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Protein Page:
Calmodulin (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
Calmodulin a calcium-binding small regulatory protein that mediates the control of a large number of enzymes by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Has four functional calcium-binding domains. Phosphorylation and ubiquitination result in a decreased activity. Note: This description may include information from UniProtKB.
Protein type: Calcium-binding protein
Chromosomal Location of Human Ortholog: 14q32.11
Cellular Component: nucleoplasm; spindle pole; centrosome; sarcomere; growth cone; spindle microtubule; cytoplasm; extracellular region; plasma membrane; nucleus; cytosol; vesicle
Molecular Function: protein domain specific binding; nitric-oxide synthase regulator activity; titin binding; calcium ion binding; protein kinase binding; calcium-dependent protein binding; protein serine/threonine kinase activator activity; protein binding; N-terminal myristoylation domain binding; phospholipase binding; thioesterase binding; phosphoinositide 3-kinase binding; type 3 metabotropic glutamate receptor binding; nitric-oxide synthase binding; adenylate cyclase binding
Biological Process: positive regulation of phosphoprotein phosphatase activity; phototransduction, visible light; inositol phosphate metabolic process; nerve growth factor receptor signaling pathway; pathogenesis; signal transduction; nitric oxide metabolic process; positive regulation of protein amino acid dephosphorylation; synaptic transmission; platelet degranulation; substantia nigra development; muscle contraction; positive regulation of cyclic nucleotide metabolic process; response to corticosterone stimulus; epidermal growth factor receptor signaling pathway; platelet activation; mitochondrion organization and biogenesis; fibroblast growth factor receptor signaling pathway; glycogen catabolic process; regulation of heart rate; organelle organization and biogenesis; positive regulation of nitric-oxide synthase activity; adenylate cyclase activation; response to amphetamine; glucose metabolic process; positive regulation of protein amino acid autophosphorylation; regulation of cytokinesis; rhodopsin mediated signaling; G-protein coupled receptor protein signaling pathway; regulation of rhodopsin mediated signaling; phospholipase C activation; carbohydrate metabolic process; innate immune response; positive regulation of cyclic-nucleotide phosphodiesterase activity; regulation of nitric-oxide synthase activity; detection of calcium ion; vascular endothelial growth factor receptor signaling pathway; response to calcium ion; blood coagulation
Disease: Ventricular Tachycardia, Catecholaminergic Polymorphic, 4
Reference #:  P62158 (UniProtKB)
Alt. Names/Synonyms: CALM; CALM1; CALM2; CALM3; CALML2; Calmodulin; calmodulin 1 (phosphorylase kinase, delta); calmodulin 2 (phosphorylase kinase, delta); calmodulin 3 (phosphorylase kinase, delta); CAM; CAM1; CAM2; CAM3; CAMB; CAMC; CAMI; CAMIII; DD132; PHKD; phosphorylase kinase, delta subunit
Gene Symbols: CALM1, CALM2, CALM3
Molecular weight: 16,838 Da
Basal Isoelectric point: 4.09  Predict pI for various phosphorylation states
Select Structure to View Below

Calmodulin

Protein Structure Not Found.


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Sites Implicated In
protein conformation: S82‑p

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 18 K14-ac EEQIAEFkEAFsLFD
1 1 K14-ub EEQIAEFkEAFsLFD
0 4 S18-p AEFkEAFsLFDkDGD
0 5 K22-ac EAFsLFDkDGDGTIt
0 18 K22-ub EAFsLFDkDGDGTIt
0 1 K22-sc EAFsLFDkDGDGTIt
0 1 T29-p kDGDGTIttkELGTV
0 1 T30-p DGDGTIttkELGTVM
0 1 K31 GDGTIttKELGTVMR
0 77 K31-ub GDGTIttkELGTVMR
1 0 T45 RSLGQNPTEAELQDM
1 0 K76-ac FLTMMARkMkDtDsE
0 4 K76-ub FLTMMARkMkDtDsE
0 3 K78-ac TMMARkMkDtDsEEE
0 8 K78-ub TMMARkMkDtDsEEE
0 1 K78-sc TMMARkMkDtDsEEE
8 2 T80-p MARkMkDtDsEEEIR
6 7 S82-p RkMkDtDsEEEIREA
0 7 K95-ac EAFRVFDkDGNGyIs
0 36 K95-ub EAFRVFDkDGNGyIs
0 1 K95-sc EAFRVFDkDGNGyIs
3 2129 Y100-p FDkDGNGyIsAAELR
5 54 S102-p kDGNGyIsAAELRHV
0 1 T111-p AELRHVMtNLGEkLt
0 5 K116-ac VMtNLGEkLtDEEVD
0 1 K116-m1 VMtNLGEkLtDEEVD
0 1 K116-m2 VMtNLGEkLtDEEVD
9 8 K116-m3 VMtNLGEkLtDEEVD
3 0 T118-p tNLGEkLtDEEVDEM
3 20 Y139-p DGDGQVNyEEFVQMM
1 0 K149-ac FVQMMTAk_______
0 6 K149-ub FVQMMTAk_______
  mouse

