Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Calmodulin  

UniProtKB / Swiss-Prot ID :  CALM_HUMAN

Gene Name (Synonyms) : 
CALM1, CALM, CAM, CAM1
CALM2, CAM2, CAMB
CALM3, CALML2, CAM3, CAMC, CAMIII  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. 

Protein Function :  Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. 

Protein Sequence MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFL...
Predicted Secondary Structure CCCCCCHHHHHHHHHHHHHHCCCCCCEECHHHHHHHHHHHCCCCCHHHHHHHHHHHCCCCCCEECHHHHH...
Protein Variant
LocationDescription
73M -> T (in dbSNP:rs41389749). VAR_048585
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADQLT
---CCCCCC
17.16UniProtKB
Link-
14N6-acetyllysineIAEFKEAFS
HHHHHHHHH
39.37HPRD
Link
14N6-acetyllysineIAEFKEAFS
HHHHHHHHH
39.37Phosphositeplus
Link
14N6-acetyllysine.IAEFKEAFS
HHHHHHHHH
39.37UniProtKB
Link
22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLFDKDGDG
HHHCCCCCC
57.17Phosphositeplus
Link
22N6-acetyllysineSLFDKDGDG
HHHCCCCCC
57.17HPRD
Link
22N6-acetyllysineSLFDKDGDG
HHHCCCCCC
57.17Phosphositeplus
Link
22N6-acetyllysine.SLFDKDGDG
HHHCCCCCC
57.17UniProtKB
Link
31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TITTKELGT
EECHHHHHH
42.14Phosphositeplus
Link
76N6-acetyllysineMMARKMKDT
HHHHHCCCC
40.54Phosphositeplus
Link
78Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ARKMKDTDS
HHHCCCCCC
61.59Phosphositeplus
Link
78N6,N6,N6-trimethyllysineARKMKDTDS
HHHCCCCCC
61.59MeMo
Link
80PhosphothreonineKMKDTDSEE
HCCCCCCHH
35.59Phosphositeplus
Link
80Phosphothreonine (CK2_group)KMKDTDSEE
HCCCCCCHH
35.59PhosphoELM
Link
82PhosphoserineKDTDSEEEI
CCCCCHHHH
49.34Phosphositeplus
Link
95Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RVFDKDGNG
HHHCCCCCC
56.95Phosphositeplus
Link
95N6-acetyllysineRVFDKDGNG
HHHCCCCCC
56.95HPRD
Link
95N6-acetyllysineRVFDKDGNG
HHHCCCCCC
56.95Phosphositeplus
Link
95N6-acetyllysine.RVFDKDGNG
HHHCCCCCC
56.95UniProtKB
Link
100PhosphotyrosineDGNGYISAA
CCCCCCCHH
8.83Phosphositeplus
Link
100PhosphotyrosineDGNGYISAA
CCCCCCCHH
8.83SysPTM
Link
100Phosphotyrosine (EGFR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine (EGFR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine (EGFR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine (EGFR;INSR;INSR)DGNGYISAA
CCCCCCCHH
8.83PhosphoELM
Link
100Phosphotyrosine (INSR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine (INSR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine (INSR)DGNGYISAA
CCCCCCCHH
8.83HPRD
Link
100Phosphotyrosine.DGNGYISAA
CCCCCCCHH
8.83UniProtKB
Link
102PhosphoserineNGYISAAEL
CCCCCHHHH
16.97HPRD
Link
102PhosphoserineNGYISAAEL
CCCCCHHHH
16.97HPRD
Link
102PhosphoserineNGYISAAEL
CCCCCHHHH
16.97Phosphositeplus
Link
102Phosphoserine (CK2_group)NGYISAAEL
CCCCCHHHH
16.97PhosphoELM
Link
116N6,N6,N6-trimethyllysineNLGEKLTDE
HHCCCCCHH
55.69MeMo
Link
116N6,N6,N6-trimethyllysineNLGEKLTDE
HHCCCCCHH
55.69Phosphositeplus
Link
116N6,N6,N6-trimethyllysine.NLGEKLTDE
HHCCCCCHH
55.69UniProtKB
Link
116N6-acetyllysineNLGEKLTDE
HHCCCCCHH
55.69Phosphositeplus
Link
116N6-methylated lysineNLGEKLTDE
HHCCCCCHH
55.69HPRD
Link
118PhosphothreonineGEKLTDEEV
CCCCCHHHH
53.05Phosphositeplus
Link
139PhosphotyrosineGQVNYEEFV
CEECHHHHH
20.27Phosphositeplus
Link
139Phosphotyrosine (INSR)GQVNYEEFV
CEECHHHHH
20.27HPRD
Link
139Phosphotyrosine.GQVNYEEFV
CEECHHHHH
20.27UniProtKB
Link
149N6-acetyllysineMMTAK
HHHCC
52.27Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IKKA_HUMANphysical interactionMINT-48052MINT14743216
RIPK2_HUMANphysical interactionMINT-49067MINT14743216
RALA_HUMANphysical interactionMINT-15766MINT12034722
RALA_HUMANphysical interactionMINT-15765MINT12034722
RALA_HUMANphysical interactionMINT-15764MINT12034722
RALB_HUMANphysical interactionMINT-16957MINT12034722
RALB_HUMANphysical interactionMINT-16956MINT12034722
RALB_HUMANphysical interactionMINT-16955MINT12034722
TNR1A_HUMANphysical interactionMINT-49341MINT14743216
NFKB1_HUMANphysical interactionMINT-48670MINT14743216
VIPR1_HUMANphysical interactionMINT-51637MINT15670850
CRFR1_HUMANphysical interactionMINT-51638MINT15670850
PACR_HUMANphysical interactionMINT-51636MINT15670850
CANB1_HUMANphysical interactionMINT-58232MINT15757646
