RS5_YEAST - dbPTM
RS5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS5_YEAST
UniProt AC P26783
Protein Name 40S ribosomal protein S5 {ECO:0000303|PubMed:9559554}
Gene Name RPS5 {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 225
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 MSDTEAPVEVQEDFEVVEEFTPVVLATPIPEEVQQAQTEIKLFNKWSFEEVEVKDASLVDYVQVRQPIFVAHTAGRYANKRFRKAQCPIIERLTNSLMMNGRNNGKKLKAVRIIKHTLDIINVLTDQNPIQVVVDAITNTGPREDTTRVGGGGAARRQAVDVSPLRRVNQAIALLTIGAREAAFRNIKTIAETLAEELINAAKGSSTSYAIKKKDELERVAKSNR
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------MSDTEAPVE
------CCCCCCCCC		53.9210601260
2Phosphorylation------MSDTEAPVE
------CCCCCCCCC		53.9219823750
4Phosphorylation----MSDTEAPVEVQ
----CCCCCCCCCHH		27.0919795423
21PhosphorylationFEVVEEFTPVVLATP
CHHHCCCCCEEEEEC		20.6019795423
27PhosphorylationFTPVVLATPIPEEVQ
CCCEEEEECCCHHHH		20.0027214570
38PhosphorylationEEVQQAQTEIKLFNK
HHHHHHHHHHHHHHC		42.5719795423
41UbiquitinationQQAQTEIKLFNKWSF
HHHHHHHHHHHCCCC		40.5722817900
45UbiquitinationTEIKLFNKWSFEEVE
HHHHHHHCCCCEEEE		36.5623749301
45AcetylationTEIKLFNKWSFEEVE
HHHHHHHCCCCEEEE		36.5624489116
47PhosphorylationIKLFNKWSFEEVEVK
HHHHHCCCCEEEEEC		25.1222369663
54UbiquitinationSFEEVEVKDASLVDY
CCEEEEECCCHHCCE		33.7923749301
57PhosphorylationEVEVKDASLVDYVQV
EEEECCCHHCCEEEE		38.7728889911
73PhosphorylationQPIFVAHTAGRYANK
CCEEEEECCCHHHCH		22.5223749301
80UbiquitinationTAGRYANKRFRKAQC
CCCHHHCHHHHHCCC		44.7522817900
84UbiquitinationYANKRFRKAQCPIIE
HHCHHHHHCCCHHHH		39.8523749301
94PhosphorylationCPIIERLTNSLMMNG
CHHHHHHHHHHHHCC		29.0528889911
96PhosphorylationIIERLTNSLMMNGRN
HHHHHHHHHHHCCCC		16.6521440633
115UbiquitinationLKAVRIIKHTLDIIN
HHHHHHHHHHHHHHH		28.3223749301
163PhosphorylationRRQAVDVSPLRRVNQ
HHCCCCCCCHHHHHH		17.4723749301
188UbiquitinationEAAFRNIKTIAETLA
HHHHHHHHHHHHHHH		37.1123749301
189PhosphorylationAAFRNIKTIAETLAE
HHHHHHHHHHHHHHH		22.9421440633
203UbiquitinationEELINAAKGSSTSYA
HHHHHHHCCCCCHHH		57.8423749301
203AcetylationEELINAAKGSSTSYA
HHHHHHHCCCCCHHH		57.8424489116
205PhosphorylationLINAAKGSSTSYAIK
HHHHHCCCCCHHHHH		29.7228889911
206PhosphorylationINAAKGSSTSYAIKK
HHHHCCCCCHHHHHC		30.0023749301
207PhosphorylationNAAKGSSTSYAIKKK
HHHCCCCCHHHHHCH		27.7028889911
208PhosphorylationAAKGSSTSYAIKKKD
HHCCCCCHHHHHCHH		17.9530377154
209PhosphorylationAKGSSTSYAIKKKDE
HCCCCCHHHHHCHHH		16.6628889911
212UbiquitinationSSTSYAIKKKDELER
CCCHHHHHCHHHHHH		45.6723749301
212AcetylationSSTSYAIKKKDELER
CCCHHHHHCHHHHHH		45.6724489116
2122-HydroxyisobutyrylationSSTSYAIKKKDELER
CCCHHHHHCHHHHHH		45.67-
212SuccinylationSSTSYAIKKKDELER
CCCHHHHHCHHHHHH		45.6723954790
213UbiquitinationSTSYAIKKKDELERV
CCHHHHHCHHHHHHH		60.3822817900
214UbiquitinationTSYAIKKKDELERVA
CHHHHHCHHHHHHHH		51.9722817900
2222-HydroxyisobutyrylationDELERVAKSNR----
HHHHHHHHHCC----		45.46-
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 RS5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS5_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 RS5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC23_YEASTSEC23genetic
20101242
UBI4P_YEASTUBI4genetic
15527788
RIO2_YEASTRIO2physical
21283762
UB2D3_HUMANUBE2D3physical
15960978
UBC4_YEASTUBC4physical
17551511
UBC4_YEASTUBC4physical
21076411
UBC4_YEASTUBC4physical
19153599
IF5_YEASTTIF5genetic
24948608
YPK1_YEASTYPK1physical
29352143
RIO2_YEASTRIO2genetic
29352143
SUI1_YEASTSUI1genetic
26134896
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS5_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 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: PROTEIN SEQUENCE OF 2-21, AND 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 THR-27, AND MASSSPECTROMETRY.

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