dbPTM

RRP8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRP8_HUMAN
UniProt AC	O43159
Protein Name	Ribosomal RNA-processing protein 8
Gene Name	RRP8
Organism	Homo sapiens (Human).
Sequence Length	456
Subcellular Localization	Nucleus, nucleolus . Localizes at rDNA locus.
Protein Description	Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown..
Protein Sequence	MFEEPEWAEAAPVAAGLGPVISRPPPAASSQNKGSKRRQLLATLRALEAASLSQHPPSLCISDSEEEEEERKKKCPKKASFASASAEVGKKGKKKCQKQGPPCSDSEEEVERKKKCHKQALVGSDSAEDEKRKRKCQKHAPINSAQHLDNVDQTGPKAWKGSTTNDPPKQSPGSTSPKPPHTLSRKQWRNRQKNKRRCKNKFQPPQVPDQAPAEAPTEKTEVSPVPRTDSHEARAGALRARMAQRLDGARFRYLNEQLYSGPSSAAQRLFQEDPEAFLLYHRGFQSQVKKWPLQPVDRIARDLRQRPASLVVADFGCGDCRLASSIRNPVHCFDLASLDPRVTVCDMAQVPLEDESVDVAVFCLSLMGTNIRDFLEEANRVLKPGGLLKVAEVSSRFEDVRTFLRAVTKLGFKIVSKDLTNSHFFLFDFQKTGPPLVGPKAQLSGLQLQPCLYKRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Phosphorylation	KRRQLLATLRALEAA HHHHHHHHHHHHHHH	19.42	20068231
51	Phosphorylation	LRALEAASLSQHPPS HHHHHHHHHHCCCCC	35.28	29255136
53	Phosphorylation	ALEAASLSQHPPSLC HHHHHHHHCCCCCCC	24.77	25463755
58	Phosphorylation	SLSQHPPSLCISDSE HHHCCCCCCCCCCCH	40.08	30266825
62	Phosphorylation	HPPSLCISDSEEEEE CCCCCCCCCCHHHHH	33.80	29255136
64	Phosphorylation	PSLCISDSEEEEEER CCCCCCCCHHHHHHH	39.87	29255136
78	Acetylation	RKKKCPKKASFASAS HHHHCCHHHHHHHHH	34.11	26051181
80	Phosphorylation	KKCPKKASFASASAE HHCCHHHHHHHHHHH	30.17	25159151
83	Phosphorylation	PKKASFASASAEVGK CHHHHHHHHHHHHHH	22.27	20873877
85	Phosphorylation	KASFASASAEVGKKG HHHHHHHHHHHHHHC	23.59	28188228
90	Acetylation	SASAEVGKKGKKKCQ HHHHHHHHHCHHHHH	64.63	26051181
90	2-Hydroxyisobutyrylation	SASAEVGKKGKKKCQ HHHHHHHHHCHHHHH	64.63	-
104	Phosphorylation	QKQGPPCSDSEEEVE HHCCCCCCCCHHHHH	50.36	29255136
106	Phosphorylation	QGPPCSDSEEEVERK CCCCCCCCHHHHHHH	30.52	29255136
124	Phosphorylation	HKQALVGSDSAEDEK HHHHHCCCCCHHHHH	22.40	29255136
126	Phosphorylation	QALVGSDSAEDEKRK HHHCCCCCHHHHHHH	34.94	29255136
131	Acetylation	SDSAEDEKRKRKCQK CCCHHHHHHHHHHHH	75.45	26051181
138	Acetylation	KRKRKCQKHAPINSA HHHHHHHHHCCCCHH	51.72	26051181
144	Phosphorylation	QKHAPINSAQHLDNV HHHCCCCHHHCCCCC	29.99	28555341
154	Phosphorylation	HLDNVDQTGPKAWKG CCCCCCCCCCCCCCC	51.49	28555341
157	Sumoylation	NVDQTGPKAWKGSTT CCCCCCCCCCCCCCC	69.12	-
157	Ubiquitination	NVDQTGPKAWKGSTT CCCCCCCCCCCCCCC	69.12	29967540
157	Sumoylation	NVDQTGPKAWKGSTT CCCCCCCCCCCCCCC	69.12	-
162	Phosphorylation	GPKAWKGSTTNDPPK CCCCCCCCCCCCCCC	28.47	23927012
163	Phosphorylation	PKAWKGSTTNDPPKQ CCCCCCCCCCCCCCC	37.98	23927012
164	Phosphorylation	KAWKGSTTNDPPKQS CCCCCCCCCCCCCCC	39.04	23663014
171	Phosphorylation	TNDPPKQSPGSTSPK CCCCCCCCCCCCCCC	37.04	23927012
174	Phosphorylation	PPKQSPGSTSPKPPH CCCCCCCCCCCCCCC	29.15	23401153
175	Phosphorylation	PKQSPGSTSPKPPHT CCCCCCCCCCCCCCC	55.77	30266825
176	Phosphorylation	KQSPGSTSPKPPHTL CCCCCCCCCCCCCCC	32.40	30266825
182	Phosphorylation	TSPKPPHTLSRKQWR CCCCCCCCCCHHHHH	32.00	22167270
184	Phosphorylation	PKPPHTLSRKQWRNR CCCCCCCCHHHHHHH	38.29	22167270
201	Sumoylation	NKRRCKNKFQPPQVP HHHHHCCCCCCCCCC	30.76	-
201	Sumoylation	NKRRCKNKFQPPQVP HHHHHCCCCCCCCCC	30.76	-
201	Acetylation	NKRRCKNKFQPPQVP HHHHHCCCCCCCCCC	30.76	26051181
217	Phosphorylation	QAPAEAPTEKTEVSP CCCCCCCCCCCCCCC	58.10	24732914
220	Phosphorylation	AEAPTEKTEVSPVPR CCCCCCCCCCCCCCC	35.07	30266825
223	Phosphorylation	PTEKTEVSPVPRTDS CCCCCCCCCCCCCCC	17.59	29255136
228	Phosphorylation	EVSPVPRTDSHEARA CCCCCCCCCCHHHHH	35.47	24732914
230	Phosphorylation	SPVPRTDSHEARAGA CCCCCCCCHHHHHHH	23.71	28111955
259	Phosphorylation	RYLNEQLYSGPSSAA HHHHHHHHCCCCHHH	15.98	27642862
286	Phosphorylation	LYHRGFQSQVKKWPL HHCCCCHHHHHCCCC	34.38	21712546
309	Phosphorylation	DLRQRPASLVVADFG HHHHCCCCEEEEECC	25.12	27080861
401	Methylation	SSRFEDVRTFLRAVT HHHHHHHHHHHHHHH	31.89	115492947
