S10A1_RAT - dbPTM
S10A1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S10A1_RAT
UniProt AC P35467
Protein Name Protein S100-A1
Gene Name S100a1
Organism Rattus norvegicus (Rat).
Sequence Length 94
Subcellular Localization Cytoplasm .
Protein Description Probably acts as a Ca(2+) signal transducer (By similarity). In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. [PubMed: 16169012]
Protein Sequence MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDADAVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS
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
86S-nitrosocysteineVAALTVACNNFFWEN
HHHHHHHHHHHHCCC
3.58-
86S-nitrosylationVAALTVACNNFFWEN
HHHHHHHHHHHHCCC
3.58-

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 S10A1_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S10A1_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 S10A1_RAT !!

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

Oops, there are no PPI records of S10A1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of S10A1_RAT

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Related Literatures of Post-Translational Modification

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