Home Page for S100A1

S100A1

Primary information about S100A1:
Basic chemical and physical information	Basic biological information	Basic genomic information	Metal ion binding constants	Interspecies sequence alignment	Information on function
Summary of structural studies	Information on the conformational change	List of available structures	Information about mutations	References about S100A1	Other web resources about S100A1
Additional information about S100A1:
Information about the evolutionary relationship of S100A1 to other proteins

Basic Information

Basic Chemical and Physical Information:
Additional names and abbreviations:	No additional names are stored in the database
Isoforms:	No information about isoforms is stored in the database
Yeast Protein Database Entries:	No links to the YPD are stored in the database

Number of amino acids:	93 (all species) View a list of all sources stored in the database
Molecular weight:	10.374 kD (Mus musculus) - 10.429 kD (Rattus norvegicus) View a list of all sources stored in the database
pI:	not yet available in the data library
Number of functional calcium binding sites:	not yet available in the data library
Macroscopic calcium binding constants:	not yet available in the data library
Other metal binding constants:	not yet available in the data library
Protein stability:	not yet available in the data library
Post-translational modifications:	not yet available in the data library

Basic Biological Information:
Source organisms:	Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus View an annotated list of all sources stored in the database
Tissues:	not yet available in the data library
Subcellular localization:	not yet available in the data library
Regulation:	not yet available in the data library

Genomic Information:
GenBank entries:	View a list of GenBank entries stored in the database
Gene length:	not yet available in the data library
Gene structure:	not yet available in the data library
Promoter:	not yet available in the data library
Gene copies:	not yet available in the data library
Alleles:	no alleles are currently stored in the data library
Chromosomal localization:	Homo sapiens, expressed (GenBank code X58079): q21 region of chromosome 1 (part of the cluster of S100 protein genes) (InfoCard)

Interspecies Sequence Alignment


 
                   |-helixA-|--loop1------|helixB|
                   En**nn**nX**Y*Z**#Ix**zn**nn*n          

HUMAN   : GSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVD
RAT     : GSELETAMETLINVFHAHSGKEGDKYKLSKKELKDLLQTELSSFLDVQKDAD
BOVINE  : GSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDAD

         |-helixC-|--loop2-----|helixD| 
          En**nn**nX*Y*ZG#Ix**zn**nn*n

HUMAN   : AVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
RAT     : AVDKIMKELDENGDGEVDFQEFVVLVAALTVACNNFFWENS
BOVINE  : AVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS

Sequence alignment of the entire S100 subfamily

Functional Information:

General information:

no general functional information is currently stored in the database

Biological roles:

calcium-induced release of calcium from the sarcoplasmic reticulum: is though to stimulate this release
biochemical evidence in Rattus norvegicus: The S100A1 homodimer was found to stimulate calcium-induced calcium release from terminal cisternae isolated from rat skeletal muscles (InfoCard)
microtubule assembly: may inhibit this process
biochemical evidence in Bos taurus: Purified S100B inhibits DMSO-induced assembly of tubulin (InfoCard)

Disease states:

not yet available in the data library

Target molecules:

S100B
biochemical evidence for interaction in Bos taurus: S100A1 and S100B can be isolated as a complex from bovine brain (InfoCard)
adenylate cyclase
biochemical evidence for interaction in Rattus norvegicus: S100A1 was found to stimulate adenylate cyclase activity (InfoCard)
fructose-1,6-bisphosphate aldolase
biochemical evidence for interaction in Rattus norvegicus: interaction of purified aldolase with a mixture of S100A1 and S100B was demonstrated by gel overlay (InfoCard)
glycogen phosphorylase
biochemical evidence for interaction in Rattus norvegicus: purified glyocogen phosphorylase was shown to interact with S100A1 by affinity chromatography and gel overlay (InfoCard)
myoD
biochemical evidence for interaction in Bos taurus: S100A1 was shown to interact with myoD by affinity chromatography and cross-linking experiments (InfoCard)
phosphoglucomutase
biochemical evidence for interaction in Sus scrofa: Affinity chromatography demonstrates that phosphoglucomutase binds to S100A1-Sepharose, and S100A1 binds to phosphoglucomutase-Sepharose in a calcium-dependent manner (InfoCard)
effect of interaction in Sus scrofa: S100A1 inhibits phosphoglucomutase activity in a calcium-dependent manner (InfoCard)
tubulin
biochemical evidence for interaction in Bos taurus: A mixture of S100A1 and S100B was shown to inhibit the assembly of tubulin into microtubules (InfoCard)

Structural Information:

Calcium-coordination:
not yet available in the data library

Nature of the conformational changes:
not yet available in the data library

Secondary structure: (as reported in the PDB file and its accompanying reference)
not yet available in the data library

Additional structural information:
no additional structural information is currently stored in the database

Available structures: (follow the links from the PDB code to the retrieve the PDB files)
no structures are currently stored in the database

Information about mutants:

no mutants are currently stored in the database