Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P62157

- CALM_BOVIN

UniProt

P62157 - CALM_BOVIN

Protein

Calmodulin

Gene

CALM

Organism
Bos taurus (Bovine)
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: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein phosphatase activator activity Source: Ensembl

    GO - Biological processi

    1. detection of calcium ion Source: Ensembl
    2. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    3. positive regulation of cyclic nucleotide metabolic process Source: Ensembl
    4. positive regulation of cyclic-nucleotide phosphodiesterase activity Source: Ensembl
    5. positive regulation of phosphoprotein phosphatase activity Source: Ensembl
    6. positive regulation of protein dephosphorylation Source: Ensembl
    7. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    8. regulation of cardiac muscle contraction Source: Ensembl
    9. regulation of cytokinesis Source: Ensembl
    10. regulation of heart rate Source: Ensembl
    11. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_202422. Calmodulin induced events.
    REACT_205490. DARPP-32 events.
    REACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_209727. Ca2+ pathway.
    REACT_209867. CREB phosphorylation through the activation of CaMKII.
    REACT_209927. CaMK IV-mediated phosphorylation of CREB.
    REACT_212364. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_212942. Cam-PDE 1 activation.
    REACT_213597. Activation of CaMK IV.
    REACT_214174. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_214581. Transcriptional activation of mitochondrial biogenesis.
    REACT_216082. CaM pathway.
    REACT_216829. FCERI mediated Ca+2 mobilization.
    REACT_217010. Smooth Muscle Contraction.
    REACT_217517. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_217718. Translocation of GLUT4 to the plasma membrane.
    REACT_217977. eNOS activation.
    REACT_221074. Activation of Ca-permeable Kainate Receptor.
    REACT_225102. Synthesis of IP3 and IP4 in the cytosol.
    REACT_225885. Glycogen breakdown (glycogenolysis).
    REACT_227054. CREB phosphorylation through the activation of CaMKK.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calmodulin
    Short name:
    CaM
    Gene namesi
    Name:CALM
    Synonyms:CAM
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 10, UP000009136: Chromosome 18

    Subcellular locationi

    Cytoplasm. 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. sarcomere Source: Ensembl
    5. spindle microtubule Source: Ensembl
    6. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 149148CalmodulinPRO_0000198222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei22 – 221N6-acetyllysine; alternateBy similarity
    Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei45 – 451Phosphothreonine; by CaMK4By similarity
    Modified residuei95 – 951N6-acetyllysineBy similarity
    Modified residuei100 – 1001PhosphotyrosineBy similarity
    Modified residuei102 – 1021PhosphoserineBy similarity
    Modified residuei116 – 1161N6,N6,N6-trimethyllysine2 Publications
    Modified residuei139 – 1391PhosphotyrosineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP62157.
    PRIDEiP62157.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACA8Q9LF7914EBI-397403,EBI-980643From a different organism.
    At4g30490Q8L5174EBI-397403,EBI-4439046From a different organism.
    GRB7Q144512EBI-397403,EBI-970191From a different organism.
    Hmox2P237113EBI-397403,EBI-2910092From a different organism.
    LTFP027882EBI-397403,EBI-1058602From a different organism.
    Nos1P294762EBI-397403,EBI-349460From a different organism.
    Nos3Q626002EBI-397403,EBI-7052018From a different organism.
    NOX5Q96PH1-43EBI-397403,EBI-7305642From a different organism.
    STIM1Q135862EBI-397403,EBI-448878From a different organism.

    Protein-protein interaction databases

    BioGridi176895. 1 interaction.
    544691. 5 interactions.
    DIPiDIP-36674N.
    IntActiP62157. 100 interactions.
    MINTiMINT-1347941.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Turni21 – 233
    Beta strandi25 – 284
    Helixi30 – 3910
    Helixi46 – 5611
    Beta strandi61 – 655
    Helixi66 – 7510
    Beta strandi79 – 824
    Helixi83 – 9311
    Beta strandi98 – 1014
    Helixi103 – 11210
    Helixi119 – 12911
    Beta strandi131 – 1388
    Helixi139 – 1468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A29X-ray2.74A2-149[»]
    1AK8NMR-A1-76[»]
    1CDMX-ray2.00A5-148[»]
    1CM1X-ray2.00A2-149[»]
    1CM4X-ray2.00A2-149[»]
    1CMFNMR-A77-149[»]
    1CMGNMR-A77-149[»]
    1DEGX-ray2.90A6-148[»]
    1FW4X-ray1.70A79-149[»]
    1LINX-ray2.00A2-149[»]
    1PRWX-ray1.70A2-149[»]
    1QIVX-ray2.64A2-149[»]
    1QIWX-ray2.30A/B2-149[»]
    1XA5X-ray2.12A2-149[»]
    2CLNmodel-A1-149[»]
    2F2OX-ray2.17A/B1-149[»]
    2F2PX-ray2.60A/B1-149[»]
    2FOTX-ray2.45A2-149[»]
    3IF7X-ray1.60A2-149[»]
    ProteinModelPortaliP62157.
    SMRiP62157. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62157.