NFKB2_HUMANphysical interactionMINT-48738MINT14743216
RELB_HUMANphysical interactionMINT-49007MINT14743216
PTHR1_HUMANphysical interactionMINT-51633MINT15670850
PTHR1_HUMANphysical interactionMINT-51634MINT15670850
TRAF2_HUMANphysical interactionMINT-49550MINT14743216
M3K1_HUMANphysical interactionMINT-48323MINT14743216
FKBP8_HUMANphysical interactionMINT-58233MINT15757646
Q14784_HUMANphysical interactionMINT-63955MINT16169070
TANK_HUMANphysical interactionMINT-48261MINT14743216
M3K3_HUMANphysical interactionMINT-48456MINT14743216
GPVI_HUMANphysical interactionMINT-17793MINT12594225
GPVI_HUMANphysical interactionMINT-17795MINT12594225
TRAF6_HUMANphysical interactionMINT-49596MINT14743216
NEMO_HUMANphysical interactionMINT-48186MINT14743216
NEUM_HUMANphysical interactionDIP:489EDIP8872303
ACTN2_HUMANphysical interactionDIP:31EDIP9009191
AT2B4_HUMANphysical interactionDIP:11001EDIP10493800
EGFR_HUMANphysical interaction
physical interaction
EBI-1256982
EBI-1188138
intact14960328
16799092
CE110_HUMANphysical interaction
physical interaction
EBI-1571831
EBI-1570038
intact17719545
17719545
TNR6_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-518367
EBI-518367
EBI-518
intact14594800
14594800
14594800
14594800
14594800
14594800
14594800
RM20_HUMANphysical interactionEBI-734102
intact16169070
MYO6_HUMANphysical interactionEBI-734105
intact16169070
K1683_HUMANphysical interactionEBI-756661
intact16189514
OBSCN_HUMANphysical interactionEBI-983088
intact11448995
DIRA2_HUMANphysical interactionEBI-911456
intact16512683
TNR1B_HUMANphysical interactionEBI-364708
intact14743216
K1683_HUMANyeast 2-hybridHPRD:00242HPRD16189514
MYO6_HUMANyeast 2-hybridHPRD:00242HPRD16169070
RM20_HUMANyeast 2-hybridHPRD:00242HPRD16169070
RALA_HUMANENSP00000272298STRING
PYGM_HUMANENSP00000272298STRING
ESR1_HUMANENSP00000272298STRING
PYGL_HUMANENSP00000272298STRING
EDF1_HUMANENSP00000272298STRING
CREB1_HUMANENSP00000272298STRING
MYOG_HUMANENSP00000272298STRING
INS_HUMANENSP00000272298STRING
INS_HUMANENSP00000272298STRING
CNN1_HUMANENSP00000272298STRING
KCC1A_HUMANENSP00000272298STRING
SL9A1_HUMANENSP00000272298STRING
KCNN2_HUMANENSP00000272298STRING
TRPC3_HUMANENSP00000272298STRING
TENA_HUMANENSP00000272298STRING
AMPE_HUMANENSP00000272298STRING
ERBB2_HUMANENSP00000272298STRING
EGFR_HUMANENSP00000272298STRING
NEUG_HUMANENSP00000272298STRING
GRIA1_HUMANENSP00000272298STRING
PPE2_HUMANENSP00000272298STRING
PHKG1_HUMANENSP00000272298STRING
NOS3_HUMANENSP00000272298STRING
RAD_HUMANENSP00000272298STRING
GRM5_HUMANENSP00000272298STRING
EF2_HUMANENSP00000272298STRING
KKCC2_HUMANENSP00000272298STRING
KPBB_HUMANENSP00000272298STRING
NOS2A_HUMANENSP00000272298STRING
PHKG2_HUMANENSP00000272298STRING
TNR6_HUMANENSP00000272298STRING
PCNT_HUMANENSP00000272298STRING
RYR1_HUMANENSP00000272298STRING
RASK_HUMANENSP00000291295STRING
IP3KA_HUMANENSP00000291295STRING
IP3KB_HUMANENSP00000291295STRING
ADCY8_HUMANENSP00000291295STRING
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Disease Reference
Kegg disease
OMIM disease
614916Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)
616247Long QT syndrome 14 (LQT14)
616249Long QT syndrome 15 (LQT15)
Drug Reference
DrugBank
DB01429Aprindine
DB01244Bepridil
DB00477Chlorpromazine
DB00527Cinchocaine
DB01023Felodipine
DB04841Flunarizine
DB00623Fluphenazine
DB00753Isoflurane
DB00836Loperamide
DB01065Melatonin
DB00622Nicardipine
DB01115Nifedipine
DB00850Perphenazine
DB00925Phenoxybenzamine
DB01100Pimozide
DB01069Promethazine
DB00831Trifluoperazine
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Complete amino acid sequence of human brain calmodulin.";
Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,Titani K.;
Biochemistry 21:2565-2569(1982).
Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION ATLYS-116.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-22 AND LYS-95, ANDMASS SPECTROMETRY.
Methylation
ReferencePubMed
"Complete amino acid sequence of human brain calmodulin.";
Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,Titani K.;
Biochemistry 21:2565-2569(1982).
Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION ATLYS-116.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures