RLA3_YEAST - dbPTM
RLA3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA3_YEAST
UniProt AC P10622
Protein Name 60S acidic ribosomal protein P1-beta {ECO:0000303|PubMed:9559554}
Gene Name RPP1B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 106
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 MSDSIISFAAFILADAGLEITSDNLLTITKAAGANVDNVWADVYAKALEGKDLKEILSGFHNAGPVAGAGAASGAAAAGGDAAAEEEKEEEAAEESDDDMGFGLFD
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
2Acetylation------MSDSIISFA
------CCHHHHHHH		39.818476850
46UbiquitinationVWADVYAKALEGKDL
HHHHHHHHHHCCCCH		35.5023749301
46AcetylationVWADVYAKALEGKDL
HHHHHHHHHHCCCCH		35.5024489116
46SuccinylationVWADVYAKALEGKDL
HHHHHHHHHHCCCCH		35.5023954790
51UbiquitinationYAKALEGKDLKEILS
HHHHHCCCCHHHHHH		50.9823749301
54UbiquitinationALEGKDLKEILSGFH
HHCCCCHHHHHHCCC		53.4922817900
58PhosphorylationKDLKEILSGFHNAGP
CCHHHHHHCCCCCCC		45.1119795423
73PhosphorylationVAGAGAASGAAAAGG
CCCHHHHHHHHHHCC		28.5619823750
96PhosphorylationEEEAAEESDDDMGFG
HHHHHHHCCCCCCCC		37.5322369663
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 RLA3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA3_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 RLA3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RLA2_YEASTRPP2Aphysical
20225338
RLA1_YEASTRPP1Aphysical
20225338
RLA4_YEASTRPP2Bphysical
20225338
RLA3_YEASTRPP1Bphysical
17040491
RLA4_YEASTRPP2Bphysical
14617190
RLA1_YEASTRPP1Aphysical
14617190
RLA2_YEASTRPP2Aphysical
14617190
RLA0_YEASTRPP0genetic
22275522
TCPZ_YEASTCCT6genetic
27708008
SAC3_YEASTSAC3genetic
27708008
GCN1_YEASTGCN1genetic
27708008
BUB1_YEASTBUB1genetic
27708008
RL17B_YEASTRPL17Bgenetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
RS10B_YEASTRPS10Bgenetic
27708008
NEW1_YEASTNEW1genetic
27708008
POP7_YEASTPOP7genetic
27708008
NOT1_YEASTCDC39genetic
27708008
TFB1_YEASTTFB1genetic
27708008
PSB3_YEASTPUP3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
ESP1_YEASTESP1genetic
27708008
DAM1_YEASTDAM1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
RPN1_YEASTRPN1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
MED11_YEASTMED11genetic
27708008
LCB1_YEASTLCB1genetic
27708008
NOG2_YEASTNOG2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
PSA7_YEASTPRE10genetic
27708008
IPL1_YEASTIPL1genetic
27708008
IF6_YEASTTIF6genetic
27708008
PSB5_YEASTPRE2genetic
27708008
RPN7_YEASTRPN7genetic
27708008
FLO1_YEASTFLO1genetic
27708008
YBI1_YEASTYBL081Wgenetic
27708008
ETR1_YEASTETR1genetic
27708008
TCM62_YEASTTCM62genetic
27708008
MUM2_YEASTMUM2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
EF1A_YEASTTEF2genetic
27708008
HPC2_YEASTHPC2genetic
27708008
ATG22_YEASTATG22genetic
27708008
PAT1_YEASTPAT1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
RPA14_YEASTRPA14genetic
27708008
FCY21_YEASTFCY21genetic
27708008
CEM1_YEASTCEM1genetic
27708008
MSH4_YEASTMSH4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
PYC1_YEASTPYC1genetic
27708008
ITC1_YEASTITC1genetic
27708008
YRB30_YEASTYRB30genetic
27708008
MDM34_YEASTMDM34genetic
27708008
MSB2_YEASTMSB2genetic
27708008
ORM1_YEASTORM1genetic
27708008
ASK10_YEASTASK10genetic
27708008
YG51_YEASTYGR237Cgenetic
27708008
MGA1_YEASTMGA1genetic
27708008
MAL12_YEASTMAL12genetic
27708008
YHJ5_YEASTNEL1genetic
27708008
PUT2_YEASTPUT2genetic
27708008
HTD2_YEASTHTD2genetic
27708008
ARP1_YEASTARP1genetic
27708008
RPN10_YEASTRPN10genetic
27708008
LSM1_YEASTLSM1genetic
27708008
DYHC_YEASTDYN1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
LDB18_YEASTLDB18genetic
27708008
LOT6_YEASTLOT6genetic
27708008
POC3_YEASTIRC25genetic
27708008
SIC1_YEASTSIC1genetic
27708008
SRR1L_YEASTBER1genetic
27708008
PPZ1_YEASTPPZ1genetic
27708008
SAM37_YEASTSAM37genetic
27708008
YMW4_YEASTYMR074Cgenetic
27708008
GBLP_YEASTASC1genetic
27708008
YM94_YEASTYMR315Wgenetic
27708008
DOM34_YEASTDOM34genetic
27708008
ATG3_YEASTATG3genetic
27708008
TRM11_YEASTTRM11genetic
27708008
TYW4_YEASTPPM2genetic
27708008
YORA4_YEASTYOR114Wgenetic
27708008
LIPA_YEASTLIP5genetic
27708008
LIS1_YEASTPAC1genetic
27708008
CHL1_YEASTCHL1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
NIP80_YEASTNIP100genetic
27708008
CTI6_YEASTCTI6genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLA3_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes.NH2-terminal acetylation is a conserved difference between P1 and P2proteins.";
Santos C., Ortiz-Reyes B., Naranda T., Remacha M., Ballesta J.P.G.;
Biochemistry 32:4231-4236(1993).
Cited for: PROTEIN SEQUENCE OF 9-16, AND ACETYLATION AT SER-2.
Phosphorylation
ReferencePubMed
"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-96, AND MASSSPECTROMETRY.

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