RSSA_RAT - dbPTM
RSSA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSSA_RAT
UniProt AC P38983
Protein Name 40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03016}
Gene Name Rpsa
Organism Rattus norvegicus (Rat).
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. Coloca
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..
Protein Sequence MSGGLDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTAAQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTEWS
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------MSGGLDVLQ
------CCCCCCEEE
41.3815548204
43PhosphorylationQYIYKRKSDGIYIIN
HHEEEECCCCEEEEE
45.1423984901
52AcetylationGIYIINLKRTWEKLL
CEEEEECCCHHHHHH
43.2122902405
75PhosphorylationIENPADVSVISSRNT
ECCCCCEEEEECCCC
17.8023984901
78PhosphorylationPADVSVISSRNTGQR
CCCEEEEECCCCCHH
22.5323984901
79PhosphorylationADVSVISSRNTGQRA
CCEEEEECCCCCHHH
20.5823984901
82PhosphorylationSVISSRNTGQRAVLK
EEEECCCCCHHHHHH
33.3123984901
89AcetylationTGQRAVLKFAAATGA
CCHHHHHHHHHHCCC
26.76-
89UbiquitinationTGQRAVLKFAAATGA
CCHHHHHHHHHHCCC
26.76-
94PhosphorylationVLKFAAATGATPIAG
HHHHHHHCCCCCCCC
23.7123984901
97PhosphorylationFAAATGATPIAGRFT
HHHHCCCCCCCCCCC
19.3023984901
135PhosphorylationRADHQPLTEASYVNL
CCCCCCCCCCCCCCC
35.8723984901
138PhosphorylationHQPLTEASYVNLPTI
CCCCCCCCCCCCCEE
24.3123984901
139PhosphorylationQPLTEASYVNLPTIA
CCCCCCCCCCCCEEE
10.6223984901

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 RSSA_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 RSSA_RAT !!

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

Oops, there are no PPI records of RSSA_RAT !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Cellular prion protein/laminin receptor: distribution in adultcentral nervous system and characterization of an isoform associatedwith a subtype of cortical neurons.";
Baloui H., von Boxberg Y., Vinh J., Weiss S., Rossier J., Nothias F.,Stettler O.;
Eur. J. Neurosci. 20:2605-2616(2004).
Cited for: PROTEIN SEQUENCE OF 2-11; 43-52; 90-102 AND 156-166, CLEAVAGE OFINITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY,SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.

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