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P62204

- CALM_MOUSE

UniProt

P62204 - CALM_MOUSE

Protein

Calmodulin

Gene

Calm1

more
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi21 – 32121Add
    BLAST
    Calcium bindingi57 – 68122Add
    BLAST
    Calcium bindingi94 – 105123Add
    BLAST
    Calcium bindingi130 – 141124Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: Ensembl
    2. nitric-oxide synthase regulator activity Source: Ensembl
    3. protein binding Source: IntAct
    4. protein phosphatase activator activity Source: Ensembl

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: Ensembl
    2. calcium-mediated signaling Source: Ensembl
    3. detection of calcium ion Source: Ensembl
    4. positive regulation of cyclic-nucleotide phosphodiesterase activity Source: Ensembl
    5. positive regulation of nitric-oxide synthase activity Source: Ensembl
    6. positive regulation of phosphoprotein phosphatase activity Source: Ensembl
    7. positive regulation of protein dephosphorylation Source: Ensembl
    8. positive regulation of ryanodine-sensitive calcium-release channel activity Source: Ensembl
    9. regulation of cardiac muscle contraction Source: Ensembl
    10. regulation of cytokinesis Source: Ensembl
    11. regulation of heart rate Source: Ensembl
    12. regulation of high voltage-gated calcium channel activity Source: Ensembl
    13. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: Ensembl
    14. response to amphetamine Source: Ensembl
    15. response to corticosterone Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_198694. Activation of Ca-permeable Kainate Receptor.
    REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_203795. DARPP-32 events.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_215503. CREB phosphorylation through the activation of CaMKK.
    REACT_215587. Calmodulin induced events.
    REACT_216520. CaMK IV-mediated phosphorylation of CREB.
    REACT_218249. Activation of CaMK IV.
    REACT_221264. eNOS activation.
    REACT_221970. Ca2+ pathway.
    REACT_227001. Cam-PDE 1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calmodulin
    Short name:
    CaM
    Gene namesi
    Name:Calm1
    Synonyms:Calm, Cam, Cam1
    AND
    Name:Calm2
    Synonyms:Cam2, Camb
    AND
    Name:Calm3
    Synonyms:Cam3, Camc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12, UP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:88251. Calm1.
    MGI:103250. Calm2.
    MGI:103249. Calm3.

    Subcellular locationi

    Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole
    Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.By similarity

    GO - Cellular componenti

    1. calcium channel complex Source: Ensembl
    2. centrosome Source: Ensembl
    3. cytosol Source: Reactome
    4. growth cone Source: Ensembl
    5. nucleus Source: Ensembl
    6. plasma membrane Source: Ensembl
    7. sarcomere Source: Ensembl
    8. spindle microtubule Source: Ensembl
    9. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 149148CalmodulinPRO_0000198224Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei22 – 221N6-acetyllysine; alternate1 Publication
    Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei45 – 451Phosphothreonine; by CaMK4By similarity
    Modified residuei95 – 951N6-acetyllysineBy similarity
    Modified residuei100 – 1001Phosphotyrosine1 Publication
    Modified residuei102 – 1021PhosphoserineBy similarity
    Modified residuei116 – 1161N6,N6,N6-trimethyllysineBy similarity
    Modified residuei139 – 1391PhosphotyrosineBy similarity

    Post-translational modificationi

    Ubiquitination results in a strongly decreased activity.By similarity
    Phosphorylation results in a decreased activity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP62204.
    PaxDbiP62204.
    PRIDEiP62204.

    2D gel databases

    REPRODUCTION-2DPAGEP62204.
    SWISS-2DPAGEP62204.

    PTM databases

    PhosphoSiteiP62204.

    Expressioni

    Gene expression databases

    ArrayExpressiP62204.
    BgeeiP62204.
    CleanExiMM_CALM1.
    MM_CALM2.
    MM_CALM3.
    GenevestigatoriP62204.