409	Malonylation	TFLRAVTKLGFKIVS HHHHHHHHHCCEEEE	39.76	26320211
409	Acetylation	TFLRAVTKLGFKIVS HHHHHHHHHCCEEEE	39.76	25953088
413	Acetylation	AVTKLGFKIVSKDLT HHHHHCCEEEECCCC	40.16	26051181
417	Acetylation	LGFKIVSKDLTNSHF HCCEEEECCCCCCCE	45.95	26051181
431	Ubiquitination	FFLFDFQKTGPPLVG EEEEEECCCCCCCCC	56.28	-
440	Sumoylation	GPPLVGPKAQLSGLQ CCCCCCCCHHHCCCC	42.72	-
440	Sumoylation	GPPLVGPKAQLSGLQ CCCCCCCCHHHCCCC	42.72	-
440	Ubiquitination	GPPLVGPKAQLSGLQ CCCCCCCCHHHCCCC	42.72	29967540
454	Sumoylation	QLQPCLYKRR----- CCCCCCCCCC-----	28.84	-
454	Sumoylation	QLQPCLYKRR----- CCCCCCCCCC-----	28.84	-

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 RRP8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRP8_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 RRP8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR1_HUMAN	SIRT1	physical	18485871
SUV91_HUMAN	SUV39H1	physical	18485871
CENPV_HUMAN	CENPV	physical	28514442
SPT2_HUMAN	SPTY2D1	physical	28514442
ZN800_HUMAN	ZNF800	physical	28514442
RRP5_HUMAN	PDCD11	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
TAF1D_HUMAN	TAF1D	physical	28514442
CENPL_HUMAN	CENPL	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
WDR3_HUMAN	WDR3	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
RRP12_HUMAN	RRP12	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
NVL_HUMAN	NVL	physical	28514442
FXR1_HUMAN	FXR1	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
URB2_HUMAN	URB2	physical	28514442
NPA1P_HUMAN	URB1	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
TAF1B_HUMAN	TAF1B	physical	28514442
ZNF48_HUMAN	ZNF48	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
NOL6_HUMAN	NOL6	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
SRBD1_HUMAN	SRBD1	physical	28514442
TUT7_HUMAN	ZCCHC6	physical	28514442
NEPRO_HUMAN	C3orf17	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
RPF1_HUMAN	RPF1	physical	28514442
HERC5_HUMAN	HERC5	physical	28514442
NSD2_HUMAN	WHSC1	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
RLA0_HUMAN	RPLP0	physical	28514442
DHX30_HUMAN	DHX30	physical	28514442
CH033_HUMAN	C8orf33	physical	28514442
NO40_HUMAN	ZCCHC17	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
DDX50_HUMAN	DDX50	physical	28514442
POP7_HUMAN	POP7	physical	28514442
NOC2L_HUMAN	NOC2L	physical	28514442
FXR2_HUMAN	FXR2	physical	28514442
DDX27_HUMAN	DDX27	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
RRP1B_HUMAN	RRP1B	physical	28514442
MBB1A_HUMAN	MYBBP1A	physical	28514442
EBP2_HUMAN	EBNA1BP2	physical	28514442
TAF1C_HUMAN	TAF1C	physical	28514442
THA11_HUMAN	THAP11	physical	28514442
CC137_HUMAN	CCDC137	physical	28514442
RFC1_HUMAN	RFC1	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
NAT10_HUMAN	NAT10	physical	28514442
POP1_HUMAN	POP1	physical	28514442
ZFP62_HUMAN	ZFP62	physical	28514442
NOC4L_HUMAN	NOC4L	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
RL7A_HUMAN	RPL7A	physical	28514442
NOP14_HUMAN	NOP14	physical	28514442
RLP24_HUMAN	RSL24D1	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
DDX52_HUMAN	DDX52	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
RL3_HUMAN	RPL3	physical	28514442
SPB1_HUMAN	FTSJ3	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 RRP8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64; SER-104;SER-106; SER-124 AND SER-126, AND MASS SPECTROMETRY.	19413330 [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-62; SER-64; SER-171;THR-175 AND SER-223, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, AND MASSSPECTROMETRY.	18220336 [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-126, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-126, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-176, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64; SER-104 ANDSER-106, AND MASS SPECTROMETRY.	17081983 [Abstract]