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P62157

- CALM_BOVIN

UniProt

P62157 - CALM_BOVIN

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Protein

Calmodulin

Gene

CALM

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

  1. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  2. positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  3. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
Complete GO annotation...

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.
REACT_229952. VEGFR2 mediated cell proliferation.
REACT_236208. VEGFR2 mediated vascular permeability.

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. cytoskeleton Source: UniProtKB-KW
  2. cytosol Source: Reactome
Complete GO annotation...

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 – 2014Combined sources
Turni21 – 233Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 3910Combined sources
Helixi46 – 5611Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 7510Combined sources
Beta strandi79 – 824Combined sources
Helixi83 – 9311Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 11210Combined sources
Helixi119 – 12911Combined sources
Beta strandi131 – 1388Combined sources
Helixi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118901.
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

        10         20         30         40         50
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY
110 120 130 140
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK
Length:149
Mass (Da):16,838
Last modified:January 23, 2007 - v2
Checksum:i6B4BC3FCDE10727B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000118901.
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.
REACT_229952. VEGFR2 mediated cell proliferation.
REACT_236208. VEGFR2 mediated vascular permeability.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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