dbPTM

RRP3_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRP3_YEAST
UniProt AC	P38712
Protein Name	ATP-dependent rRNA helicase RRP3 {ECO:0000305}
Gene Name	RRP3 {ECO:0000303\|PubMed:8774901}
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	501
Subcellular Localization	Nucleus .
Protein Description	ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA..
Protein Sequence	MSKIVKRKEKKANDELTSLAEKIRAKALENQKKLIEAEKEGGSESDSEEDATAEKKKVLKSKSKSTVSTQNENTNEDESFESFSELNLVPELIQACKNLNYSKPTPIQSKAIPPALEGHDIIGLAQTGSGKTAAFAIPILNRLWHDQEPYYACILAPTRELAQQIKETFDSLGSLMGVRSTCIVGGMNMMDQARDLMRKPHIIIATPGRLMDHLENTKGFSLRKLKFLVMDEADRLLDMEFGPVLDRILKIIPTQERTTYLFSATMTSKIDKLQRASLTNPVKCAVSNKYQTVDTLVQTLMVVPGGLKNTYLIYLLNEFIGKTMIIFTRTKANAERLSGLCNLLEFSATALHGDLNQNQRMGSLDLFKAGKRSILVATDVAARGLDIPSVDIVVNYDIPVDSKSYIHRVGRTARAGRSGKSISLVSQYDLELILRIEEVLGKKLPKESVDKNIILTLRDSVDKANGEVVMEMNRRNKEKIARGKGRRGRMMTRENMDMGER

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	KKANDELTSLAEKIR HHCCHHHHHHHHHHH	21.46	28889911
18	Phosphorylation	KANDELTSLAEKIRA HCCHHHHHHHHHHHH	37.90	30377154
22	Acetylation	ELTSLAEKIRAKALE HHHHHHHHHHHHHHH	31.70	24489116
26	Acetylation	LAEKIRAKALENQKK HHHHHHHHHHHHHHH	43.59	25381059
43	Phosphorylation	EAEKEGGSESDSEED HHHHCCCCCCCCHHH	44.79	17330950
45	Phosphorylation	EKEGGSESDSEEDAT HHCCCCCCCCHHHHH	48.40	25521595
47	Phosphorylation	EGGSESDSEEDATAE CCCCCCCCHHHHHHH	52.76	25521595
52	Phosphorylation	SDSEEDATAEKKKVL CCCHHHHHHHHHHHH	47.90	22890988
97	Ubiquitination	PELIQACKNLNYSKP HHHHHHHHCCCCCCC	68.44	17644757
103	Ubiquitination	CKNLNYSKPTPIQSK HHCCCCCCCCCCCCC	42.42	17644757
103	Acetylation	CKNLNYSKPTPIQSK HHCCCCCCCCCCCCC	42.42	24489116
110	Ubiquitination	KPTPIQSKAIPPALE CCCCCCCCCCCHHHC	33.68	17644757
217	Phosphorylation	LMDHLENTKGFSLRK HHHHHHHCCCCCHHH	24.14	27017623
250	Acetylation	PVLDRILKIIPTQER HHHHHHHHHCCCCCC	35.90	22865919
277	Phosphorylation	IDKLQRASLTNPVKC HHHHHHCCCCCCCHH	37.60	19823750
279	Phosphorylation	KLQRASLTNPVKCAV HHHHCCCCCCCHHHH	34.67	19823750
421	Phosphorylation	RAGRSGKSISLVSQY CCCCCCCCEEEEEHH	22.42	28889911
423	Phosphorylation	GRSGKSISLVSQYDL CCCCCCEEEEEHHCH	29.79	28889911
426	Phosphorylation	GKSISLVSQYDLELI CCCEEEEEHHCHHHH	28.46	28889911
428	Phosphorylation	SISLVSQYDLELILR CEEEEEHHCHHHHHH	18.26	28889911
460	Phosphorylation	IILTLRDSVDKANGE EEEEEHHHHHHCCCE	26.28	27017623

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 RRP3_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRP3_YEAST !!

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 RRP3_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYDM_YEAST	MSD1	genetic	19061648
MPP10_YEAST	MPP10	physical	16449634

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RRP3_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45 AND SER-47,AND MASS SPECTROMETRY.	18407956 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-45 AND SER-47,AND MASS SPECTROMETRY.	17330950 [Abstract]