RS27A_YEAST - dbPTM
RS27A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS27A_YEAST
UniProt AC P35997
Protein Name 40S ribosomal protein S27-A {ECO:0000303|PubMed:9559554}
Gene Name RPS27A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 82
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 MVLVQDLLHPTAASEARKHKLKTLVQGPRSYFLDVKCPGCLNITTVFSHAQTAVTCESCSTILCTPTGGKAKLSEGTSFRRK
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
11PhosphorylationVQDLLHPTAASEARK
CCCCCCHHHHHHHHH		31.3628889911
14PhosphorylationLLHPTAASEARKHKL
CCCHHHHHHHHHHHH		23.3025704821
18UbiquitinationTAASEARKHKLKTLV
HHHHHHHHHHHHHHH		34.8422817900
20UbiquitinationASEARKHKLKTLVQG
HHHHHHHHHHHHHCC		25.8522817900
22AcetylationEARKHKLKTLVQGPR
HHHHHHHHHHHCCCC		31.9825381059
22UbiquitinationEARKHKLKTLVQGPR
HHHHHHHHHHHCCCC		31.9823749301
23PhosphorylationARKHKLKTLVQGPRS
HHHHHHHHHHCCCCC		4.3222369663
30PhosphorylationTLVQGPRSYFLDVKC
HHHCCCCCEECCCCC		9.1628889911
31PhosphorylationLVQGPRSYFLDVKCP
HHCCCCCEECCCCCC		60.5021440633
36UbiquitinationRSYFLDVKCPGCLNI
CCEECCCCCCCCEEE		4.7315699485
40MethylationLDVKCPGCLNITTVF
CCCCCCCCEEEEEEE		35.7522650761
70UbiquitinationLCTPTGGKAKLSEGT
EECCCCCCEECCCCC		1.7222817900
72UbiquitinationTPTGGKAKLSEGTSF
CCCCCCEECCCCCCC		18.1723749301
722-HydroxyisobutyrylationTPTGGKAKLSEGTSF
CCCCCCEECCCCCCC		18.17-
72AcetylationTPTGGKAKLSEGTSF
CCCCCCEECCCCCCC		18.1724489116
74PhosphorylationTGGKAKLSEGTSFRR
CCCCEECCCCCCCCC		34.9622369663
77PhosphorylationKAKLSEGTSFRRK--
CEECCCCCCCCCC--		34.8322369663
78PhosphorylationAKLSEGTSFRRK---
EECCCCCCCCCC---		53.3221440633
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 RS27A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS27A_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 RS27A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTC6_YEASTRTC6genetic
20691087
RS27B_YEASTRPS27Bgenetic
22377630
CND2_YEASTBRN1genetic
27708008
UBC3_YEASTCDC34genetic
27708008
SWC4_YEASTSWC4genetic
27708008
SEC22_YEASTSEC22genetic
27708008
CLP1_YEASTCLP1genetic
27708008
LSM2_YEASTLSM2genetic
27708008
CDC27_YEASTCDC27genetic
27708008
APC11_YEASTAPC11genetic
27708008
PRP11_YEASTPRP11genetic
27708008
RPN6_YEASTRPN6genetic
27708008
CDC53_YEASTCDC53genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC1_YEASTCDC1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
RSP5_YEASTRSP5genetic
27708008
CDC20_YEASTCDC20genetic
27708008
PRP18_YEASTPRP18genetic
27708008
TEL2_YEASTTEL2genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
PRP19_YEASTPRP19genetic
27708008
COFI_YEASTCOF1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
PRP24_YEASTPRP24genetic
27708008
LCB1_YEASTLCB1genetic
27708008
DBP6_YEASTDBP6genetic
27708008
SGT1_YEASTSGT1genetic
27708008
SMP3_YEASTSMP3genetic
27708008
APC5_YEASTAPC5genetic
27708008
GPI2_YEASTGPI2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
ARP1_YEASTARP1genetic
27708008
SIC1_YEASTSIC1genetic
27708008
DOM34_YEASTDOM34genetic
27708008
INO4_YEASTINO4genetic
27708008
DIA2_YEASTDIA2genetic
27708008
BECN1_YEASTVPS30genetic
27708008
THI21_YEASTTHI21genetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS27A_YEAST

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Related Literatures of Post-Translational Modification
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-57 AND SER-122, 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-122, AND MASSSPECTROMETRY (S31).
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PROTEIN SEQUENCE OF 43-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-57, UBIQUITINATION AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33;LYS-48 AND LYS-63, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87, AND MASSSPECTROMETRY (S31).
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48 AND LYS-63,AND MASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PROTEIN SEQUENCE OF 43-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-57, UBIQUITINATION AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33;LYS-48 AND LYS-63, AND MASS SPECTROMETRY.

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