RL1D1_YEAST - dbPTM
RL1D1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL1D1_YEAST
UniProt AC P36144
Protein Name Ribosome biogenesis protein UTP30
Gene Name UTP30
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 274
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in rRNA-processing and ribosome biosynthesis..
Protein Sequence MVESNDIIKSGLAEKALKALILQCEENPSLKNDKDIHIIINTGKKMGINRDNIPRIIPLTKYKLFKPRDLNILLITKDPSALYRETLTKDEHTSELFKEIISVKNLRRRFKGSKLTQLYKDFDLVVADYRVHHLLPEVLGSRFYHGSKKLPYMIRMSKEVKLKRQQMVEKCDPIYVRAQLRSICKNTSYIPNNDNCLSVRVGYIQKHSIPEILQNIQDTINFLTDKSKRPQGGVIKGGIISIFVKTSNSTSLPIYQFSEARENQKNEDLSDIKL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
42PhosphorylationDIHIIINTGKKMGIN
CEEEEEECCCCCCCC		39.7128889911
89AcetylationLYRETLTKDEHTSEL
HHHHHCCCCHHHHHH		65.3224489116
265AcetylationSEARENQKNEDLSDI
HHHHHHHCCCCHHHC		74.1024489116
270PhosphorylationNQKNEDLSDIKL---
HHCCCCHHHCCC---		50.0022369663
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 RL1D1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL1D1_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 RL1D1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN9_YEASTCSN9physical
10688190
CMS1_YEASTCMS1genetic
19061648
LRP1_YEASTLRP1genetic
19061648
ENT5_YEASTENT5genetic
20093466
PBS2_YEASTPBS2genetic
20093466
FRA1_YEASTFRA1genetic
20093466
WHI2_YEASTWHI2genetic
20093466
ASK10_YEASTASK10genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
STN1_YEASTSTN1genetic
29674565
FCF1_YEASTFCF1genetic
29674565
SIC1_YEASTSIC1genetic
29674565
RRP5_YEASTRRP5genetic
29674565
DCAM_YEASTSPE2genetic
29674565
GGPPS_YEASTBTS1genetic
29674565
CDC27_YEASTCDC27genetic
29674565
SAC3_YEASTSAC3genetic
29674565
TAF6_YEASTTAF6genetic
29674565
KEL1_YEASTKEL1genetic
29674565
THP2_YEASTTHP2genetic
29674565
SAC1_YEASTSAC1genetic
29674565
PPQ1_YEASTPPQ1genetic
29674565
SUR1_YEASTSUR1genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL1D1_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-270, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory