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P62161

- CALM_RAT

UniProt

P62161 - CALM_RAT

Protein

Calmodulin

Gene

Calm1

more
Organism
Rattus norvegicus (Rat)
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. adenylate cyclase binding Source: RGD
    2. calcium channel regulator activity Source: RGD
    3. calcium-dependent protein binding Source: RGD
    4. calcium ion binding Source: RGD
    5. enzyme regulator activity Source: RGD
    6. ion channel binding Source: RGD
    7. nitric-oxide synthase binding Source: RGD
    8. nitric-oxide synthase regulator activity Source: RGD
    9. phosphatidylinositol 3-kinase binding Source: RGD
    10. protein binding Source: UniProtKB
    11. protein domain specific binding Source: RGD
    12. protein N-terminus binding Source: RGD
    13. protein phosphatase activator activity Source: Ensembl
    14. type 3 metabotropic glutamate receptor binding Source: RGD

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: RGD
    2. calcium-mediated signaling Source: RGD
    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: RGD
    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: RGD
    13. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: Ensembl
    14. regulation of ryanodine-sensitive calcium-release channel activity Source: RGD
    15. regulation of store-operated calcium channel activity Source: RGD
    16. response to amphetamine Source: RGD
    17. response to corticosterone Source: RGD

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_194690. Ca2+ pathway.
    REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196392. CREB phosphorylation through the activation of CaMKII.
    REACT_196422. Activation of Ca-permeable Kainate Receptor.
    REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
    REACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199176. Translocation of GLUT4 to the plasma membrane.
    REACT_203734. FCERI mediated Ca+2 mobilization.
    REACT_211910. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.
    REACT_220327. CaM pathway.
    REACT_224772. Smooth Muscle Contraction.
    REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_227999. Glycogen breakdown (glycogenolysis).

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi2257. Calm1.
    2258. Calm2.
    2259. 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. cytoplasm Source: RGD
    4. cytosol Source: Reactome
    5. growth cone Source: RGD
    6. neuron projection Source: RGD
    7. nucleoplasm Source: Reactome
    8. nucleus Source: RGD
    9. plasma membrane Source: RGD
    10. sarcomere Source: Ensembl
    11. spindle microtubule Source: Ensembl
    12. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 149148CalmodulinPRO_0000198227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei22 – 221N6-acetyllysine; alternateBy similarity
    Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei45 – 451Phosphothreonine; by CaMK41 Publication
    Modified residuei95 – 951N6-acetyllysineBy similarity
    Modified residuei100 – 1001PhosphotyrosineBy similarity
    Modified residuei102 – 1021PhosphoserineBy similarity
    Modified residuei116 – 1161N6,N6,N6-trimethyllysine1 Publication
    Modified residuei139 – 1391PhosphotyrosineBy similarity

    Post-translational modificationi

    Ubiquitination results in a strongly decreased activity.By similarity
    Phosphorylation results in a decreased activity.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP62161.
    PRIDEiP62161.

    PTM databases

    PhosphoSiteiP62161.

    Expressioni

    Gene expression databases

    GenevestigatoriP62161.

    Interactioni

    Subunit structurei

    Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10 and MYO5A. Interacts with USP6; the interaction is calcium dependent By similarity. Interacts with CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2 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 By similarity. Interacts with RRAD. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP005336EBI-397530,EBI-297353From a different organism.
    GRB7Q144519EBI-397530,EBI-970191From a different organism.
    Hmox2P237112EBI-397530,EBI-2910092
    Kcnn2P706042EBI-397530,EBI-1031103
    Kcnq2O889434EBI-397530,EBI-7900557
    SEC61A1P383774EBI-397530,EBI-8517797From a different organism.
    THOP1P528882EBI-397530,EBI-372399From a different organism.
    Thop1P241552EBI-397530,EBI-6372841

