RS14A_YEAST - dbPTM
RS14A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS14A_YEAST
UniProt AC P06367
Protein Name 40S ribosomal protein S14-A {ECO:0000303|PubMed:9559554}
Gene Name RPS14A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 137
Subcellular Localization Cytoplasm . Nucleus, nucleolus .
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 uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly]
Protein Sequence MSNVVQARDNSQVFGVARIYASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAAKCKEVGITAVHVKIRATGGTRTKTPGPGGQAALRALARSGLRIGRIEDVTPVPSDSTRKKGGRRGRRL
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------MSNVVQARD
------CCCCEECCC		38.0310601260
2Phosphorylation------MSNVVQARD
------CCCCEECCC		38.0315665377
11PhosphorylationVVQARDNSQVFGVAR
CEECCCCCCEEEEEE		31.8222369663
22PhosphorylationGVARIYASFNDTFVH
EEEEEEEECCCCEEE		13.9624961812
36UbiquitinationHVTDLSGKETIARVT
EEEECCCCCEEEEEC		48.5923749301
43PhosphorylationKETIARVTGGMKVKA
CCEEEEECCCCEEEE		23.5928889911
47UbiquitinationARVTGGMKVKADRDE
EEECCCCEEEECCCC		43.8123749301
49UbiquitinationVTGGMKVKADRDESS
ECCCCEEEECCCCCC		38.7724961812
58PhosphorylationDRDESSPYAAMLAAQ
CCCCCCHHHHHHHHH		14.6721440633
70UbiquitinationAAQDVAAKCKEVGIT
HHHHHHHHCCCCCCE		35.7823749301
72UbiquitinationQDVAAKCKEVGITAV
HHHHHHCCCCCCEEE		55.5223749301
822-HydroxyisobutyrylationGITAVHVKIRATGGT
CCEEEEEEEEECCCC		16.17-
82AcetylationGITAVHVKIRATGGT
CCEEEEEEEEECCCC		16.1724489116
91PhosphorylationRATGGTRTKTPGPGG
EECCCCCCCCCCCCH		38.8223749301
92UbiquitinationATGGTRTKTPGPGGQ
ECCCCCCCCCCCCHH		49.8123749301
922-HydroxyisobutyrylationATGGTRTKTPGPGGQ
ECCCCCCCCCCCCHH		49.81-
93PhosphorylationTGGTRTKTPGPGGQA
CCCCCCCCCCCCHHH		32.6329136822
119PhosphorylationIGRIEDVTPVPSDST
EECEEECCCCCCCCC		30.7822369663
123PhosphorylationEDVTPVPSDSTRKKG
EECCCCCCCCCCCCC		44.4122369663
125PhosphorylationVTPVPSDSTRKKGGR
CCCCCCCCCCCCCCC		34.1522369663
126PhosphorylationTPVPSDSTRKKGGRR
CCCCCCCCCCCCCCC		52.0419779198
128UbiquitinationVPSDSTRKKGGRRGR
CCCCCCCCCCCCCCC		56.7217644757
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 RS14A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS14A_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 RS14A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
RS14B_YEASTRPS14Bgenetic
8293976
RIO2_YEASTRIO2physical
21283762
LTV1_YEASTLTV1physical
21283762
RS14B_YEASTRPS14Bgenetic
22377630
SWF1_YEASTSWF1genetic
27708008
GSH1_YEASTGSH1genetic
27708008
IXR1_YEASTIXR1genetic
27708008
FRE2_YEASTFRE2genetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
YPT7_YEASTYPT7genetic
27708008
TCB3_YEASTTCB3genetic
27708008
LCF1_YEASTFAA1genetic
27708008
NACB1_YEASTEGD1genetic
27708008
SGF11_YEASTSGF11genetic
27708008
SYH1_YEASTSYH1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
S2538_YEASTYDL119Cgenetic
27708008
HBT1_YEASTHBT1genetic
27708008
TRPF_YEASTTRP1genetic
27708008
DOT1_YEASTDOT1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
FCY2_YEASTFCY2genetic
27708008
YGI1_YEASTYGL081Wgenetic
27708008
CWC26_YEASTBUD13genetic
27708008
YGY5_YEASTYGL235Wgenetic
27708008
YG5Q_YEASTYGR273Cgenetic
27708008
SSBP1_YEASTSBP1genetic
27708008
ANS1_YEASTANS1genetic
27708008
EST3_YEASTEST3genetic
27708008
RS14B_YEASTRPS14Bgenetic
27708008
TCTP_YEASTTMA19genetic
27708008
MUD2_YEASTMUD2genetic
27708008
PIR3_YEASTPIR3genetic
27708008
SAC1_YEASTSAC1genetic
27708008
CAF4_YEASTCAF4genetic
27708008
YK21_YEASTYKR041Wgenetic
27708008
HBS1_YEASTHBS1genetic
27708008
RPN13_YEASTRPN13genetic
27708008
AIM34_YEASTAIM34genetic
27708008
MTND_YEASTADI1genetic
27708008
CIN4_YEASTCIN4genetic
27708008
YM39_YEASTYMR166Cgenetic
27708008
NGL2_YEASTNGL2genetic
27708008
DOM34_YEASTDOM34genetic
27708008
MSG5_YEASTMSG5genetic
27708008
TEP1_YEASTTEP1genetic
27708008
KC12_YEASTYCK2genetic
27708008
MDM12_YEASTMDM12genetic
27708008
IRA2_YEASTIRA2genetic
27708008
MSH2_YEASTMSH2genetic
27708008
IZH4_YEASTIZH4genetic
27708008
YO08A_YEASTYOR008C-Agenetic
27708008
HST3_YEASTHST3genetic
27708008
YOR31_YEASTYOR131Cgenetic
27708008
SYC1_YEASTSYC1genetic
27708008
IES4_YEASTIES4genetic
27708008
HAP5_YEASTHAP5genetic
27708008
RMI1_YEASTRMI1genetic
27708008
TRM44_YEASTTRM44genetic
27708008
SVL3_YEASTSVL3genetic
27708008
LCL1_YEASTLCL1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
KES1_YEASTKES1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
CG12_YEASTCLN2genetic
27708008
BRR1_YEASTBRR1genetic
27708008
NCA2_YEASTNCA2genetic
27708008
QCR2_YEASTQCR2genetic
27708008
KAD6_YEASTFAP7physical
27929371
RS26B_YEASTRPS26Bphysical
27929371
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS14A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.
"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 SER-2 BY NATA.
"NH2-terminal acetylation of ribosomal proteins of Saccharomycescerevisiae.";
Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
J. Biol. Chem. 267:5442-5445(1992).
Cited for: ACETYLATION AT SER-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-11 AND SER-125, 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-11, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,AND MASS SPECTROMETRY.

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