dbPTM

RM47_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RM47_HUMAN
UniProt AC	Q9HD33
Protein Name	39S ribosomal protein L47, mitochondrial
Gene Name	MRPL47
Organism	Homo sapiens (Human).
Sequence Length	250
Subcellular Localization	Mitochondrion .
Protein Description
Protein Sequence	MAAAGLALLCRRVSSALKSSRSLITPQVPACTGFFLSLLPKSTPNVTSFHQYRLLHTTLSRKGLEEFFDDPKNWGQEKVKSGAAWTCQQLRNKSNEDLHKLWYVLLKERNMLLTLEQEAKRQRLPMPSPERLDKVVDSMDALDKVVQEREDALRLLQTGQERARPGAWRRDIFGRIIWHKFKQWVIPWHLNKRYNRKRFFALPYVDHFLRLEREKRARIKARKENLERKKAKILLKKFPHLAEAQKSSLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Ubiquitination	LKSSRSLITPQVPAC HHHCCCCCCCCCCCC	5.79	24816145
34	Acetylation	QVPACTGFFLSLLPK CCCCCCHHHHHCCCC	2.76	19608861
43	Phosphorylation	LSLLPKSTPNVTSFH HHCCCCCCCCCCCHH	25.63	-
47	Phosphorylation	PKSTPNVTSFHQYRL CCCCCCCCCHHHHHH	32.11	-
62	Ubiquitination	LHTTLSRKGLEEFFD HHHHHCHHCHHHHHC	65.55	29967540
72	Succinylation	EEFFDDPKNWGQEKV HHHHCCCCCCCCHHH	72.78	23954790
72	Ubiquitination	EEFFDDPKNWGQEKV HHHHCCCCCCCCHHH	72.78	29967540
78	Ubiquitination	PKNWGQEKVKSGAAW CCCCCCHHHHHCHHH	47.26	29967540
80	Ubiquitination	NWGQEKVKSGAAWTC CCCCHHHHHCHHHHH	54.99	29967540
114	Phosphorylation	KERNMLLTLEQEAKR HHHCCHHHHHHHHHH	25.04	30622161
120	Ubiquitination	LTLEQEAKRQRLPMP HHHHHHHHHCCCCCC	48.59	24816145
127	Ubiquitination	KRQRLPMPSPERLDK HHCCCCCCCHHHHHH	44.80	29967540
128	Phosphorylation	RQRLPMPSPERLDKV HCCCCCCCHHHHHHH	32.89	26471730
134	Ubiquitination	PSPERLDKVVDSMDA CCHHHHHHHHHHHHH	49.07	24816145
138	Phosphorylation	RLDKVVDSMDALDKV HHHHHHHHHHHHHHH	13.62	20068231
144	Malonylation	DSMDALDKVVQERED HHHHHHHHHHHHHHH	45.19	26320211
144	Acetylation	DSMDALDKVVQERED HHHHHHHHHHHHHHH	45.19	19608861
237	Ubiquitination	KAKILLKKFPHLAEA HHHHHHHHCHHHHHH	65.19	29967540

