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Protein Page:
S100A6 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
S100A6 May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. Belongs to the S-100 family. Note: This description may include information from UniProtKB.
Cellular Component: ruffle; extrinsic to internal side of plasma membrane; perinuclear region of cytoplasm; cytoplasm; nuclear envelope; nucleus; cytosol
Molecular Function: protein binding; protein homodimerization activity; zinc ion binding; ion transmembrane transporter activity; calcium ion binding; tropomyosin binding; calcium-dependent protein binding
Biological Process: positive regulation of fibroblast proliferation; axonogenesis; signal transduction
Reference #:  P06703 (UniProtKB)
Alt. Names/Synonyms: 2A9; 5B10; CABP; CACY; Calcyclin; Growth factor-inducible protein 2A9; MLN 4; PRA; Prolactin receptor-associated protein; Protein S100-A6; S100 calcium binding protein A6; S100 calcium-binding protein A6; S100 calcium-binding protein A6 (calcyclin); S100A6; S10A6
Gene Symbols: S100A6
Molecular weight: 10,180 Da
Basal Isoelectric point: 5.32  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

S100A6

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y19-p LVAIFHKysGREGDK
0 1 S20-p VAIFHKysGREGDKH
0 1 R22 IFHKysGREGDKHTL
0 8 K31-ub GDKHTLSkkELkELI
0 1 K32 DKHTLSkKELkELIQ
0 2 K32-ub DKHTLSkkELkELIQ
0 1 K35-ac TLSkkELkELIQkEL
0 1 K35-ub TLSkkELkELIQkEL
0 1 K35-sc TLSkkELkELIQkEL
0 2 K40-ac ELkELIQkELtIGsk
0 7 K40-ub ELkELIQkELtIGsk
0 1 K40-sc ELkELIQkELtIGsk
0 2 T43-p ELIQkELtIGskLQD
0 5 S46-p QkELtIGskLQDAEI
0 1 K47-ac kELtIGskLQDAEIA
0 39 K47-ub kELtIGskLQDAEIA
0 1 K89-ub LIYNEALkG______
  mouse

 
Y19 LVAIFHKYSGkEGDK
S20 VAIFHKYSGkEGDKH
K22-ac IFHKYSGkEGDKHTL
K31 GDKHTLSKkELKELI
K32-ac DKHTLSKkELKELIQ
K32 DKHTLSKKELKELIQ
K35 TLSKkELKELIQKEL
K35 TLSKkELKELIQKEL
K35 TLSKkELKELIQKEL
K40 ELKELIQKELTIGSk
K40 ELKELIQKELTIGSk
K40 ELKELIQKELTIGSk
T43 ELIQKELTIGSkLQD
S46 QKELTIGSkLQDAEI
K47 KELTIGSKLQDAEIA
K47-ub KELTIGSkLQDAEIA
K89 LIYNEALK_______
  rat

 
Y19 LVAIFHKYSGkEGDK
S20 VAIFHKYSGkEGDKH
K22-ac IFHKYSGkEGDKHTL
K31 GDKHTLSKKELkELI
K32 DKHTLSKKELkELIQ
K32 DKHTLSKKELkELIQ
K35-ac TLSKKELkELIQkEL
K35 TLSKKELKELIQkEL
K35 TLSKKELKELIQkEL
K40-ac ELkELIQkELTIGAk
K40 ELkELIQKELTIGAk
K40 ELkELIQKELTIGAk
T43 ELIQkELTIGAkLQD
A46 QkELTIGAkLQDAEI
K47-ac kELTIGAkLQDAEIA
K47 kELTIGAKLQDAEIA
K89 LIYNEALK_______
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