    Interactioni

    Subunit structurei

    Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD By similarity. Interacts with USP6; the interaction is calcium dependent By similarity. Interacts with CDK5RAP2. Interacts with SCN5A By similarity. Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport By similarity. Interacts with RYR1 and RYR2. Interacts with MYO5A.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ccp110Q7TSH44EBI-397460,EBI-646843
    Kcnma1Q084604EBI-397460,EBI-1633915
    PPEF1O148292EBI-397460,EBI-2931238From a different organism.
    PPEF2O148302EBI-397460,EBI-2931306From a different organism.

    Protein-protein interaction databases

    BioGridi198454. 13 interactions.
    198455. 3 interactions.
    198456. 1 interaction.
    IntActiP62204. 23 interactions.
    MINTiMINT-4996917.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 43
    Helixi7 – 1913
    Beta strandi22 – 298
    Helixi30 – 323
    Helixi33 – 397
    Helixi46 – 549
    Beta strandi63 – 653
    Helixi66 – 9328
    Beta strandi98 – 1025
    Helixi103 – 11210
    Beta strandi113 – 1153
    Helixi119 – 12810
    Beta strandi131 – 1333
    Beta strandi136 – 1383
    Helixi139 – 1468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DFSelectron microscopy24.00B/C/D/E/F/G/N/O/P/Q/R/S2-149[»]
    2IX7X-ray2.50A/B3-147[»]
    3WFNX-ray1.95B/C/D/E1-149[»]
    4E50X-ray2.70A1-149[»]
    4E53X-ray2.69A/B1-149[»]
    4HEXX-ray2.00A/B1-149[»]
    ProteinModelPortaliP62204.
    SMRiP62204. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62204.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini44 – 7936EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini81 – 11636EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini117 – 14933EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the calmodulin family.Curated
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    GeneTreeiENSGT00690000101867.
    HOVERGENiHBG012180.
    InParanoidiP62204.
    KOiK02183.
    OMAiTEQISEF.
    OrthoDBiEOG7F7WBV.
    PhylomeDBiP62204.
    TreeFamiTF300912.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 2 hits.
    [Graphical view]
    SMARTiSM00054. EFh. 4 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P62204-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ    50
    DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY 100
    ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK 149
    Length:149
    Mass (Da):16,838
    Last modified:January 23, 2007 - v2
    Checksum:i6B4BC3FCDE10727B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261G → N in AAA66182. (PubMed:3384819)Curated
    Sequence conflicti55 – 551E → V in BAE41271. (PubMed:16141072)Curated
    Sequence conflicti69 – 691F → L in BAE40191. (PubMed:16141072)Curated
    Sequence conflicti82 – 821S → G in BAE31439. (PubMed:16141072)Curated
    Sequence conflicti82 – 821S → G in BAE31644. (PubMed:16141072)Curated
    Sequence conflicti82 – 821S → G in BAE31442. (PubMed:16141072)Curated
