Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calmodulin

Gene

CALM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

  • calcium ion binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-111932. CaMK IV-mediated phosphorylation of CREB.
R-BTA-111933. Calmodulin induced events.
R-BTA-111957. Cam-PDE 1 activation.
R-BTA-111997. CaM pathway.
R-BTA-114608. Platelet degranulation.
R-BTA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-BTA-180024. DARPP-32 events.
R-BTA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-BTA-203615. eNOS activation.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-2672351. Stimuli-sensing channels.
R-BTA-2871809. FCERI mediated Ca+2 mobilization.
R-BTA-4086398. Ca2+ pathway.
R-BTA-418359. Reduction of cytosolic Ca++ levels.
R-BTA-425561. Sodium/Calcium exchangers.
R-BTA-442717. CREB phosphorylation through the activation of CaMKK.
R-BTA-442729. CREB phosphorylation through the activation of CaMKII.
R-BTA-442745. Activation of CaMK IV.
R-BTA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-BTA-445355. Smooth Muscle Contraction.
R-BTA-451308. Activation of Ca-permeable Kainate Receptor.
R-BTA-5218920. VEGFR2 mediated vascular permeability.
R-BTA-5218921. VEGFR2 mediated cell proliferation.
R-BTA-5576892. Phase 0 - rapid depolarisation.
R-BTA-5578775. Ion homeostasis.
R-BTA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-BTA-5626467. RHO GTPases activate IQGAPs.
R-BTA-5627123. RHO GTPases activate PAKs.
R-BTA-5673001. RAF/MAP kinase cascade.
R-BTA-70221. Glycogen breakdown (glycogenolysis).
R-BTA-936837. Ion transport by P-type ATPases.
R-BTA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL6092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved4 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 residuei82 – 821PhosphoserineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei100 – 1001PhosphotyrosineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei111 – 1111PhosphothreonineBy 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.
PeptideAtlasiP62157.
PRIDEiP62157.

PTM databases

iPTMnetiP62157.

Expressioni

Gene expression databases

BgeeiENSBTAG00000014583.

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. Interacts with SYT7 (By similarity). Interacts with MYO10 and MYO1C (PubMed:11457842, PubMed:8022785).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.
STRINGi9913.ENSBTAP00000036057.

Chemistry

BindingDBiP62157.

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

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62157.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
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.
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.

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...

Protein-protein interaction databases

BioGridi176895. 1 interaction.
544691. 5 interactions.
DIPiDIP-36674N.
IntActiP62157. 100 interactions.
MINTiMINT-1347941.
STRINGi9913.ENSBTAP00000036057.

Chemistry

BindingDBiP62157.
ChEMBLiCHEMBL6092.

PTM databases

iPTMnetiP62157.

Proteomic databases

PaxDbiP62157.
PeptideAtlasiP62157.
PRIDEiP62157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi801.
805.
808.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62157.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG091G0V73.
TreeFamiTF300912.

Enzyme and pathway databases

ReactomeiR-BTA-111932. CaMK IV-mediated phosphorylation of CREB.
R-BTA-111933. Calmodulin induced events.
R-BTA-111957. Cam-PDE 1 activation.
R-BTA-111997. CaM pathway.
R-BTA-114608. Platelet degranulation.
R-BTA-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-BTA-180024. DARPP-32 events.
R-BTA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-BTA-203615. eNOS activation.
R-BTA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-BTA-2672351. Stimuli-sensing channels.
R-BTA-2871809. FCERI mediated Ca+2 mobilization.
R-BTA-4086398. Ca2+ pathway.
R-BTA-418359. Reduction of cytosolic Ca++ levels.
R-BTA-425561. Sodium/Calcium exchangers.
R-BTA-442717. CREB phosphorylation through the activation of CaMKK.
R-BTA-442729. CREB phosphorylation through the activation of CaMKII.
R-BTA-442745. Activation of CaMK IV.
R-BTA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-BTA-445355. Smooth Muscle Contraction.
R-BTA-451308. Activation of Ca-permeable Kainate Receptor.
R-BTA-5218920. VEGFR2 mediated vascular permeability.
R-BTA-5218921. VEGFR2 mediated cell proliferation.
R-BTA-5576892. Phase 0 - rapid depolarisation.
R-BTA-5578775. Ion homeostasis.
R-BTA-5607763. CLEC7A (Dectin-1) induces NFAT activation.
R-BTA-5626467. RHO GTPases activate IQGAPs.
R-BTA-5627123. RHO GTPases activate PAKs.
R-BTA-5673001. RAF/MAP kinase cascade.
R-BTA-70221. Glycogen breakdown (glycogenolysis).
R-BTA-936837. Ion transport by P-type ATPases.
R-BTA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

EvolutionaryTraceiP62157.
PROiP62157.

Gene expression databases

BgeeiENSBTAG00000014583.

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]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.