RS25B_YEAST - dbPTM
RS25B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS25B_YEAST
UniProt AC P0C0T4
Protein Name 40S ribosomal protein S25-B {ECO:0000303|PubMed:9559554}
Gene Name RPS25B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 108
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel..
Protein Sequence MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRAAASE
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
2Methylation------MPPKQQLSK
------CCHHHHHHH		44.8120481588
9AcetylationPPKQQLSKAAKAAAA
CHHHHHHHHHHHHHH		62.0425381059
122-HydroxyisobutyrylationQQLSKAAKAAAALAG
HHHHHHHHHHHHHHC		43.34-
212-HydroxyisobutyrylationAAALAGGKKSKKKWS
HHHHHCCCCCHHCCC		53.61-
21UbiquitinationAAALAGGKKSKKKWS
HHHHHCCCCCHHCCC		53.6123749301
21SuccinylationAAALAGGKKSKKKWS
HHHHHCCCCCHHCCC		53.6123954790
21AcetylationAAALAGGKKSKKKWS
HHHHHCCCCCHHCCC		53.6123572591
31PhosphorylationKKKWSKKSMKDRAQH
HHCCCHHHHHHHHHH		34.5017287358
46SuccinylationAVILDQEKYDRILKE
EEEECHHHHHHHHHH		46.9823954790
462-HydroxyisobutyrylationAVILDQEKYDRILKE
EEEECHHHHHHHHHH		46.98-
46AcetylationAVILDQEKYDRILKE
EEEECHHHHHHHHHH		46.9824489116
46UbiquitinationAVILDQEKYDRILKE
EEEECHHHHHHHHHH		46.9823749301
47PhosphorylationVILDQEKYDRILKEV
EEECHHHHHHHHHHC		15.0921082442
52SuccinylationEKYDRILKEVPTYRY
HHHHHHHHHCCCCEE		55.0523954790
52AcetylationEKYDRILKEVPTYRY
HHHHHHHHHCCCCEE		55.0524489116
52UbiquitinationEKYDRILKEVPTYRY
HHHHHHHHHCCCCEE		55.0523749301
61PhosphorylationVPTYRYVSVSVLVDR
CCCCEEEEHHHHHHH		10.3517287358
63PhosphorylationTYRYVSVSVLVDRLK
CCEEEEHHHHHHHHC		11.3917287358
702-HydroxyisobutyrylationSVLVDRLKIGGSLAR
HHHHHHHCCCHHHHH		39.95-
70UbiquitinationSVLVDRLKIGGSLAR
HHHHHHHCCCHHHHH		39.9523749301
74PhosphorylationDRLKIGGSLARIALR
HHHCCCHHHHHHHHH		17.4021440633
85AcetylationIALRHLEKEGIIKPI
HHHHHHHHCCCCCCC		68.5424489116
85SuccinylationIALRHLEKEGIIKPI
HHHHHHHHCCCCCCC		68.5423954790
85UbiquitinationIALRHLEKEGIIKPI
HHHHHHHHCCCCCCC		68.5423749301
852-HydroxyisobutyrylationIALRHLEKEGIIKPI
HHHHHHHHCCCCCCC		68.54-
90AcetylationLEKEGIIKPISKHSK
HHHCCCCCCCCHHHH		34.0824489116
90SuccinylationLEKEGIIKPISKHSK
HHHCCCCCCCCHHHH		34.0823954790
90UbiquitinationLEKEGIIKPISKHSK
HHHCCCCCCCCHHHH		34.0823749301
93PhosphorylationEGIIKPISKHSKQAI
CCCCCCCCHHHHHHH		32.6122369663
94UbiquitinationGIIKPISKHSKQAIY
CCCCCCCHHHHHHHH		53.2523749301
94AcetylationGIIKPISKHSKQAIY
CCCCCCCHHHHHHHH		53.2525381059
97UbiquitinationKPISKHSKQAIYTRA
CCCCHHHHHHHHHHH		43.3923749301
972-HydroxyisobutyrylationKPISKHSKQAIYTRA
CCCCHHHHHHHHHHH		43.39-
97SuccinylationKPISKHSKQAIYTRA
CCCCHHHHHHHHHHH		43.3923954790
97AcetylationKPISKHSKQAIYTRA
CCCCHHHHHHHHHHH		43.3924489116
107PhosphorylationIYTRAAASE------
HHHHHHHCC------		38.8325521595
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 RS25B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS25B_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 RS25B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YRA1_YEASTYRA1physical
16554755
RS26B_YEASTRPS26Bphysical
16554755
STM1_YEASTSTM1physical
16554755
IMDH4_YEASTIMD4physical
16554755
LSP1_YEASTLSP1physical
18719252
SWC4_YEASTSWC4genetic
27708008
PRP11_YEASTPRP11genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC4_YEASTCDC4genetic
27708008
CDC14_YEASTCDC14genetic
27708008
MED6_YEASTMED6genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NMT_YEASTNMT1genetic
27708008
IPL1_YEASTIPL1genetic
27708008
CSG2_YEASTCSG2genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
NPL4_YEASTNPL4genetic
27708008
SLX5_YEASTSLX5genetic
27708008
PEX19_YEASTPEX19genetic
27708008
SAS4_YEASTSAS4genetic
27708008
MNN10_YEASTMNN10genetic
27708008
XRS2_YEASTXRS2genetic
27708008
SHE9_YEASTSHE9genetic
27708008
UBP3_YEASTUBP3genetic
27708008
ATG1_YEASTATG1genetic
27708008
SKI8_YEASTSKI8genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
YOR1_YEASTYOR1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
PEP8_YEASTPEP8genetic
27708008
KTI12_YEASTKTI12genetic
27708008
NNK1_YEASTNNK1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
DNM1_YEASTDNM1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
TOM7_YEASTTOM7genetic
27708008
MKS1_YEASTMKS1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
RTG1_YEASTRTG1genetic
27708008
INO4_YEASTINO4genetic
27708008
VPS17_YEASTVPS17genetic
27708008
VPH1_YEASTVPH1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS25B_YEAST

loading...

Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identification of protein N-terminal methyltransferases in yeast andhumans.";
Webb K.J., Lipson R.S., Al-Hadid Q., Whitelegge J.P., Clarke S.G.;
Biochemistry 49:5225-5235(2010).
Cited for: METHYLATION AT PRO-2 BY NTM1/TAE1.
Phosphorylation
ReferencePubMed
"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-31, AND MASSSPECTROMETRY.

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