Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
16838 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Cam3, Camc 
Protein Name
Protein Synonyms/Alias
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. In the I/Lyn mouse strain a mutation on the X chromosome results in a deficiency of the major calmodulin-regulated enzyme in skeletal muscle, phosphorylase kinase. Calmodulin has been identified as the delta-subunit of phosphorylase kinase, and it is estimated that approximately 40% of the total calmodulin in rabbit skeletal muscle is associated with the phosphorylase kinase hexadecamer (alpha, beta, gamma, delta)4. The absence of phosphorylase kinase in I/Lyn skeletal muscle results in a reduction in the total amount of calmodulin. The mechanisms affecting this reduction were investigated by comparing the abundance and heterogeneities in calmodulin mRNAs between normal and phosphorylase kinase-deficient skeletal muscles. The results demonstrate that in normal tissue there are four species of calmodulin mRNA distinguished by their molecular weight. All four of these species are present in the deficient tissue, and none of them are preferentially reduced. However, there is a 54% reduction in all four mRNAs as well as in calmodulin in the deficient skeletal muscle relative to normal skeletal muscle. These results indicate that the expression of calmodulin mRNAs is coordinated with the expression of its major enzyme target in skeletal muscle. PMID: [3384819] 

2. Cloning of higher eukaryotic genes has seldom been performed by complementation of a defective prokaryotic function. This is especially true in the case of functions that are normally absent from the prokaryotic host. We demonstrate here that it is possible to identify by complementation the cDNA from mouse brain, which encodes calmodulin (CaM) synthesis, in spite of the fact that the recipient strain, Escherichia coli, does not normally harbour a CaM function. A three-component cloning procedure in which a gene product requiring CaM for activity, adenylate cyclase from the pathogen Bordetella pertussis, was used to screen a cDNA library for cAMP synthesis in E. coli. The nucleotide sequence of the corresponding cDNA is also reported. PMID: [2551780] 



High growth (hg) modifier and background independent quantitative trait loci (QTL) affecting growth, adiposity and carcass composition were previously identified on mouse chromosomes (MMU) 1, 2, 5, 8, 9, 11 and 17. To confirm and further characterize each QTL, two panels of speed congenic strains were developed by introgressing CAST/EiJ (CAST) QTL alleles onto either mutant C57Bl/6J-hg/hg (HG) or wild type C57Bl/6J (B6) genetic backgrounds. PMID: [16670015] 

4. A total of 950 cDNA clones were randomly selected from mouse cerebellar cDNA libraries, and of these, about 130 clones were found to correspond to mRNAs which were expressed unequally between the cerebellum and other parts of mouse brain. Their distribution patterns in adult mouse brain were analysed by in situ hybridization, and eight clones were found restricted to specific regions of the brain, including four clones specific to cerebellar granule cells and one clone specific to Purkinje cells. Another 27 clones were preferentially expressed in a diverse, but distinctive subpopulation of brain cells. Among them seven clones were especially abundant in specific nuclei, and three in specific fibre bundles. These clones will be useful in defining new subpopulations of brain cells characterized by different gene expression. PMID: [12106288] 

5. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

6. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

7. Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine. PMID: [18034455] 

8. A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs. PMID: [17151196] 

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Calmodulin mediates the control of a large number ofenzymes, ion channels and other proteins by Ca(2+). Among theenzymes to be stimulated by the calmodulin-Ca(2+) complex are anumber of protein kinases and phosphatases. Together with CEP110and centrin, is involved in a genetic pathway that regulates thecentrosome cycle and progression through cytokinesis (Bysimilarity). 
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Subcellular Location
Cytoplasm, cytoskeleton, spindle. Cytoplasm,cytoskeleton, spindle pole. Note=Distributed throughout the cellduring interphase, but during mitosis becomes dramaticallylocalized to the spindle poles and the spindle microtubules (Bysimilarity). 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005813 C:centrosome IEA:Compara.
GO:0005829 C:cytosol TAS:Reactome.
GO:0005876 C:spindle microtubule IEA:Compara.
GO:0000922 C:spindle pole IEA:UniProtKB-SubCell.
GO:0005509 F:calcium ion binding IEA:InterPro.
GO:0032465 P:regulation of cytokinesis IEA:Compara.
GO:0051592 P:response to calcium ion IEA:Compara.
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IPR011992;    EF-hand-like_dom.
IPR018247;    EF_Hand_1_Ca_BS.
IPR018249;    EF_HAND_2.
IPR002048;    EF_hand_Ca-bd.
IPR001125;    Recoverin.
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SM00054;    EFh;    4.
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PS00018;    EF_HAND_1;    4.
PS50222;    EF_HAND_2;    4.
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PR00450;    RECOVERIN.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed.
CHAIN         2    149       Calmodulin.
DOMAIN        8     43       EF-hand 1.
DOMAIN       44     79       EF-hand 2.
DOMAIN       81    116       EF-hand 3.
DOMAIN      117    149       EF-hand 4.
CA_BIND      21     32       1.
CA_BIND      57     68       2.
CA_BIND      94    105       3.
CA_BIND     130    141       4.
MOD_RES       2      2       N-acetylalanine.
MOD_RES      14     14       N6-acetyllysine (By similarity).
MOD_RES      22     22       N6-acetyllysine (By similarity).
MOD_RES      45     45       Phosphothreonine; by CaMK4 (By
MOD_RES      95     95       N6-acetyllysine (By similarity).
MOD_RES     100    100       Phosphotyrosine.
MOD_RES     116    116       N6,N6,N6-trimethyllysine (By similarity).
MOD_RES     139    139       Phosphotyrosine (By similarity).
CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
                             (interchain with G-Cter in ubiquitin) (By
CONFLICT     26     26       G -> N (in Ref. 1; AAA66182).
CONFLICT     55     55       E -> V (in Ref. 5; BAE41271).
CONFLICT     69     69       F -> L (in Ref. 5; BAE40191).
CONFLICT     82     82       S -> G (in Ref. 5; BAE31439/BAE31644/
CONFLICT    126    126       I -> T (in Ref. 5; BAE31579).
CONFLICT    142    142       F -> S (in Ref. 5; BAC39089).
CONFLICT    143    143       V -> L (in Ref. 5; BAB28959).
HELIX         7     20
STRAND       24     29
HELIX        30     32
HELIX        33     39
HELIX        46     54
STRAND       63     65
HELIX        66     78
HELIX        83     91
HELIX       103    112
STRAND      113    115
HELIX       119    128
STRAND      135    137
HELIX       139    145
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Nucleotide Sequence
Length: 722 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 149 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data