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Protein

Calmodulin

Gene

Calm1

more
Organism
Rattus norvegicus (Rat)
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

  • adenylate cyclase binding Source: RGD
  • calcium channel regulator activity Source: RGD
  • calcium-dependent protein binding Source: RGD
  • calcium ion binding Source: RGD
  • enzyme regulator activity Source: RGD
  • ion channel binding Source: RGD
  • nitric-oxide synthase binding Source: RGD
  • nitric-oxide synthase regulator activity Source: RGD
  • phosphatidylinositol 3-kinase binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein N-terminus binding Source: RGD
  • type 3 metabotropic glutamate receptor binding Source: RGD

GO - Biological processi

  • activation of adenylate cyclase activity Source: RGD
  • calcium-mediated signaling Source: RGD
  • positive regulation of nitric-oxide synthase activity Source: RGD
  • regulation of high voltage-gated calcium channel activity Source: RGD
  • regulation of ryanodine-sensitive calcium-release channel activity Source: RGD
  • regulation of store-operated calcium channel activity Source: RGD
  • response to amphetamine Source: RGD
  • response to corticosterone Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_271496. CREB phosphorylation through the activation of CaMKK.
REACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_275454. Ca2+ pathway.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_281385. Smooth Muscle Contraction.
REACT_288006. Platelet degranulation.
REACT_288103. Activation of CaMK IV.
REACT_296726. VEGFR2 mediated cell proliferation.
REACT_303296. Glycogen breakdown (glycogenolysis).
REACT_305912. eNOS activation.
REACT_308497. CaM pathway.
REACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_313751. Cam-PDE 1 activation.
REACT_333484. CaMK IV-mediated phosphorylation of CREB.
REACT_335974. Calmodulin induced events.
REACT_337505. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_347698. Activation of Ca-permeable Kainate Receptor.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_348359. DARPP-32 events.
REACT_362366. CLEC7A (Dectin-1) induces NFAT activation.
REACT_362390. RHO GTPases activate PAKs.
REACT_362399. RHO GTPases activate IQGAPs.

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 Componentsi: Chromosome 1, Chromosome 6

Organism-specific databases

RGDi2257. Calm1.
2258. Calm2.
2259. Calm3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: Reactome
  • growth cone Source: RGD
  • neuron projection Source: RGD
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

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 residuei111 – 1111PhosphothreonineBy 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

GenevisibleiP62161. RN.

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.
FKBP1BP681062EBI-397530,EBI-6693977From a different organism.
GRB7Q144519EBI-397530,EBI-970191From a different organism.
Hmox2P237112EBI-397530,EBI-2910092
Kcnn2P706042EBI-397530,EBI-1031103
Kcnq2O889434EBI-397530,EBI-7900557
Ryr2B0LPN42EBI-397530,EBI-6694167
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. 16 interactions.
MINTiMINT-268601.
STRINGi10116.ENSRNOP00000063822.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OY4X-ray2.03A3-147[»]
4QNHX-ray2.02R1-149[»]
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.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP62161.
KOiK02183.
OMAiHRISGKA.
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

        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
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_017326.3.
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:
EMBLi
GenBanki
DDBJi
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_017326.3.
NP_114175.1. NM_031969.2.
UniGeneiRn.216430.
Rn.2892.
Rn.4166.
Rn.5968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OY4X-ray2.03A3-147[»]
4QNHX-ray2.02R1-149[»]
ProteinModelPortaliP62161.
SMRiP62161. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246428. 24 interactions.
DIPiDIP-29528N.
IntActiP62161. 16 interactions.
MINTiMINT-268601.
STRINGi10116.ENSRNOP00000063822.

Chemistry

BindingDBiP62161.

PTM databases

PhosphoSiteiP62161.

Proteomic databases

PaxDbiP62161.
PRIDEiP62161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi801.
805.
808.
RGDi2257. Calm1.
2258. Calm2.
2259. Calm3.

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP62161.
KOiK02183.
OMAiHRISGKA.
OrthoDBiEOG7F7WBV.
TreeFamiTF300912.

Enzyme and pathway databases

ReactomeiREACT_271496. CREB phosphorylation through the activation of CaMKK.
REACT_272967. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_275454. Ca2+ pathway.
REACT_276289. CREB phosphorylation through the activation of CaMKII.
REACT_280475. VEGFR2 mediated vascular permeability.
REACT_281385. Smooth Muscle Contraction.
REACT_288006. Platelet degranulation.
REACT_288103. Activation of CaMK IV.
REACT_296726. VEGFR2 mediated cell proliferation.
REACT_303296. Glycogen breakdown (glycogenolysis).
REACT_305912. eNOS activation.
REACT_308497. CaM pathway.
REACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_313751. Cam-PDE 1 activation.
REACT_333484. CaMK IV-mediated phosphorylation of CREB.
REACT_335974. Calmodulin induced events.
REACT_337505. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_337837. Synthesis of IP3 and IP4 in the cytosol.
REACT_340722. FCERI mediated Ca+2 mobilization.
REACT_341785. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_347698. Activation of Ca-permeable Kainate Receptor.
REACT_347820. Translocation of GLUT4 to the plasma membrane.
REACT_348359. DARPP-32 events.
REACT_362366. CLEC7A (Dectin-1) induces NFAT activation.
REACT_362390. RHO GTPases activate PAKs.
REACT_362399. RHO GTPases activate IQGAPs.

Miscellaneous databases

EvolutionaryTraceiP62161.
NextBioi602729.
PROiP62161.

Gene expression databases

GenevisibleiP62161. RN.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 131 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

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 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.