    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.
    InParanoidiP62157.
    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.

    P62157-1 [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
    AB099053 mRNA. Translation: BAC56543.1.
    BC105380 mRNA. Translation: AAI05381.1.
    BC120080 mRNA. Translation: AAI20081.1.
    BC123890 mRNA. Translation: AAI23891.1.
    PIRiA90719. MCBO.
    RefSeqiNP_001039714.1. NM_001046249.2.
    NP_001229501.1. NM_001242572.1.
    NP_001229516.1. NM_001242587.1.
    UniGeneiBt.12896.
    Bt.53264.
    Bt.61778.
    Bt.63542.

    Genome annotation databases

    EnsembliENSBTAT00000019411; ENSBTAP00000019411; ENSBTAG00000014583.
    ENSBTAT00000036194; ENSBTAP00000036057; ENSBTAG00000025644.
    GeneIDi100297344.
    520277.
    617095.
    KEGGibta:100297344.
    bta:520277.
    bta:617095.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB099053 mRNA. Translation: BAC56543.1 .
    BC105380 mRNA. Translation: AAI05381.1 .
    BC120080 mRNA. Translation: AAI20081.1 .
    BC123890 mRNA. Translation: AAI23891.1 .
    PIRi A90719. MCBO.
    RefSeqi NP_001039714.1. NM_001046249.2.
    NP_001229501.1. NM_001242572.1.
    NP_001229516.1. NM_001242587.1.
    UniGenei Bt.12896.
    Bt.53264.
    Bt.61778.
    Bt.63542.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A29 X-ray 2.74 A 2-149 [» ]
    1AK8 NMR - A 1-76 [» ]
    1CDM X-ray 2.00 A 5-148 [» ]
    1CM1 X-ray 2.00 A 2-149 [» ]
    1CM4 X-ray 2.00 A 2-149 [» ]
    1CMF NMR - A 77-149 [» ]
    1CMG NMR - A 77-149 [» ]
    1DEG X-ray 2.90 A 6-148 [» ]
    1FW4 X-ray 1.70 A 79-149 [» ]
    1LIN X-ray 2.00 A 2-149 [» ]
    1PRW X-ray 1.70 A 2-149 [» ]
    1QIV X-ray 2.64 A 2-149 [» ]
    1QIW X-ray 2.30 A/B 2-149 [» ]
    1XA5 X-ray 2.12 A 2-149 [» ]
    2CLN model - A 1-149 [» ]
    2F2O X-ray 2.17 A/B 1-149 [» ]
    2F2P X-ray 2.60 A/B 1-149 [» ]
    2FOT X-ray 2.45 A 2-149 [» ]
    3IF7 X-ray 1.60 A 2-149 [» ]
    ProteinModelPortali P62157.
    SMRi P62157. Positions 1-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 176895. 1 interaction.
    544691. 5 interactions.
    DIPi DIP-36674N.
    IntActi P62157. 100 interactions.
    MINTi MINT-1347941.

    Chemistry

    BindingDBi P62157.
    ChEMBLi CHEMBL6092.

    Proteomic databases

    PaxDbi P62157.
    PRIDEi P62157.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000019411 ; ENSBTAP00000019411 ; ENSBTAG00000014583 .
    ENSBTAT00000036194 ; ENSBTAP00000036057 ; ENSBTAG00000025644 .
    GeneIDi 100297344.
    520277.
    617095.
    KEGGi bta:100297344.
    bta:520277.
    bta:617095.

    Organism-specific databases

    CTDi 801.
    805.
    808.

    Phylogenomic databases

    eggNOGi COG5126.
    GeneTreei ENSGT00690000101867.
    HOVERGENi HBG012180.
    InParanoidi P62157.
    KOi K02183.
    OMAi TEQISEF.
    OrthoDBi EOG7F7WBV.
    TreeFami TF300912.

