RS21A_YEAST - dbPTM
RS21A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS21A_YEAST
UniProt AC P0C0V8
Protein Name 40S ribosomal protein S21-A {ECO:0000303|PubMed:9559554}
Gene Name RPS21A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 87
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. [PubMed: 22096102 eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability]
Protein Sequence MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYVTYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR
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
1Acetylation-------MENDKGQL
-------CCCCCCCE		11.0910601260
5Succinylation---MENDKGQLVELY
---CCCCCCCEEEEE		61.2023954790
5Acetylation---MENDKGQLVELY
---CCCCCCCEEEEE		61.2024489116
5Ubiquitination---MENDKGQLVELY
---CCCCCCCEEEEE		61.2024961812
12PhosphorylationKGQLVELYVPRKCSA
CCCEEEEECCCCCCC		8.5619823750
18PhosphorylationLYVPRKCSATNRIIK
EECCCCCCCCCCEEE		40.9621551504
20PhosphorylationVPRKCSATNRIIKAD
CCCCCCCCCCEEECC		14.5621440633
25AcetylationSATNRIIKADDHASV
CCCCCEEECCCCCEE		43.3124489116
25UbiquitinationSATNRIIKADDHASV
CCCCCEEECCCCCEE		43.3124961812
31PhosphorylationIKADDHASVQINVAK
EECCCCCEEEEEEEE		15.9024961812
38UbiquitinationSVQINVAKVDEEGRA
EEEEEEEEECCCCCC		46.0323749301
38SuccinylationSVQINVAKVDEEGRA
EEEEEEEEECCCCCC		46.0323954790
38AcetylationSVQINVAKVDEEGRA
EEEEEEEEECCCCCC		46.0324489116
61PhosphorylationALSGYVRSRGESDDS
CHHHCHHCCCCCHHH		34.2922369663
65PhosphorylationYVRSRGESDDSLNRL
CHHCCCCCHHHHHHH		49.9322369663
68PhosphorylationSRGESDDSLNRLAQN
CCCCCHHHHHHHHHH		32.3122369663
80UbiquitinationAQNDGLLKNVWSYSR
HHHCCHHHHHHHHCC		55.2723749301
80AcetylationAQNDGLLKNVWSYSR
HHHCCHHHHHHHHCC		55.2724489116
84PhosphorylationGLLKNVWSYSR----
CHHHHHHHHCC----		14.6719823750
85PhosphorylationLLKNVWSYSR-----
HHHHHHHHCC-----		7.8620377248
86PhosphorylationLKNVWSYSR------
HHHHHHHCC------		26.4625521595
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 RS21A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS21A_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 RS21A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS21B_YEASTRPS21Bgenetic
14627813
RTC6_YEASTRTC6genetic
20691087
RS21B_YEASTRPS21Bgenetic
22377630
ACT_YEASTACT1genetic
27708008
MIF2_YEASTMIF2genetic
27708008
ABF1_YEASTABF1genetic
27708008
PSB6_YEASTPRE7genetic
27708008
CDC27_YEASTCDC27genetic
27708008
ALG1_YEASTALG1genetic
27708008
RSC6_YEASTRSC6genetic
27708008
APC11_YEASTAPC11genetic
27708008
FBRL_YEASTNOP1genetic
27708008
RPN6_YEASTRPN6genetic
27708008
RPN5_YEASTRPN5genetic
27708008
NHP2_YEASTNHP2genetic
27708008
DAD1_YEASTDAD1genetic
27708008
DBF4_YEASTDBF4genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SLY1_YEASTSLY1genetic
27708008
PSB3_YEASTPUP3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
RPN11_YEASTRPN11genetic
27708008
RPN12_YEASTRPN12genetic
27708008
PRS8_YEASTRPT6genetic
27708008
CDC20_YEASTCDC20genetic
27708008
PRP18_YEASTPRP18genetic
27708008
RRP41_YEASTSKI6genetic
27708008
RPN1_YEASTRPN1genetic
27708008
UTP9_YEASTUTP9genetic
27708008
PRI1_YEASTPRI1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
SMC3_YEASTSMC3genetic
27708008
RRN3_YEASTRRN3genetic
27708008
PRS7_YEASTRPT1genetic
27708008
SN114_YEASTSNU114genetic
27708008
CD123_YEASTCDC123genetic
27708008
RU1C_YEASTYHC1genetic
27708008
RLA0_YEASTRPP0genetic
27708008
IMB1_YEASTKAP95genetic
27708008
POB3_YEASTPOB3genetic
27708008
PRP24_YEASTPRP24genetic
27708008
DPOA_YEASTPOL1genetic
27708008
MVD1_YEASTMVD1genetic
27708008
MED7_YEASTMED7genetic
27708008
SGT1_YEASTSGT1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
IPL1_YEASTIPL1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
DOM34_YEASTDOM34genetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS21A_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: ACETYLATION AT MET-1 BY NATB.
Phosphorylation
ReferencePubMed
"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-84, AND MASSSPECTROMETRY.

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