    Protein-protein interaction databases

    BioGridi246428. 24 interactions.
    DIPiDIP-29528N.
    IntActiP62161. 14 interactions.
    MINTiMINT-268601.
    STRINGi10116.ENSRNOP00000022603.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 1913
    Beta strandi24 – 296
    Helixi30 – 323
    Helixi33 – 397
    Helixi46 – 5611
    Beta strandi61 – 655
    Helixi66 – 7611
    Turni79 – 813
    Helixi83 – 919
    Beta strandi97 – 1026
    Helixi103 – 1108
    Helixi113 – 1153
    Helixi119 – 12911
    Beta strandi133 – 1386
    Helixi139 – 1479

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G4YX-ray1.60R2-149[»]
    1NIWX-ray2.05A/C/E/G2-149[»]
    1QX5X-ray2.54B/D/I/J/K/R/T/Y2-149[»]
    1QX7X-ray3.09A/B/I/M/R2-149[»]
    2HQWX-ray1.90A2-149[»]
    2MGUNMR-A2-149[»]
    2PQ3X-ray1.30A2-77[»]
    2YGGX-ray2.23B1-149[»]
    3B32X-ray1.60A2-76[»]
    3BXKX-ray2.55A/C2-149[»]
    3BXLX-ray2.30A2-149[»]
    3CLNX-ray2.20A2-149[»]
    3EK4X-ray2.65A3-149[»]
    3EK7X-ray1.85A3-149[»]
    3EK8X-ray2.80A3-149[»]
    3EKHX-ray2.00A3-149[»]
    3EKJX-ray2.80A3-149[»]
    3EVRX-ray2.00A3-148[»]
    3EVUX-ray1.75A3-148[»]
    3EVVX-ray2.60A3-148[»]
    3IFKX-ray2.03A/B2-91[»]
    3SG2X-ray2.00A3-149[»]
    3SG3X-ray2.10A3-149[»]
    3SG4X-ray2.40A3-149[»]
    3SG5X-ray1.90A3-149[»]
    3SG6X-ray1.70A3-149[»]
    3SG7X-ray1.90A3-149[»]
    3SJQX-ray1.90A/B1-149[»]
    3WLCX-ray2.49A3-149[»]
    3WLDX-ray2.70A3-149[»]
    4EHQX-ray1.90A2-149[»]
    4G27X-ray1.65R1-149[»]
    4G28X-ray1.63R1-149[»]
    4I2YX-ray2.20A/B3-149[»]
    4IL1X-ray3.00A/B/C/D1-149[»]
    4J9YX-ray1.51R1-149[»]
    4J9ZX-ray1.66R1-149[»]
    ProteinModelPortaliP62161.
    SMRiP62161. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62161.

    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.
    HOGENOMiHOG000233018.
    HOVERGENiHBG012180.
    InParanoidiP62161.
    KOiK02183.
    OMAiTEQISEF.
    OrthoDBiEOG7F7WBV.
    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.

    P62161-1 [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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16659 mRNA. Translation: AAA40864.1.
    X13817 mRNA. Translation: CAA32050.1.
    M19312 mRNA. Translation: AAA40862.1.
    M17069 mRNA. Translation: AAA40863.1.
    X13933 mRNA. Translation: CAA32120.1.
    X13931, X13932, X05117 Genomic DNA. Translation: CAA32119.1.
    X13833, X13834, X13835 Genomic DNA. Translation: CAA32062.1.
    X14265 Genomic DNA. Translation: CAA32478.1.
    AF178845 mRNA. Translation: AAD55398.1.
    BC058485 mRNA. Translation: AAH58485.1.
    BC063187 mRNA. Translation: AAH63187.1.
    PIRiS03206. MCRT.
    RefSeqiNP_036650.1. NM_012518.3.
    NP_059022.1. NM_017326.2.
    NP_114175.1. NM_031969.2.
    UniGeneiRn.216430.
    Rn.2892.
    Rn.4166.
    Rn.5968.