    Enzyme and pathway databases

    Reactomei REACT_202422. Calmodulin induced events.
    REACT_205490. DARPP-32 events.
    REACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
    REACT_209727. Ca2+ pathway.
    REACT_209867. CREB phosphorylation through the activation of CaMKII.
    REACT_209927. CaMK IV-mediated phosphorylation of CREB.
    REACT_212364. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_212942. Cam-PDE 1 activation.
    REACT_213597. Activation of CaMK IV.
    REACT_214174. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_214581. Transcriptional activation of mitochondrial biogenesis.
    REACT_216082. CaM pathway.
    REACT_216829. FCERI mediated Ca+2 mobilization.
    REACT_217010. Smooth Muscle Contraction.
    REACT_217517. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    REACT_217718. Translocation of GLUT4 to the plasma membrane.
    REACT_217977. eNOS activation.
    REACT_221074. Activation of Ca-permeable Kainate Receptor.
    REACT_225102. Synthesis of IP3 and IP4 in the cytosol.
    REACT_225885. Glycogen breakdown (glycogenolysis).
    REACT_227054. CREB phosphorylation through the activation of CaMKK.

    Miscellaneous databases

    EvolutionaryTracei P62157.
    NextBioi 20873068.

    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. "Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
      Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.
      Mol. Reprod. Dev. 65:9-18(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus and Hereford.
      Tissue: Fetal pons, Ileum and Uterus.
    3. "The amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus."
      Grand R.J.A., Perry S.V.
      FEBS Lett. 92:137-142(1978)
      Cited for: PROTEIN SEQUENCE OF 2-149.
      Tissue: Uterus.
    4. "Determination of the complete amino acid sequence of calmodulin (phenylalanine-rich acidic protein II) from bovine brain."
      Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.
      Biomed. Res. 1:248-264(1980)
      Cited for: PROTEIN SEQUENCE OF 2-149.
      Tissue: Brain.
    5. "The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain."
      Watterson D.M., Sharief F., Vanaman T.C.
      J. Biol. Chem. 255:962-975(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
      Tissue: Brain.
    6. "Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin."
      Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E., Jennissen H.P.
      Eur. J. Biochem. 255:422-431(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-28, UBIQUITINATION AT LYS-22.
    7. "Heat-resistant inhibitors of protein kinase C from bovine brain."
      Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W., Tripier D., Hucho F.
      Eur. J. Biochem. 177:657-664(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 39-61.
    8. Weise C.
      Unpublished observations (OCT-2002)
      Cited for: METHYLATION AT LYS-116.
    9. Cited for: INTERACTION WITH MYO1C.
    10. Cited for: INTERACTION WITH MYO10.
    11. "Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin-C."
      Strynadka N.C.J., James M.N.G.
      Proteins 3:1-17(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF TRIMETHYLATED CALMODULIN.
    12. "Solution structure of the paramagnetic complex of the N-terminal domain of calmodulin with two Ce3+ ions by 1H NMR."
      Bentrop D., Bertini I., Cremonini M.A., Forsen S., Luchinat C., Malmendal A.
      Biochemistry 36:11605-11618(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-75.
    13. "The structure of apo-calmodulin. A 1H NMR examination of the carboxy-terminal domain."
      Finn B.E., Drakenberg T., Forsen S.
      FEBS Lett. 336:368-374(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 77-149.
    14. "Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex."
      Meador W.E., Means A.R., Quiocho F.A.
      Science 257:1251-1255(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
    15. "Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures."
      Meador W.E., Means A.R., Quiocho F.A.
      Science 262:1718-1721(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-148.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 6-148 GLU-85 DEL.
    17. "Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex."
      Cook W.J., Walter L.J., Walter M.R.
      Biochemistry 33:15259-15265(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
    18. "Trifluoperazine-induced conformational change in Ca(2+)-calmodulin."
      Vandonselaar M., Hickie R.A., Quail J.W., Delbaere L.T.
      Nat. Struct. Biol. 1:795-801(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-149.
    19. "Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering."
      Wall M.E., Clarage J.B., Phillips G.N.
      Structure 5:1599-1612(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-147.
    20. "Structure of Escherichia coli fragment TR2C from calmodulin to 1.7 A resolution."
      Olsson L.L., Sjolin L.
      Acta Crystallogr. D 57:664-669(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 79-149.

    Entry informationi

    Entry nameiCALM_BOVIN
    AccessioniPrimary (citable) accession number: P62157
    Secondary accession number(s): P02593
    , P70667, P99014, Q08D84, Q2KJE6, 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