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 RM47_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RM47_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 RM47_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RM50_HUMAN	MRPL50	physical	22939629
TSR1_HUMAN	TSR1	physical	22939629
RM12_HUMAN	MRPL12	physical	26186194
RM46_HUMAN	MRPL46	physical	26186194
RM09_HUMAN	MRPL9	physical	26186194
RL26L_HUMAN	RPL26L1	physical	26186194
RM32_HUMAN	MRPL32	physical	26186194
RM11_HUMAN	MRPL11	physical	26186194
RM48_HUMAN	MRPL48	physical	26186194
RM40_HUMAN	MRPL40	physical	26186194
RM03_HUMAN	MRPL3	physical	26186194
RM01_HUMAN	MRPL1	physical	26186194
RM23_HUMAN	MRPL23	physical	26186194
RM41_HUMAN	MRPL41	physical	26186194
RM22_HUMAN	MRPL22	physical	26186194
RM10_HUMAN	MRPL10	physical	26186194
RM24_HUMAN	MRPL24	physical	26186194
RM49_HUMAN	MRPL49	physical	26186194
RM44_HUMAN	MRPL44	physical	26186194
RM50_HUMAN	MRPL50	physical	26186194
RM38_HUMAN	MRPL38	physical	26186194
RM20_HUMAN	MRPL20	physical	26186194
GRM1A_HUMAN	GRAMD1A	physical	26186194
RM27_HUMAN	MRPL27	physical	26186194
RM55_HUMAN	MRPL55	physical	26186194
MASU1_HUMAN	MALSU1	physical	26186194
RM16_HUMAN	MRPL16	physical	26186194
RM19_HUMAN	MRPL19	physical	26186194
RM15_HUMAN	MRPL15	physical	26186194
ICT1_HUMAN	ICT1	physical	26186194
RM02_HUMAN	MRPL2	physical	26186194
RM21_HUMAN	MRPL21	physical	26186194
RM13_HUMAN	MRPL13	physical	26186194
RM43_HUMAN	MRPL43	physical	26186194
RM17_HUMAN	MRPL17	physical	26186194
RM33_HUMAN	MRPL33	physical	26186194
G45IP_HUMAN	GADD45GIP1	physical	26186194
RM35_HUMAN	MRPL35	physical	26186194
RM30_HUMAN	MRPL30	physical	26186194
RM18_HUMAN	MRPL18	physical	26186194
RM14_HUMAN	MRPL14	physical	26186194
RM42_HUMAN	MRPL42	physical	26186194
MRM3_HUMAN	RNMTL1	physical	26186194
RM51_HUMAN	MRPL51	physical	26186194
RT63_HUMAN	MRPL57	physical	26186194
RM34_HUMAN	MRPL34	physical	26186194
ICT1_HUMAN	ICT1	physical	26344197
RM13_HUMAN	MRPL13	physical	26344197
RM17_HUMAN	MRPL17	physical	26344197
RM24_HUMAN	MRPL24	physical	26344197
RM38_HUMAN	MRPL38	physical	26344197
G45IP_HUMAN	GADD45GIP1	physical	28514442
RM41_HUMAN	MRPL41	physical	28514442
RM24_HUMAN	MRPL24	physical	28514442
RM49_HUMAN	MRPL49	physical	28514442
RM13_HUMAN	MRPL13	physical	28514442
RM32_HUMAN	MRPL32	physical	28514442
RM51_HUMAN	MRPL51	physical	28514442
RM55_HUMAN	MRPL55	physical	28514442
RM22_HUMAN	MRPL22	physical	28514442
RM11_HUMAN	MRPL11	physical	28514442
RM01_HUMAN	MRPL1	physical	28514442
RM30_HUMAN	MRPL30	physical	28514442
RM27_HUMAN	MRPL27	physical	28514442
RM02_HUMAN	MRPL2	physical	28514442
RM40_HUMAN	MRPL40	physical	28514442
RM15_HUMAN	MRPL15	physical	28514442
RM46_HUMAN	MRPL46	physical	28514442
RM44_HUMAN	MRPL44	physical	28514442
RM19_HUMAN	MRPL19	physical	28514442
RM23_HUMAN	MRPL23	physical	28514442
RM48_HUMAN	MRPL48	physical	28514442
RM20_HUMAN	MRPL20	physical	28514442
RM09_HUMAN	MRPL9	physical	28514442
RM17_HUMAN	MRPL17	physical	28514442
RM16_HUMAN	MRPL16	physical	28514442
RM18_HUMAN	MRPL18	physical	28514442
RT63_HUMAN	MRPL57	physical	28514442
RM38_HUMAN	MRPL38	physical	28514442
RM03_HUMAN	MRPL3	physical	28514442
ICT1_HUMAN	ICT1	physical	28514442
RM33_HUMAN	MRPL33	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
MASU1_HUMAN	MALSU1	physical	28514442
RM43_HUMAN	MRPL43	physical	28514442
MRM3_HUMAN	RNMTL1	physical	28514442
RM14_HUMAN	MRPL14	physical	28514442

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 RM47_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-144, AND MASS SPECTROMETRY.	19608861 [Abstract]