RS8_MOUSE - dbPTM
RS8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS8_MOUSE
UniProt AC P62242
Protein Name 40S ribosomal protein S8
Gene Name Rps8
Organism Mus musculus (Mouse).
Sequence Length 208
Subcellular Localization Cytoplasm. Membrane
Lipid-anchor . Localized in cytoplasmic mRNP granules containing untranslated mRNAs..
Protein Description
Protein Sequence MGISRDNWHKRRKTGGKRKPYHKKRKYELGRPAANTKIGPRRIHTVRVRGGNKKYRALRLDVGNFSWGSECCTRKTRIIDVVYNASNNELVRTKTLVKNCIVLIDSTPYRQWYESHYALPLGRKKGAKLTPEEEEILNKKRSKKIQKKYDERKKNAKISSLLEEQFQQGKLLACIASRPGQCGRADGYVLEGKELEFYLRKIKARKGK
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
2Myristoylation------MGISRDNWH
------CCCCCCCHH
26.95-
4Phosphorylation----MGISRDNWHKR
----CCCCCCCHHHC
28.0523375375
37UbiquitinationGRPAANTKIGPRRIH
CCCCCCCCCCCCEEE
45.5322790023
37AcetylationGRPAANTKIGPRRIH
CCCCCCCCCCCCEEE
45.5323806337
71S-palmitoylationNFSWGSECCTRKTRI
CCCCCHHHCCCCCEE
2.8428526873
71GlutathionylationNFSWGSECCTRKTRI
CCCCCHHHCCCCCEE
2.8424333276
72S-palmitoylationFSWGSECCTRKTRII
CCCCHHHCCCCCEEE
3.4628526873
72GlutathionylationFSWGSECCTRKTRII
CCCCHHHCCCCCEEE
3.4624333276
83PhosphorylationTRIIDVVYNASNNEL
CEEEEEEEECCCCCE
12.5925367039
98UbiquitinationVRTKTLVKNCIVLID
ECCHHHHCCEEEEEC
49.57-
98AcetylationVRTKTLVKNCIVLID
ECCHHHHCCEEEEEC
49.5722826441
100S-palmitoylationTKTLVKNCIVLIDST
CHHHHCCEEEEECCC
1.5628526873
100GlutathionylationTKTLVKNCIVLIDST
CHHHHCCEEEEECCC
1.5624333276
115PhosphorylationPYRQWYESHYALPLG
CCHHHHHHCCCCCCC
13.2029514104
125MalonylationALPLGRKKGAKLTPE
CCCCCCCCCCCCCHH
63.8426320211
128MalonylationLGRKKGAKLTPEEEE
CCCCCCCCCCHHHHH
62.6626320211
128AcetylationLGRKKGAKLTPEEEE
CCCCCCCCCCHHHHH
62.6623806337
128UbiquitinationLGRKKGAKLTPEEEE
CCCCCCCCCCHHHHH
62.66-
128SuccinylationLGRKKGAKLTPEEEE
CCCCCCCCCCHHHHH
62.66-
130PhosphorylationRKKGAKLTPEEEEIL
CCCCCCCCHHHHHHH
28.1325521595
139AcetylationEEEEILNKKRSKKIQ
HHHHHHCHHHHHHHH
46.2323864654
157AcetylationDERKKNAKISSLLEE
HHHHHHHHHHHHHHH
53.1423806337
157SuccinylationDERKKNAKISSLLEE
HHHHHHHHHHHHHHH
53.14-
157MalonylationDERKKNAKISSLLEE
HHHHHHHHHHHHHHH
53.1426320211
157UbiquitinationDERKKNAKISSLLEE
HHHHHHHHHHHHHHH
53.14-
159PhosphorylationRKKNAKISSLLEEQF
HHHHHHHHHHHHHHH
17.7727087446
160PhosphorylationKKNAKISSLLEEQFQ
HHHHHHHHHHHHHHH
40.2125521595
170AcetylationEEQFQQGKLLACIAS
HHHHHHCCEEHHHHC
35.6722826441
170UbiquitinationEEQFQQGKLLACIAS
HHHHHHCCEEHHHHC
35.67-
182GlutathionylationIASRPGQCGRADGYV
HHCCCCCCCCCCCEE
5.0224333276
193AcetylationDGYVLEGKELEFYLR
CCEEECCCCHHHHHH
50.1523236377
193UbiquitinationDGYVLEGKELEFYLR
CCEEECCCCHHHHHH
50.1522790023

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 RS8_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS8_MOUSE !!

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 RS8_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RS8_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS8_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASSSPECTROMETRY.

TOP