    Sequence conflicti126 – 1261I → T in BAE31579. (PubMed:16141072)Curated
    Sequence conflicti142 – 1421F → S in BAC39089. (PubMed:16141072)Curated
    Sequence conflicti143 – 1431V → L in BAB28959. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19380 mRNA. Translation: AAA66181.1.
    M19381 mRNA. Translation: AAA66182.1.
    L31642 mRNA. Translation: AAA65934.1.
    M27844 Genomic DNA. Translation: AAA37365.1.
    AY902353 Genomic DNA. Translation: AAY21063.1.
    X61432 mRNA. Translation: CAA43674.1.
    AK004673 mRNA. Translation: BAB23462.1.
    AK012247 mRNA. Translation: BAB28116.1.
    AK012564 mRNA. Translation: BAB28319.1.
    AK013068 mRNA. Translation: BAB28631.1.
    AK013695 mRNA. Translation: BAB28959.1.
    AK083996 mRNA. Translation: BAC39089.2.
    AK088141 mRNA. Translation: BAC40168.1.
    AK150288 mRNA. Translation: BAE29443.1.
    AK150978 mRNA. Translation: BAE30007.1.
    AK151001 mRNA. Translation: BAE30025.1.
    AK151552 mRNA. Translation: BAE30497.1.
    AK151610 mRNA. Translation: BAE30549.1.
    AK151784 mRNA. Translation: BAE30686.1.
    AK151923 mRNA. Translation: BAE30801.1.
    AK151992 mRNA. Translation: BAE30856.1.
    AK152148 mRNA. Translation: BAE30984.1.
    AK152303 mRNA. Translation: BAE31109.1.
    AK152715 mRNA. Translation: BAE31439.1.
    AK152719 mRNA. Translation: BAE31442.1.
    AK152754 mRNA. Translation: BAE31469.1.
    AK152850 mRNA. Translation: BAE31543.1.
    AK152897 mRNA. Translation: BAE31579.1.
    AK153004 mRNA. Translation: BAE31644.1.
    AK153179 mRNA. Translation: BAE31782.1.
    AK153348 mRNA. Translation: BAE31924.1.
    AK153426 mRNA. Translation: BAE31985.1.
    AK153546 mRNA. Translation: BAE32083.1.
    AK159762 mRNA. Translation: BAE35353.1.
    AK160057 mRNA. Translation: BAE35595.1.
    AK160508 mRNA. Translation: BAE35832.1.
    AK160636 mRNA. Translation: BAE35930.1.
    AK161268 mRNA. Translation: BAE36280.1.
    AK161302 mRNA. Translation: BAE36309.1.
    AK161984 mRNA. Translation: BAE36667.1.
    AK162314 mRNA. Translation: BAE36849.1.
    AK166308 mRNA. Translation: BAE38695.1.
    AK167353 mRNA. Translation: BAE39452.1.
    AK168002 mRNA. Translation: BAE39990.1.
    AK168241 mRNA. Translation: BAE40191.1.
    AK168663 mRNA. Translation: BAE40516.1.
    AK168741 mRNA. Translation: BAE40582.1.
    AK168803 mRNA. Translation: BAE40633.1.
    AK169027 mRNA. Translation: BAE40819.1.
    AK169055 mRNA. Translation: BAE40843.1.
    AK169640 mRNA. Translation: BAE41271.1.
    BC010730 mRNA. Translation: AAH10730.1.
    BC021347 mRNA. Translation: AAH21347.1.
    BC050926 mRNA. Translation: AAH50926.1.
    BC051444 mRNA. Translation: AAH51444.1.
    BC054805 mRNA. Translation: AAH54805.1.
    BC100301 mRNA. Translation: AAI00302.1.
    CCDSiCCDS36523.1.
    CCDS37716.1.
    CCDS39789.1.
    PIRiI49567.
    S37707.
    RefSeqiNP_031615.1. NM_007589.5.
    NP_031616.1. NM_007590.3.
    NP_033920.1. NM_009790.4.
    UniGeneiMm.285993.
    Mm.288630.
    Mm.329243.

