination	PKGATYGKPVHHGVN CCCCCCCCCCCCHHH	33.19	21890473
83	Ubiquitination	PKGATYGKPVHHGVN CCCCCCCCCCCCHHH	33.19	21890473
83	Acetylation	PKGATYGKPVHHGVN CCCCCCCCCCCCHHH	33.19	23749302
93	Ubiquitination	HHGVNQLKFARSLQS CCHHHHHHHHHHHHH	27.49	21890473
93	Ubiquitination	HHGVNQLKFARSLQS CCHHHHHHHHHHHHH	27.49	21890473
93	Ubiquitination	HHGVNQLKFARSLQS CCHHHHHHHHHHHHH	27.49	21890473
93	2-Hydroxyisobutyrylation	HHGVNQLKFARSLQS CCHHHHHHHHHHHHH	27.49	-
93	Acetylation	HHGVNQLKFARSLQS CCHHHHHHHHHHHHH	27.49	25825284
97	Phosphorylation	NQLKFARSLQSVAEE HHHHHHHHHHHHHHH	27.60	29255136
100	Phosphorylation	KFARSLQSVAEERAG HHHHHHHHHHHHHHH	28.70	23911959
105	Methylation	LQSVAEERAGRHCGA HHHHHHHHHHCCCCC	33.57	115491747
110	S-palmitoylation	EERAGRHCGALRVLN HHHHHCCCCCEEECC	3.08	21044946
118	Phosphorylation	GALRVLNSYWVGEDS CCEEECCCEECCCCC	19.06	30257219
119	Phosphorylation	ALRVLNSYWVGEDST CEEECCCEECCCCCC	11.75	28152594
125	Phosphorylation	SYWVGEDSTYKFFEV CEECCCCCCEEEEEE	29.36	30622161
126	Phosphorylation	YWVGEDSTYKFFEVI EECCCCCCEEEEEEE	42.95	30622161
127	Phosphorylation	WVGEDSTYKFFEVIL ECCCCCCEEEEEEEE	15.11	23917254
140	Sumoylation	ILIDPFHKAIRRNPD EEECHHHHHHHHCCC	45.98	-
140	Ubiquitination	ILIDPFHKAIRRNPD EEECHHHHHHHHCCC	45.98	21906983
140	Ubiquitination	ILIDPFHKAIRRNPD EEECHHHHHHHHCCC	45.98	21890473
140	Acetylation	ILIDPFHKAIRRNPD EEECHHHHHHHHCCC	45.98	26051181
153	Acetylation	PDTQWITKPVHKHRE CCCCCCCCCCHHCHH	35.59	23749302
153	Ubiquitination	PDTQWITKPVHKHRE CCCCCCCCCCHHCHH	35.59	21890473
153	Ubiquitination	PDTQWITKPVHKHRE CCCCCCCCCCHHCHH	35.59	21906983
157	Ubiquitination	WITKPVHKHREMRGL CCCCCCHHCHHHHCC	44.59	21890473
157	Ubiquitination	WITKPVHKHREMRGL CCCCCCHHCHHHHCC	44.59	21906983
162	Methylation	VHKHREMRGLTSAGR CHHCHHHHCCCCCCH	32.01	115491727
176	Ubiquitination	RKSRGLGKGHKFHHT HHHCCCCCCCCCCHH	63.99	-
179	Acetylation	RGLGKGHKFHHTIGG CCCCCCCCCCHHCCC	55.87	25825284
179	Ubiquitination	RGLGKGHKFHHTIGG CCCCCCCCCCHHCCC	55.87	21906983
179	2-Hydroxyisobutyrylation	RGLGKGHKFHHTIGG CCCCCCCCCCHHCCC	55.87	-
183	Phosphorylation	KGHKFHHTIGGSRRA CCCCCCHHCCCCHHH	16.85	20068231
187	Phosphorylation	FHHTIGGSRRAAWRR CCHHCCCCHHHHHHH	17.24	30108239
197	Phosphorylation	AAWRRRNTLQLHRYR HHHHHHCCCCCEECC	17.67	30266825
202	Methylation	RNTLQLHRYR----- HCCCCCEECC-----	37.20	115491737

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 RL15_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RL15_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 RL15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN6_HUMAN	COPS6	physical	16169070
RL18_HUMAN	RPL18	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL22_HUMAN	RPL22	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RL24_HUMAN	RPL24	physical	22939629
RL27A_HUMAN	RPL27A	physical	22939629
RL30_HUMAN	RPL30	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL7_HUMAN	RPL7	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RS16_HUMAN	RPS16	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
RS3A_HUMAN	RPS3A	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS5_HUMAN	RPS5	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RL18A_HUMAN	RPL18A	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS12_HUMAN	RPS12	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RS27A_HUMAN	RPS27A	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
RS27L_HUMAN	RPS27L	physical	22939629
VASN_HUMAN	VASN	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
AIMP1_HUMAN	AIMP1	physical	22863883
SYDC_HUMAN	DARS	physical	22863883
MCA3_HUMAN	EEF1E1	physical	22863883
SYIC_HUMAN	IARS	physical	22863883
SYQ_HUMAN	QARS	physical	22863883
RL13_HUMAN	RPL13	physical	22863883
RL21_HUMAN	RPL21	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
RL26_HUMAN	RPL26	physical	22863883
RL36_HUMAN	RPL36	physical	22863883
RL3_HUMAN	RPL3	physical	22863883
RL7A_HUMAN	RPL7A	physical	22863883
RLA0_HUMAN	RPLP0	physical	22863883
RL10A_HUMAN	RPL10A	physical	26344197
RL11_HUMAN	RPL11	physical	26344197
RL12_HUMAN	RPL12	physical	26344197
RL17_HUMAN	RPL17	physical	26344197
RL23A_HUMAN	RPL23A	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
RL9_HUMAN	RPL9	physical	26344197
RLA1_HUMAN	RPLP1	physical	26344197
RS16_HUMAN	RPS16	physical	26344197
RS18_HUMAN	RPS18	physical	26344197
RS19_HUMAN	RPS19	physical	26344197
RS27_HUMAN	RPS27	physical	26344197
RS4X_HUMAN	RPS4X	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
RS7_HUMAN	RPS7	physical	26344197
COPRS_HUMAN	COPRS	physical	28514442
F192A_HUMAN	FAM192A	physical	28514442
ICLN_HUMAN	CLNS1A	physical	28514442
ANM5_HUMAN	PRMT5	physical	28514442
DCAF1_HUMAN	VPRBP	physical	28514442
PWP1_HUMAN	PWP1	physical	28514442
KLDC3_HUMAN	KLHDC3	physical	28514442
NLE1_HUMAN	NLE1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
UBE2O_HUMAN	UBE2O	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
MY18A_HUMAN	MYO18A	physical	28514442
RIOK1_HUMAN	RIOK1	physical	28514442
MDM2_HUMAN	MDM2	physical	28514442
CUED1_HUMAN	CUEDC1	physical	28514442
TRBP2_HUMAN	TARBP2	physical	28514442
NP1L1_HUMAN	NAP1L1	physical	28514442
DICER_HUMAN	DICER1	physical	28514442
CYTSA_HUMAN	SPECC1L	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615550	Diamond-Blackfan anemia 12 (DBA12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RL15_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-83, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-97 AND SER-100,AND MASS SPECTROMETRY.	19369195 [Abstract]
"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 SER-97, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-34, 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-34 AND THR-197, AND MASSSPECTROMETRY.	19007248 [Abstract]