    Genome annotation databases

    EnsembliENSRNOT00000022603; ENSRNOP00000022603; ENSRNOG00000016770.
    ENSRNOT00000064679; ENSRNOP00000063822; ENSRNOG00000004060.
    GeneIDi24242.
    24244.
    50663.
    KEGGirno:24242.
    rno:24244.
    rno:50663.
    UCSCiRGD:2257. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16659 mRNA. Translation: AAA40864.1 .
    X13817 mRNA. Translation: CAA32050.1 .
    M19312 mRNA. Translation: AAA40862.1 .
    M17069 mRNA. Translation: AAA40863.1 .
    X13933 mRNA. Translation: CAA32120.1 .
    X13931 , X13932 , X05117 Genomic DNA. Translation: CAA32119.1 .
    X13833 , X13834 , X13835 Genomic DNA. Translation: CAA32062.1 .
    X14265 Genomic DNA. Translation: CAA32478.1 .
    AF178845 mRNA. Translation: AAD55398.1 .
    BC058485 mRNA. Translation: AAH58485.1 .
    BC063187 mRNA. Translation: AAH63187.1 .
    PIRi S03206. MCRT.
    RefSeqi NP_036650.1. NM_012518.3.
    NP_059022.1. NM_017326.2.
    NP_114175.1. NM_031969.2.
    UniGenei Rn.216430.
    Rn.2892.
    Rn.4166.
    Rn.5968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G4Y X-ray 1.60 R 2-149 [» ]
    1NIW X-ray 2.05 A/C/E/G 2-149 [» ]
    1QX5 X-ray 2.54 B/D/I/J/K/R/T/Y 2-149 [» ]
    1QX7 X-ray 3.09 A/B/I/M/R 2-149 [» ]
    2HQW X-ray 1.90 A 2-149 [» ]
    2MGU NMR - A 2-149 [» ]
    2PQ3 X-ray 1.30 A 2-77 [» ]
    2YGG X-ray 2.23 B 1-149 [» ]
    3B32 X-ray 1.60 A 2-76 [» ]
    3BXK X-ray 2.55 A/C 2-149 [» ]
    3BXL X-ray 2.30 A 2-149 [» ]
    3CLN X-ray 2.20 A 2-149 [» ]
    3EK4 X-ray 2.65 A 3-149 [» ]
    3EK7 X-ray 1.85 A 3-149 [» ]
    3EK8 X-ray 2.80 A 3-149 [» ]
    3EKH X-ray 2.00 A 3-149 [» ]
    3EKJ X-ray 2.80 A 3-149 [» ]
    3EVR X-ray 2.00 A 3-148 [» ]
    3EVU X-ray 1.75 A 3-148 [» ]
    3EVV X-ray 2.60 A 3-148 [» ]
    3IFK X-ray 2.03 A/B 2-91 [» ]
    3SG2 X-ray 2.00 A 3-149 [» ]
    3SG3 X-ray 2.10 A 3-149 [» ]
    3SG4 X-ray 2.40 A 3-149 [» ]
    3SG5 X-ray 1.90 A 3-149 [» ]
    3SG6 X-ray 1.70 A 3-149 [» ]
    3SG7 X-ray 1.90 A 3-149 [» ]
    3SJQ X-ray 1.90 A/B 1-149 [» ]
    3WLC X-ray 2.49 A 3-149 [» ]
    3WLD X-ray 2.70 A 3-149 [» ]
    4EHQ X-ray 1.90 A 2-149 [» ]
    4G27 X-ray 1.65 R 1-149 [» ]
    4G28 X-ray 1.63 R 1-149 [» ]
    4I2Y X-ray 2.20 A/B 3-149 [» ]
    4IL1 X-ray 3.00 A/B/C/D 1-149 [» ]
    4J9Y X-ray 1.51 R 1-149 [» ]
    4J9Z X-ray 1.66 R 1-149 [» ]
    ProteinModelPortali P62161.
    SMRi P62161. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246428. 24 interactions.
    DIPi DIP-29528N.
    IntActi P62161. 14 interactions.
    MINTi MINT-268601.
    STRINGi 10116.ENSRNOP00000022603.

