RL36A_YEAST - dbPTM
RL36A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL36A_YEAST
UniProt AC P05745
Protein Name 60S ribosomal protein L36-A {ECO:0000303|PubMed:9559554}
Gene Name RPL36A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 100
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 MTVKTGIAIGLNKGKKVTSMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNSGEKRARKVAKKRLGSFTRAKAKVEEMNNIIAASRRH
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------MTVKTGIAI
------CCCCCCEEE		30.6110601260
5Phosphorylation---MTVKTGIAIGLN
---CCCCCCEEEECC		29.5021440633
152-HydroxyisobutyrylationAIGLNKGKKVTSMTP
EEECCCCCCCEECCC		45.76-
162-HydroxyisobutyrylationIGLNKGKKVTSMTPA
EECCCCCCCEECCCC		60.45-
18PhosphorylationLNKGKKVTSMTPAPK
CCCCCCCEECCCCCC		22.9723749301
19PhosphorylationNKGKKVTSMTPAPKI
CCCCCCEECCCCCCC		24.5220377248
21PhosphorylationGKKVTSMTPAPKISY
CCCCEECCCCCCCCC		18.9623749301
42PhosphorylationNRTKFVRSLVREIAG
CHHHHHHHHHHHHCC		26.3921440633
51PhosphorylationVREIAGLSPYERRLI
HHHHCCCCHHHHHHH		25.2327214570
64PhosphorylationLIDLIRNSGEKRARK
HHHHHHHCHHHHHHH		38.1828152593
79PhosphorylationVAKKRLGSFTRAKAK
HHHHHHCCHHHHHHH		28.2119823750
81PhosphorylationKKRLGSFTRAKAKVE
HHHHCCHHHHHHHHH		31.2624961812
84UbiquitinationLGSFTRAKAKVEEMN
HCCHHHHHHHHHHHH		45.5122817900
86UbiquitinationSFTRAKAKVEEMNNI
CHHHHHHHHHHHHHH		49.8523749301
97PhosphorylationMNNIIAASRRH----
HHHHHHHHHCC----		22.3322369663
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 RL36A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL36A_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 RL36A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL36B_YEASTRPL36Bgenetic
22377630
RL36B_YEASTRPL36Bgenetic
25119672
EBP2_YEASTEBP2physical
25119672
NOP12_YEASTNOP12physical
25119672
CND2_YEASTBRN1genetic
27708008
SLU7_YEASTSLU7genetic
27708008
MOB2_YEASTMOB2genetic
27708008
PTI1_YEASTPTI1genetic
27708008
SAM35_YEASTSAM35genetic
27708008
TPS2_YEASTTPS2genetic
27708008
SSU1_YEASTSSU1genetic
27708008
MCM2_YEASTMCM2genetic
27708008
ORC2_YEASTORC2genetic
27708008
EXO84_YEASTEXO84genetic
27708008
FBRL_YEASTNOP1genetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPN5_YEASTRPN5genetic
27708008
NOP14_YEASTNOP14genetic
27708008
CAB5_YEASTCAB5genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
RPN11_YEASTRPN11genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
PRP31_YEASTPRP31genetic
27708008
MPPA_YEASTMAS2genetic
27708008
RPN1_YEASTRPN1genetic
27708008
MET30_YEASTMET30genetic
27708008
EXO70_YEASTEXO70genetic
27708008
FIP1_YEASTFIP1genetic
27708008
RRN3_YEASTRRN3genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RU1C_YEASTYHC1genetic
27708008
CDC3_YEASTCDC3genetic
27708008
RLA0_YEASTRPP0genetic
27708008
SEC65_YEASTSEC65genetic
27708008
TRM6_YEASTGCD10genetic
27708008
SEC12_YEASTSEC12genetic
27708008
PSA4_YEASTPRE6genetic
27708008
NUF2_YEASTNUF2genetic
27708008
BRX1_YEASTBRX1genetic
27708008
CH10_YEASTHSP10genetic
27708008
TYSY_YEASTCDC21genetic
27708008
PRS10_YEASTRPT4genetic
27708008
NAB3_YEASTNAB3genetic
27708008
PSB5_YEASTPRE2genetic
27708008
IWS1_YEASTSPN1genetic
27708008
PGTB2_YEASTBET2genetic
27708008
UBC4_YEASTUBC4genetic
27708008
NHP10_YEASTNHP10genetic
27708008
PEX19_YEASTPEX19genetic
27708008
PEX10_YEASTPEX10genetic
27708008
APA2_YEASTAPA2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
PRM8_YEASTPRM8genetic
27708008
XRN1_YEASTXRN1genetic
27708008
SKI8_YEASTSKI8genetic
27708008
PSA3_YEASTPRE9genetic
27708008
YG3O_YEASTYGR153Wgenetic
27708008
ARN1_YEASTARN1genetic
27708008
SODM_YEASTSOD2genetic
27708008
STB5_YEASTSTB5genetic
27708008
HOS4_YEASTHOS4genetic
27708008
ELM1_YEASTELM1genetic
27708008
TCTP_YEASTTMA19genetic
27708008
DOA1_YEASTDOA1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
ORM2_YEASTORM2genetic
27708008
SRR1L_YEASTBER1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
INO4_YEASTINO4genetic
27708008
SKI7_YEASTSKI7genetic
27708008
ETFD_YEASTCIR2genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
KES1_YEASTKES1genetic
27708008
RL20A_YEASTRPL20Bgenetic
29158977
RL20B_YEASTRPL20Bgenetic
29158977
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL36A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT THR-2 BY NATA.
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-19 AND SER-97, AND MASSSPECTROMETRY.
"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-79, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASSSPECTROMETRY.

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