RS25A_YEAST - dbPTM
RS25A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS25A_YEAST
UniProt AC Q3E792
Protein Name 40S ribosomal protein S25-A {ECO:0000303|PubMed:9559554}
Gene Name RPS25A {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 MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRATASE
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
21UbiquitinationAAALAGGKKSKKKWS
HHHHHCCCCCHHCCC		53.6123749301
31PhosphorylationKKKWSKKSMKDRAQH
HHCCCHHHHHHHHHH		34.5017287358
46UbiquitinationAVILDQEKYDRILKE
EEEECHHHHHHHHHH		46.9823749301
47PhosphorylationVILDQEKYDRILKEV
EEECHHHHHHHHHHC		15.0921082442
52UbiquitinationEKYDRILKEVPTYRY
HHHHHHHHHCCCCEE		55.0523749301
61PhosphorylationVPTYRYVSVSVLVDR
CCCCEEEEHHHHHHH		10.3517287358
63PhosphorylationTYRYVSVSVLVDRLK
CCEEEEHHHHHHHHC		11.3917287358
70UbiquitinationSVLVDRLKIGGSLAR
HHHHHHHCCCHHHHH		39.9523749301
74PhosphorylationDRLKIGGSLARIALR
HHHCCCHHHHHHHHH		17.4021440633
85UbiquitinationIALRHLEKEGIIKPI
HHHHHHHHCCCCCCC		68.5423749301
90UbiquitinationLEKEGIIKPISKHSK
HHHCCCCCCCCHHCH		34.0823749301
93PhosphorylationEGIIKPISKHSKQAI
CCCCCCCCHHCHHHH		32.6122369663
94UbiquitinationGIIKPISKHSKQAIY
CCCCCCCHHCHHHHH		53.2523749301
97UbiquitinationKPISKHSKQAIYTRA
CCCCHHCHHHHHHHH		43.3923749301
101PhosphorylationKHSKQAIYTRATASE
HHCHHHHHHHHCCCC		8.0019779198
102PhosphorylationHSKQAIYTRATASE-
HCHHHHHHHHCCCC-		14.0221126336
105PhosphorylationQAIYTRATASE----
HHHHHHHCCCC----		27.6822369663
107PhosphorylationIYTRATASE------
HHHHHCCCC------		39.2120377248
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 RS25A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS25A_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 RS25A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSP1_YEASTLSP1physical
18719252
PIL1_YEASTPIL1physical
18719252
SSB1_YEASTSSB1physical
19536198
DEP1_YEASTDEP1genetic
20093466
EF1A_YEASTTEF2genetic
20093466
ATU1_YEASTPCA1genetic
20093466
DHE2_YEASTGDH2genetic
20093466
RL41A_YEASTRPL41Agenetic
20093466
RL41B_YEASTRPL41Agenetic
20093466
MNN10_YEASTMNN10genetic
20093466
OMS1_YEASTOMS1genetic
20093466
EF2_YEASTEFT2genetic
20093466
CTU1_YEASTNCS6genetic
20093466
ATG1_YEASTATG1genetic
20093466
YOR1_YEASTYOR1genetic
20093466
LRP1_YEASTLRP1genetic
20093466
UBA4_YEASTUBA4genetic
20093466
STB5_YEASTSTB5genetic
20093466
HOC1_YEASTHOC1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
CAF4_YEASTCAF4genetic
20093466
RL8B_YEASTRPL8Bgenetic
20093466
RS25B_YEASTRPS25Bgenetic
20093466
VRP1_YEASTVRP1genetic
20093466
YL352_YEASTYLR352Wgenetic
20093466
ELP1_YEASTIKI3genetic
20093466
MSC1_YEASTMSC1genetic
20093466
CIK1_YEASTCIK1genetic
20093466
PSK2_YEASTPSK2genetic
20093466
PLB3_YEASTPLB3genetic
20093466
TSR3_YEASTTSR3genetic
20093466
MCP1_YEASTMCP1genetic
20093466
ELP3_YEASTELP3genetic
20093466
KAR3_YEASTKAR3genetic
20093466
SRS2_YEASTSRS2genetic
21459050
RS25B_YEASTRPS25Bgenetic
22377630
ATG1_YEASTATG1genetic
22282571
TCPZ_YEASTCCT6genetic
27708008
TCPA_YEASTTCP1genetic
27708008
STU1_YEASTSTU1genetic
27708008
CND2_YEASTBRN1genetic
27708008
NHP2_YEASTNHP2genetic
27708008
DBF4_YEASTDBF4genetic
27708008
CDC1_YEASTCDC1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
BCD1_YEASTBCD1genetic
27708008
KRE9_YEASTKRE9genetic
27708008
IF2A_YEASTSUI2genetic
27708008
PRS7_YEASTRPT1genetic
27708008
SSL1_YEASTSSL1genetic
27708008
MED14_YEASTRGR1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
CDC25_YEASTCDC25genetic
27708008
TAD3_YEASTTAD3genetic
27708008
AFG2_YEASTAFG2genetic
27708008
NOG2_YEASTNOG2genetic
27708008
MED7_YEASTMED7genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PROF_YEASTPFY1genetic
27708008
RRS1_YEASTRRS1genetic
27708008
KRE5_YEASTKRE5genetic
27708008
TF2B_YEASTSUA7genetic
27708008
PSB5_YEASTPRE2genetic
27708008
EF1A_YEASTTEF2genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
MNN10_YEASTMNN10genetic
27708008
UBP3_YEASTUBP3genetic
27708008
STB5_YEASTSTB5genetic
27708008
FABG_YEASTOAR1genetic
27708008
RS25B_YEASTRPS25Bgenetic
27708008
ELP1_YEASTIKI3genetic
27708008
SST2_YEASTSST2genetic
27708008
VPS9_YEASTVPS9genetic
27708008
SIN3_YEASTSIN3genetic
27708008
TSR3_YEASTTSR3genetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS25A_YEAST

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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-61 AND SER-63, AND MASSSPECTROMETRY.

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