 
K14-ac EEQIAEFkEAFsLFD
K14 EEQIAEFKEAFsLFD
S18-p AEFkEAFsLFDkDGD
K22-ac EAFsLFDkDGDGTIT
K22-ub EAFsLFDkDGDGTIT
K22-sc EAFsLFDkDGDGTIT
T29 kDGDGTITTkELGTV
T30 DGDGTITTkELGTVM
K31 GDGTITTKELGTVMR
K31-ub GDGTITTkELGTVMR
T45 RSLGQNPTEAELQDM
K76 FLTMMARKMkDtDsE
K76-ub FLTMMARkMkDtDsE
K78-ac TMMARkMkDtDsEEE
K78-ub TMMARkMkDtDsEEE
K78 TMMARkMKDtDsEEE
T80-p MARkMkDtDsEEEIR
S82-p RkMkDtDsEEEIREA
K95-ac EAFRVFDkDGNGyIs
K95-ub EAFRVFDkDGNGyIs
K95 EAFRVFDKDGNGyIs
Y100-p FDkDGNGyIsAAELR
S102-p kDGNGyIsAAELRHV
T111 AELRHVMTNLGEkLT
K116-ac VMTNLGEkLTDEEVD
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
T118 TNLGEkLTDEEVDEM
Y139 DGDGQVNYEEFVQMM
K149 FVQMMTAK_______
K149 FVQMMTAK_______
  rat

 
K14 EEQIAEFKEAFsLFD
K14 EEQIAEFKEAFsLFD
S18-p AEFKEAFsLFDkDGD
K22-ac EAFsLFDkDGDGTIT
K22 EAFsLFDKDGDGTIT
K22 EAFsLFDKDGDGTIT
T29 kDGDGTITTkELGTV
T30 DGDGTITTkELGTVM
K31-ac GDGTITTkELGTVMR
K31 GDGTITTKELGTVMR
T45-p RSLGQNPtEAELQDM
K76 FLTMMARKMkDtDsE
K76 FLTMMARKMkDtDsE
K78-ac TMMARKMkDtDsEEE
K78 TMMARKMKDtDsEEE
K78 TMMARKMKDtDsEEE
T80-p MARKMkDtDsEEEIR
S82-p RKMkDtDsEEEIREA
K95-ac EAFRVFDkDGNGyIs
K95-ub EAFRVFDkDGNGyIs
K95 EAFRVFDKDGNGyIs
Y100-p FDkDGNGyIsAAELR
S102-p kDGNGyIsAAELRHV
T111 AELRHVMTNLGEkLt
K116 VMTNLGEKLtDEEVD
K116 VMTNLGEKLtDEEVD
K116 VMTNLGEKLtDEEVD
K116-m3 VMTNLGEkLtDEEVD
T118-p TNLGEkLtDEEVDEM
Y139-p DGDGQVNyEEFVQMM
K149 FVQMMTAK_______
K149 FVQMMTAK_______
  chicken

 
K14 EEQIAEFKEAFSLFD
K14 EEQIAEFKEAFSLFD
S18 AEFKEAFSLFDKDGD
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
T29 KDGDGTITTKELGTV
T30 DGDGTITTKELGTVM
K31 GDGTITTKELGTVMR
K31 GDGTITTKELGTVMR
T45 RSLGQNPTEAELQDM
K76 FLTMMARKMKDTDSE
K76 FLTMMARKMKDTDSE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
T80 MARKMKDTDSEEEIR
S82 RKMKDTDSEEEIREA
K95 EAFRVFDKDGNGyIS
K95 EAFRVFDKDGNGyIS
K95 EAFRVFDKDGNGyIS
Y100-p FDKDGNGyISAAELR
S102 KDGNGyISAAELRHV
T111 AELRHVMTNLGEkLT
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116-m3 VMTNLGEkLTDEEVD
T118 TNLGEkLTDEEVDEM
Y139-p DGDGQVNyEEFVQMM
K149 FVQMMTAK_______
K149 FVQMMTAK_______
  sheep

 
K14 EEQIAEFKEAFSLFD
K14 EEQIAEFKEAFSLFD
S18 AEFKEAFSLFDKDGD
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
T29 KDGDGTITTKELGTV
T30 DGDGTITTKELGTVM
K31 GDGTITTKELGTVMR
K31 GDGTITTKELGTVMR
T45 RSLGQNPTEAELQDM
K76 FLTMMARKMKDTDSE
K76 FLTMMARKMKDTDSE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
T80 MARKMKDTDSEEEIR
S82 RKMKDTDSEEEIREA
K95 EAFRVFDKDGNGYIS
K95 EAFRVFDKDGNGYIS
K95 EAFRVFDKDGNGYIS
Y100 FDKDGNGYISAAELR
S102 KDGNGYISAAELRHV
T111 AELRHVMTNLGEkLT
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116-m3 VMTNLGEkLTDEEVD
T118 TNLGEkLTDEEVDEM
Y139 DGDGQVNYEEFVQMM
K149 FVQMMTAK_______
K149 FVQMMTAK_______
  cow

 
K14 EEQIAEFKEAFSLFD
K14 EEQIAEFKEAFSLFD
S18 AEFKEAFSLFDKDGD
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
K22 EAFSLFDKDGDGTIT
T29 KDGDGTITTKELGTV
T30 DGDGTITTKELGTVM
K31 GDGTITTKELGTVMR
K31 GDGTITTKELGTVMR
T45 RSLGQNPTEAELQDM
K76 FLTMMARKMKDTDSE
K76 FLTMMARKMKDTDSE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
K78 TMMARKMKDTDSEEE
T80 MARKMKDTDSEEEIR
S82 RKMKDTDSEEEIREA
K95 EAFRVFDKDGNGYIS
K95 EAFRVFDKDGNGYIS
K95 EAFRVFDKDGNGYIS
Y100 FDKDGNGYISAAELR
S102 KDGNGYISAAELRHV
T111 AELRHVMTNLGEkLT
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116 VMTNLGEKLTDEEVD
K116-m3 VMTNLGEkLTDEEVD
T118 TNLGEkLTDEEVDEM
Y139 DGDGQVNYEEFVQMM
K149 FVQMMTAK_______
K149 FVQMMTAK_______
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