RSSA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RSSA_MOUSE
• UniProt AC: P14206
• Protein Name: 40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03016}
• Gene Name: Rpsa
• Organism: Mus musculus (Mouse).
• Sequence Length: 295
• Subcellular Localization: Cell membrane. Cytoplasm. Nucleus. 67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Colocaliz
• Protein Description: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity). Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10..
• Protein Sequence: MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS

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
2	Acetylation	------MSGALDVLQ ------CCCCCCHHH	32.54	-
2	Phosphorylation	------MSGALDVLQ ------CCCCCCHHH	32.54	29472430
11	Acetylation	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	22826441
11	Ubiquitination	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	-
11	Succinylation	ALDVLQMKEEDVLKF CCCHHHCCHHHHHHH	45.02	23954790
23	Phosphorylation	LKFLAAGTHLGGTNL HHHHHHCCCCCCCCC	14.81	28059163
28	Phosphorylation	AGTHLGGTNLDFQME HCCCCCCCCCCHHHH	30.70	28059163
39	Phosphorylation	FQMEQYIYKRKSDGI HHHHHHEEEECCCCE	10.37	-
42	Ubiquitination	EQYIYKRKSDGIYII HHHEEEECCCCEEEE	49.07	-
43	Phosphorylation	QYIYKRKSDGIYIIN HHEEEECCCCEEEEE	45.14	26824392
47	Phosphorylation	KRKSDGIYIINLKRT EECCCCEEEEECCCH	10.98	28833060
52	Acetylation	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	22826441
52	Ubiquitination	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	-
52	Succinylation	GIYIINLKRTWEKLL CEEEEECCCHHHHHH	43.21	23954790
57	Acetylation	NLKRTWEKLLLAARA ECCCHHHHHHHHHHH	35.68	22826441
75	Phosphorylation	IENPADVSVISSRNT ECCCCCEEEEECCCC	17.80	23984901
78	Phosphorylation	PADVSVISSRNTGQR CCCEEEEECCCCCHH	22.53	23984901
79	Phosphorylation	ADVSVISSRNTGQRA CCEEEEECCCCCHHH	20.58	23984901
82	Phosphorylation	SVISSRNTGQRAVLK EEEECCCCCHHHHHH	33.31	23984901
89	Malonylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	26320211
89	Ubiquitination	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	27667366
89	Acetylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	23806337
89	Succinylation	TGQRAVLKFAAATGA CCHHHHHHHHHHCCC	26.76	23806337
97	Phosphorylation	FAAATGATPIAGRFT HHHHCCCCCCCCCCC	19.30	-
135	Phosphorylation	RADHQPLTEASYVNL CCCCCCCCCCCCCCC	35.87	22499769
138	Phosphorylation	HQPLTEASYVNLPTI CCCCCCCCCCCCCEE	24.31	22499769
139	Phosphorylation	QPLTEASYVNLPTIA CCCCCCCCCCCCEEE	10.62	26824392
139	Nitration	QPLTEASYVNLPTIA CCCCCCCCCCCCEEE	10.62	-
148	S-palmitoylation	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	28526873
148	S-nitrosylation	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	21278135
148	Glutathionylation	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	24333276
148	S-nitrosocysteine	NLPTIALCNTDSPLR CCCEEEEECCCCCCE	3.68	-
163	S-palmitoylation	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	28526873
163	S-nitrosylation	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	24895380
163	Glutathionylation	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	24333276
163	S-nitrosocysteine	YVDIAIPCNNKGAHS EEEEEEECCCCCHHH	7.77	-
212	Acetylation	RDPEEIEKEEQAAAE CCHHHHHHHHHHHHH	72.68	23954790

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RSSA_MOUSE !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RSSA_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RSSA_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
PubMed: 19367708