dbPTM

RRP36_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRP36_YEAST
UniProt AC	Q12481
Protein Name	rRNA biogenesis protein RRP36
Gene Name	RRP36
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	300
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Component of the 90S pre-ribosome involved in the maturation of rRNAs. Required for early cleavages of the pre-RNAs in the 40S ribosomal subunit maturation pathway..
Protein Sequence	MSYYFKNLKPDLNSDVEEDDGNLLESIMANKSKREIDEQESSDDELKTLSFGSLKKAETVIDEEDFKDTKPVHKKPITTTYREESFDEDEDSEDQSDEDAGFFEEDSEDETHHGQKVPKKKSKHAPVEQSSKKRVPRVRNIPGLEIPRNKRSNLYQDIRFDKSTGKALDSSIIRKRYQFLDEYREKEIDELQKLLQERKFLSKIDQGEREEMEQRLKSMKSRLQSMKNKDLEREILKEYENDMNKNNNTRYHLKKSEKRKVVQKWKFDHMKAKQREKVMERKRKKRLGKEFKQFEFHNRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	NLKPDLNSDVEEDDG CCCCCCCCCCCCCCC	50.78	22369663
26	Phosphorylation	DDGNLLESIMANKSK CCCHHHHHHHHCCCH	20.03	25521595
32	Phosphorylation	ESIMANKSKREIDEQ HHHHHCCCHHCCCCC	36.43	19823750
41	Phosphorylation	REIDEQESSDDELKT HCCCCCCCCCHHHHH	38.47	17330950
42	Phosphorylation	EIDEQESSDDELKTL CCCCCCCCCHHHHHC	48.61	17330950
48	Phosphorylation	SSDDELKTLSFGSLK CCCHHHHHCHHHHHC	40.01	28889911
50	Phosphorylation	DDELKTLSFGSLKKA CHHHHHCHHHHHCCC	32.56	21440633
53	Phosphorylation	LKTLSFGSLKKAETV HHHCHHHHHCCCEEE	34.70	21440633
59	Phosphorylation	GSLKKAETVIDEEDF HHHCCCEEEECHHHH	27.85	25521595
123	Acetylation	KVPKKKSKHAPVEQS CCCCCCCCCCCCCHH	53.30	25381059
162	Acetylation	YQDIRFDKSTGKALD HHHHCEEHHHCCCCC	47.40	25381059
166	Acetylation	RFDKSTGKALDSSII CEEHHHCCCCCHHHH	45.95	25381059
170	Phosphorylation	STGKALDSSIIRKRY HHCCCCCHHHHHHHH	25.04	30377154
171	Phosphorylation	TGKALDSSIIRKRYQ HCCCCCHHHHHHHHH	23.00	21440633
203	Acetylation	QERKFLSKIDQGERE HHHHHHHHCCHHHHH	53.07	24489116
264	Acetylation	EKRKVVQKWKFDHMK HHHHHHHHHHHHHHH	40.52	25381059
266	Acetylation	RKVVQKWKFDHMKAK HHHHHHHHHHHHHHH	48.20	25381059

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 RRP36_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RRP36_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 RRP36_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DBP4_YEAST	HCA4	physical	20038530
FBRL_YEAST	NOP1	physical	20038530
KRR1_YEAST	KRR1	physical	20038530
EBP2_YEAST	EBP2	physical	20038530
RRP14_YEAST	RRP14	physical	20038530
UTP22_YEAST	UTP22	physical	20038530
CSK21_YEAST	CKA1	physical	20038530
CSK22_YEAST	CKA2	physical	20038530
CSK2B_YEAST	CKB1	physical	20038530
CSK2C_YEAST	CKB2	physical	20038530
MRT4_YEAST	MRT4	physical	20038530
NOP12_YEAST	NOP12	physical	20038530
DVL2_HUMAN	DVL2	physical	27107014

Drug and Disease Associations

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

Regulatory Network of RRP36_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-14; SER-41 AND SER-42,AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.	17563356 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASSSPECTROMETRY.	17287358 [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-14; SER-41 AND SER-42,AND MASS SPECTROMETRY.	17330950 [Abstract]