    Genome annotation databases

    EnsembliENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
    ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
    ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
    GeneIDi12313.
    12314.
    12315.
    KEGGimmu:12313.
    mmu:12314.
    mmu:12315.
    UCSCiuc007osq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19380 mRNA. Translation: AAA66181.1 .
    M19381 mRNA. Translation: AAA66182.1 .
    L31642 mRNA. Translation: AAA65934.1 .
    M27844 Genomic DNA. Translation: AAA37365.1 .
    AY902353 Genomic DNA. Translation: AAY21063.1 .
    X61432 mRNA. Translation: CAA43674.1 .
    AK004673 mRNA. Translation: BAB23462.1 .
    AK012247 mRNA. Translation: BAB28116.1 .
    AK012564 mRNA. Translation: BAB28319.1 .
    AK013068 mRNA. Translation: BAB28631.1 .
    AK013695 mRNA. Translation: BAB28959.1 .
    AK083996 mRNA. Translation: BAC39089.2 .
    AK088141 mRNA. Translation: BAC40168.1 .
    AK150288 mRNA. Translation: BAE29443.1 .
    AK150978 mRNA. Translation: BAE30007.1 .
    AK151001 mRNA. Translation: BAE30025.1 .
    AK151552 mRNA. Translation: BAE30497.1 .
    AK151610 mRNA. Translation: BAE30549.1 .
    AK151784 mRNA. Translation: BAE30686.1 .
    AK151923 mRNA. Translation: BAE30801.1 .
    AK151992 mRNA. Translation: BAE30856.1 .
    AK152148 mRNA. Translation: BAE30984.1 .
    AK152303 mRNA. Translation: BAE31109.1 .
    AK152715 mRNA. Translation: BAE31439.1 .
    AK152719 mRNA. Translation: BAE31442.1 .
    AK152754 mRNA. Translation: BAE31469.1 .
    AK152850 mRNA. Translation: BAE31543.1 .
    AK152897 mRNA. Translation: BAE31579.1 .
    AK153004 mRNA. Translation: BAE31644.1 .
    AK153179 mRNA. Translation: BAE31782.1 .
    AK153348 mRNA. Translation: BAE31924.1 .
    AK153426 mRNA. Translation: BAE31985.1 .
    AK153546 mRNA. Translation: BAE32083.1 .
    AK159762 mRNA. Translation: BAE35353.1 .
    AK160057 mRNA. Translation: BAE35595.1 .
    AK160508 mRNA. Translation: BAE35832.1 .
    AK160636 mRNA. Translation: BAE35930.1 .
    AK161268 mRNA. Translation: BAE36280.1 .
    AK161302 mRNA. Translation: BAE36309.1 .
    AK161984 mRNA. Translation: BAE36667.1 .
    AK162314 mRNA. Translation: BAE36849.1 .
    AK166308 mRNA. Translation: BAE38695.1 .
    AK167353 mRNA. Translation: BAE39452.1 .
    AK168002 mRNA. Translation: BAE39990.1 .
    AK168241 mRNA. Translation: BAE40191.1 .
    AK168663 mRNA. Translation: BAE40516.1 .
    AK168741 mRNA. Translation: BAE40582.1 .
    AK168803 mRNA. Translation: BAE40633.1 .
    AK169027 mRNA. Translation: BAE40819.1 .
    AK169055 mRNA. Translation: BAE40843.1 .
    AK169640 mRNA. Translation: BAE41271.1 .
    BC010730 mRNA. Translation: AAH10730.1 .
    BC021347 mRNA. Translation: AAH21347.1 .
    BC050926 mRNA. Translation: AAH50926.1 .
    BC051444 mRNA. Translation: AAH51444.1 .
    BC054805 mRNA. Translation: AAH54805.1 .
    BC100301 mRNA. Translation: AAI00302.1 .
    CCDSi CCDS36523.1.
    CCDS37716.1.
    CCDS39789.1.
    PIRi I49567.
    S37707.
    RefSeqi NP_031615.1. NM_007589.5.
    NP_031616.1. NM_007590.3.
    NP_033920.1. NM_009790.4.
    UniGenei Mm.285993.
    Mm.288630.
    Mm.329243.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DFS electron microscopy 24.00 B/C/D/E/F/G/N/O/P/Q/R/S 2-149 [» ]
    2IX7 X-ray 2.50 A/B 3-147 [» ]
    3WFN X-ray 1.95 B/C/D/E 1-149 [» ]
    4E50 X-ray 2.70 A 1-149 [» ]
    4E53 X-ray 2.69 A/B 1-149 [» ]
    4HEX X-ray 2.00 A/B 1-149 [» ]
    ProteinModelPortali P62204.
    SMRi P62204. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198454. 13 interactions.
    198455. 3 interactions.
    198456. 1 interaction.
    IntActi P62204. 23 interactions.
    MINTi MINT-4996917.