    Chemistry

    BindingDBi P62161.

    PTM databases

    PhosphoSitei P62161.

    Proteomic databases

    PaxDbi P62161.
    PRIDEi P62161.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022603 ; ENSRNOP00000022603 ; ENSRNOG00000016770 .
    ENSRNOT00000064679 ; ENSRNOP00000063822 ; ENSRNOG00000004060 .
    GeneIDi 24242.
    24244.
    50663.
    KEGGi rno:24242.
    rno:24244.
    rno:50663.
    UCSCi RGD:2257. rat.

    Organism-specific databases

    CTDi 801.
    805.
    808.
    RGDi 2257. Calm1.
    2258. Calm2.
    2259. Calm3.

    Phylogenomic databases

    eggNOGi COG5126.
    GeneTreei ENSGT00690000101867.
    HOGENOMi HOG000233018.
    HOVERGENi HBG012180.
    InParanoidi P62161.
    KOi K02183.
    OMAi TEQISEF.
    OrthoDBi EOG7F7WBV.
    TreeFami TF300912.

    Enzyme and pathway databases

    Reactomei REACT_194690. Ca2+ pathway.
    REACT_196389. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_196392. CREB phosphorylation through the activation of CaMKII.
    REACT_196422. Activation of Ca-permeable Kainate Receptor.
    REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
    REACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_199176. Translocation of GLUT4 to the plasma membrane.
    REACT_203734. FCERI mediated Ca+2 mobilization.
    REACT_211910. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_216049. Transcriptional activation of mitochondrial biogenesis.
    REACT_220327. CaM pathway.
    REACT_224772. Smooth Muscle Contraction.
    REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_227999. Glycogen breakdown (glycogenolysis).

    Miscellaneous databases

    EvolutionaryTracei P62161.
    NextBioi 602729.
    PROi P62161.

    Gene expression databases

    Genevestigatori P62161.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Structure of a gene for rat calmodulin."
      Nojima H., Hirofumi S.
      J. Mol. Biol. 193:439-445(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Multiple calmodulin mRNA species are derived from two distinct genes."
      Nojima H., Kishi K., Sokabe H.
      Mol. Cell. Biol. 7:1873-1880(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structural organization of multiple rat calmodulin genes."
      Nojima H.
      J. Mol. Biol. 208:269-282(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SHR.
    5. "Molecular cloning of calmodulin mRNA species which are preferentially expressed in neurons in the rat brain."
      Ni B., Rush S., Gurd J.W., Brown I.R.
      Brain Res. Mol. Brain Res. 13:7-17(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Brain.
    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].
      Tissue: Pituitary.
    7. "Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins."
      Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.
      J. Biol. Chem. 253:343-346(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
      Tissue: Testis.
    8. Lubec G., Chen W.-Q., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.
    9. "Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV."
      Ishida A., Kameshita I., Okuno S., Kitani T., Fujisawa H.
      Arch. Biochem. Biophys. 407:72-82(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-45.
    10. Cited for: INTERACTION WITH RRAD.
    11. Lubec G., Chen W.-Q.
      Submitted (FEB-2007) to UniProtKB
      Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    13. "Structure of calmodulin refined at 2.2-A resolution."
      Babu Y.S., Bugg C.E., Cook W.J.
      J. Mol. Biol. 204:191-204(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    14. "Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode."
      Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y., London R.E., Birnbaumer L.
      J. Biol. Chem. 287:43030-43041(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ORAI1, INTERACTION WITH ORAI1.

    Entry informationi

    Entry nameiCALM_RAT
    AccessioniPrimary (citable) accession number: P62161
    Secondary accession number(s): P02593
    , P70667, P99014, Q61379, Q61380
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3