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Protein

Calmodulin

Gene

CMD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca2+. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication.1 Publication

Miscellaneous

This protein has three functional calcium-binding sites.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi21 – 321Add BLAST12
Calcium bindingi57 – 682Add BLAST12
Calcium bindingi94 – 1053Add BLAST12

GO - Molecular functioni

  • calcium-dependent protein binding Source: SGD
  • calcium ion binding Source: SGD
  • mitogen-activated protein kinase binding Source: SGD

GO - Biological processi

  • cell budding Source: SGD
  • cytoskeleton organization Source: SGD
  • endocytosis Source: SGD
  • karyogamy involved in conjugation with cellular fusion Source: SGD
  • lysosomal microautophagy Source: SGD
  • phosphatidylinositol biosynthetic process Source: SGD
  • protein import into nucleus Source: SGD
  • receptor-mediated endocytosis Source: SGD
  • regulation of membrane tubulation Source: SGD
  • spindle pole body organization Source: SGD
  • vacuole fusion, non-autophagic Source: SGD

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29071-MONOMER
ReactomeiR-SCE-111932 CaMK IV-mediated phosphorylation of CREB
R-SCE-111933 Calmodulin induced events
R-SCE-114608 Platelet degranulation
R-SCE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-SCE-203615 eNOS activation
R-SCE-2871809 FCERI mediated Ca+2 mobilization
R-SCE-4086398 Ca2+ pathway
R-SCE-442729 CREB phosphorylation through the activation of CaMKII
R-SCE-442745 Activation of CaMK IV
R-SCE-451308 Activation of Ca-permeable Kainate Receptor
R-SCE-5218920 VEGFR2 mediated vascular permeability
R-SCE-5578775 Ion homeostasis
R-SCE-5607763 CLEC7A (Dectin-1) induces NFAT activation
R-SCE-5626467 RHO GTPases activate IQGAPs
R-SCE-6798695 Neutrophil degranulation
R-SCE-936837 Ion transport by P-type ATPases

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin
Short name:
CaM
Gene namesi
Name:CMD1
Ordered Locus Names:YBR109C
ORF Names:YBR0904
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR109C
SGDiS000000313 CMD1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21D → A: Highly reduced affinity for Ca(2+). 1 Publication1
Mutagenesisi32E → V: Highly reduced affinity for Ca(2+). 1 Publication1
Mutagenesisi57D → A: Highly reduced affinity for Ca(2+). 1 Publication1
Mutagenesisi68E → V: Highly reduced affinity for Ca(2+). 1 Publication1
Mutagenesisi94D → A: Highly reduced affinity for Ca(2+). 1 Publication1
Mutagenesisi105E → V: Highly reduced affinity for Ca(2+). 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1667687

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001983281 – 147CalmodulinAdd BLAST147

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineCombined sources1
Modified residuei102PhosphoserineCombined sources1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06787
PaxDbiP06787
PRIDEiP06787
TopDownProteomicsiP06787

PTM databases

iPTMnetiP06787

Interactioni

Subunit structurei

Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110. Interacts with SPC110.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calcium-dependent protein binding Source: SGD
  • mitogen-activated protein kinase binding Source: SGD

Protein-protein interaction databases

BioGridi32813, 967 interactors
DIPiDIP-536N
IntActiP06787, 68 interactors
MINTiP06787
STRINGi4932.YBR109C

Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 19Combined sources13
Beta strandi25 – 29Combined sources5
Helixi30 – 40Combined sources11
Helixi46 – 54Combined sources9
Beta strandi58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Helixi66 – 73Combined sources8
Helixi82 – 93Combined sources12
Beta strandi95 – 98Combined sources4
Beta strandi100 – 102Combined sources3
Helixi103 – 113Combined sources11
Helixi119 – 129Combined sources11
Beta strandi132 – 137Combined sources6
Helixi138 – 145Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F54NMR-A2-78[»]
1F55NMR-A2-78[»]
1LKJNMR-A2-147[»]
2LHHNMR-A2-121[»]
2LHINMR-A2-147[»]
ProteinModelPortaliP06787
SMRiP06787
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06787

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 43EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini44 – 79EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini81 – 116EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini117 – 147EF-hand 4PROSITE-ProRule annotationAdd BLAST31

Sequence similaritiesi

Belongs to the calmodulin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00760000118901
HOGENOMiHOG000233018
InParanoidiP06787
KOiK02183
OMAiESELTDM
OrthoDBiEOG092C4XFN

Family and domain databases

CDDicd00051 EFh, 2 hits
InterProiView protein in InterPro
IPR011992 EF-hand-dom_pair
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
PfamiView protein in Pfam
PF13499 EF-hand_7, 2 hits
SMARTiView protein in SMART
SM00054 EFh, 3 hits
SUPFAMiSSF47473 SSF47473, 1 hit
PROSITEiView protein in PROSITE
PS00018 EF_HAND_1, 3 hits
PS50222 EF_HAND_2, 3 hits

Sequencei

Sequence statusi: Complete.

P06787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNLTEEQI AEFKEAFALF DKDNNGSISS SELATVMRSL GLSPSEAEVN
60 70 80 90 100
DLMNEIDVDG NHQIEFSEFL ALMSRQLKSN DSEQELLEAF KVFDKNGDGL
110 120 130 140
ISAAELKHVL TSIGEKLTDA EVDDMLREVS DGSGEINIQQ FAALLSK
Length:147
Mass (Da):16,135
Last modified:January 1, 1988 - v1
Checksum:i819ED1AD5D9400D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14760 Genomic DNA Translation: AAA34504.1
AF081667 Genomic DNA Translation: AAC68888.1
X78993 Genomic DNA Translation: CAA55612.1
Z35978 Genomic DNA Translation: CAA85064.1
AY558184 Genomic DNA Translation: AAS56510.1
BK006936 Genomic DNA Translation: DAA07228.1
PIRiA25060 MCBY
RefSeqiNP_009667.1, NM_001178457.1

Genome annotation databases

EnsemblFungiiYBR109C; YBR109C; YBR109C
GeneIDi852406
KEGGisce:YBR109C

Similar proteinsi

Entry informationi

Entry nameiCALM_YEAST
AccessioniPrimary (citable) accession number: P06787
Secondary accession number(s): D6VQA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 23, 2018
This is version 198 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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