    Chemistry

    BindingDBi P62204.

    PTM databases

    PhosphoSitei P62204.

    2D gel databases

    REPRODUCTION-2DPAGE P62204.
    SWISS-2DPAGE P62204.

    Proteomic databases

    MaxQBi P62204.
    PaxDbi P62204.
    PRIDEi P62204.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019514 ; ENSMUSP00000019514 ; ENSMUSG00000019370 .
    ENSMUST00000040440 ; ENSMUSP00000048857 ; ENSMUSG00000036438 .
    ENSMUST00000110082 ; ENSMUSP00000105709 ; ENSMUSG00000001175 .
    GeneIDi 12313.
    12314.
    12315.
    KEGGi mmu:12313.
    mmu:12314.
    mmu:12315.
    UCSCi uc007osq.1. mouse.

    Organism-specific databases

    CTDi 801.
    805.
    808.
    MGIi MGI:88251. Calm1.
    MGI:103250. Calm2.
    MGI:103249. Calm3.

    Phylogenomic databases

    eggNOGi COG5126.
    GeneTreei ENSGT00690000101867.
    HOVERGENi HBG012180.
    InParanoidi P62204.
    KOi K02183.
    OMAi TEQISEF.
    OrthoDBi EOG7F7WBV.
    PhylomeDBi P62204.
    TreeFami TF300912.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188266. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_198244. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_198694. Activation of Ca-permeable Kainate Receptor.
    REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_203795. DARPP-32 events.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_215503. CREB phosphorylation through the activation of CaMKK.
    REACT_215587. Calmodulin induced events.
    REACT_216520. CaMK IV-mediated phosphorylation of CREB.
    REACT_218249. Activation of CaMK IV.
    REACT_221264. eNOS activation.
    REACT_221970. Ca2+ pathway.
    REACT_227001. Cam-PDE 1 activation.

    Miscellaneous databases

    ChiTaRSi CALM1. mouse.
    CALM2. mouse.
    CALM3. mouse.
    EvolutionaryTracei P62204.
    NextBioi 280868.
    PROi P62204.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62204.
    Bgeei P62204.
    CleanExi MM_CALM1.
    MM_CALM2.
    MM_CALM3.
    Genevestigatori P62204.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 2 hits.
    [Graphical view ]
    SMARTi SM00054. EFh. 4 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 4 hits.
    PS50222. EF_HAND_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-deficient skeletal muscle."
      Bender P.K., Dedman J.R., Emerson C.P. Jr.
      J. Biol. Chem. 263:9733-9737(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and expression of mouse-brain calmodulin as an activator of Bordetella pertussis adenylate cyclase in Escherichia coli."
      Danchin A., Sezer O., Glaser P., Chalon P., Caput D.
      Gene 80:145-149(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "Genome-wide isolation of growth and obesity QTL using mouse speed congenic strains."
      Farber C.R., Corva P.M., Medrano J.F.
      BMC Genomics 7:102-102(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CAST/EiJ.
      Tissue: Brain.
    4. "A collection of cDNA clones with specific expression patterns in mouse brain."
      Kato K.
      Eur. J. Neurosci. 2:704-711(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J, DBA/2 and NOD.
      Tissue: Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung, Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus and Tongue.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: 129, C57BL/6 and Czech II.
      Tissue: Brain, Mammary tumor, Placenta and Spinal ganglion.
    7. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    8. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    9. "S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
      Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
      J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RYR1 AND RYR2.
    10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features."
      Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M., Cohen C.
      Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.

    Entry informationi

    Entry nameiCALM_MOUSE
    AccessioniPrimary (citable) accession number: P62204
    Secondary accession number(s): P02593
    , P70667, P99014, Q3TEH7, Q3THK5, Q3U6Z5, Q3U7C7, Q498A3, Q61379, Q61380, Q8BNC9, Q91VQ9, Q9D6G4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein has four functional calcium-binding sites.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3