Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
S100A10 (mouse)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
S100A10 Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine- specific kinase. Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36. Interacts with SCN10A. Belongs to the S-100 family. Note: This description may include information from UniProtKB.
Protein type: Calcium-binding protein
Cellular Component: extrinsic to plasma membrane; endoplasmic reticulum
Molecular Function: protein binding; calcium ion binding
Biological Process: positive regulation of binding
Reference #:  P08207 (UniProtKB)
Alt. Names/Synonyms: 42C; AA409961; AL024248; CAL12; Cal1l; calcium binding protein A11 (calgizzarin); Calpactin I light chain; Calpactin-1 light chain; Cellular ligand of annexin II; CLP11; OTTMUSP00000024909; p10; p10 protein; p11; Protein S100-A10; S100 calcium binding protein A10 (calgizzarin); S100 calcium binding protein A10 (calpactin); S100 calcium-binding protein A10; S100a10; S10AA
Gene Symbols: S100a10
Molecular weight: 11,186 Da
Basal Isoelectric point: 6.27  Predict pI for various phosphorylation states
Select Structure to View Below

S100A10

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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.


       mouse

 
0 1 K23 FHRFAGDKDHLTKED
0 1 R18 TMMLTFHRFAGDKDH
0 748 H25 RFAGDKDHLTKEDLR
0 29 T27 AGDKDHLTKEDLRVL
0 1 K28 GDKDHLTKEDLRVLM
0 1 K28 GDKDHLTKEDLRVLM
0 5 R37 DLRVLMEREFPGFLE
0 8 R37 DLRVLMEREFPGFLE
0 12 K47-u PGFLENQkDPLAVDk
0 1 K54 kDPLAVDKIMkDLDQ
0 2 K54-u kDPLAVDkIMkDLDQ
0 14 K57-u LAVDkIMkDLDQCRD
0 1 K57 LAVDkIMKDLDQCRD
0 22 Y86 LTIACNDYFVVNMKQ
  human

 
K23-a FHkFAGDkGyLtkED
K18-u TMMFTFHkFAGDkGy
Y25-p kFAGDkGyLtkEDLR
T27-p AGDkGyLtkEDLRVL
K28-a GDkGyLtkEDLRVLM
K28-u GDkGyLtkEDLRVLM
K37-a DLRVLMEkEFPGFLE
K37-u DLRVLMEkEFPGFLE
K47-u PGFLENQkDPLAVDk
K54-a kDPLAVDkIMkDLDQ
K54-u kDPLAVDkIMkDLDQ
K57-u LAVDkIMkDLDQCRD
K57-a LAVDkIMkDLDQCRD
Y86-p LTIACNDyFVVHMKQ
  rat

 
K23 FHRFAGEKNyLTKED
R18 TMMLTFHRFAGEKNy
Y25-p RFAGEKNyLTKEDLR
T27 AGEKNyLTKEDLRVL
K28 GEKNyLTKEDLRVLM
K28 GEKNyLTKEDLRVLM
R37 DLRVLMEREFPGFLE
R37 DLRVLMEREFPGFLE
K47 PGFLENQKDPLAVDK
K54 KDPLAVDKIMKDLDQ
K54 KDPLAVDKIMKDLDQ
K57 LAVDKIMKDLDQCRD
K57 LAVDKIMKDLDQCRD
Y86 LIIACNDYFVVHMKQ
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.