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Protein

Calmodulin

Gene

CALM1

more
Organism
Homo sapiens (Human)
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.2 Publications

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
  • ion channel binding Source: BHF-UCL
  • nitric-oxide synthase regulator activity Source: Ensembl
  • N-terminal myristoylation domain binding Source: UniProtKB
  • phospholipase binding Source: BHF-UCL
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • protein phosphatase activator activity Source: BHF-UCL
  • protein serine/threonine kinase activator activity Source: BHF-UCL
  • thioesterase binding Source: UniProtKB
  • titin binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000143933-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12477. eNOS activation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_15334. DARPP-32 events.
REACT_15408. Cam-PDE 1 activation.
REACT_15502. CaMK IV-mediated phosphorylation of CREB.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_188329. CLEC7A (Dectin-1) induces NFAT activation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20558. Smooth Muscle Contraction.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_20652. Activation of CaMK IV.
REACT_20661. CREB phosphorylation through the activation of CaMKK.
REACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_263982. Ca2+ pathway.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264273. VEGFR2 mediated cell proliferation.
REACT_318. Platelet degranulation.
REACT_355347. RHO GTPases activate PAKs.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_9000. Calmodulin induced events.
REACT_9053. CaM pathway.

Protein family/group databases

TCDBi9.C.15.1.1. the animal calmodulin-dependent e.r. secretion pathway (csp) family.

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:CALML2, CAM3, CAMC, CAMIII
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 14, Chromosome 19, Chromosome 2

Organism-specific databases

HGNCiHGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • growth cone Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcomere Source: BHF-UCL
  • spindle microtubule Source: UniProtKB
  • spindle pole Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress.

See also OMIM:614916
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. 1 Publication
VAR_069222
Natural varianti98 – 981N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 Publications
VAR_069223
Long QT syndrome 14 (LQT14)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.

See also OMIM:616247
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901F → L in LQT14. 1 Publication
VAR_073275
Natural varianti130 – 1301D → G in LQT14; reduction in Ca(2+) affinity. 1 Publication
VAR_073278
Natural varianti142 – 1421F → L in LQT14; reduction in Ca(2+) affinity. 1 Publication
VAR_073282
Long QT syndrome 15 (LQT15)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.

See also OMIM:616249
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961D → V in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073276
Natural varianti98 – 981N → I in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073277
Natural varianti98 – 981N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 Publications
VAR_069223
Natural varianti132 – 1321D → E in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073279
Natural varianti134 – 1341D → H in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073280
Natural varianti136 – 1361Q → P in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073281

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

MIMi614916. phenotype.
616247. phenotype.
616249. phenotype.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
PharmGKBiPA26042.

Chemistry

DrugBankiDB01429. Aprindine.
DB01244. Bepridil.
DB00477. Chlorpromazine.
DB00527. Cinchocaine.
DB01023. Felodipine.
DB04841. Flunarizine.
DB00623. Fluphenazine.
DB00753. Isoflurane.
DB00836. Loperamide.
DB01065. Melatonin.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB00850. Perphenazine.
DB00925. Phenoxybenzamine.
DB01100. Pimozide.
DB01069. Promethazine.
DB00831. Trifluoperazine.

Polymorphism and mutation databases

BioMutaiCALM1.
DMDMi49037474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 149148CalmodulinPRO_0000198223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei22 – 221N6-acetyllysine; alternate1 Publication
Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei45 – 451Phosphothreonine; by CaMK4By similarity
Modified residuei95 – 951N6-acetyllysine1 Publication
Modified residuei100 – 1001Phosphotyrosine2 Publications
Modified residuei102 – 1021Phosphoserine2 Publications
Modified residuei111 – 1111Phosphothreonine1 Publication
Modified residuei116 – 1161N6,N6,N6-trimethyllysine1 Publication
Modified residuei139 – 1391Phosphotyrosine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62158.
PaxDbiP62158.
PRIDEiP62158.

2D gel databases

DOSAC-COBS-2DPAGEP62158.
OGPiP02593.
SWISS-2DPAGEP62158.

PTM databases

PhosphoSiteiP62158.

Expressioni

Gene expression databases

BgeeiP62158.
CleanExiHS_CALM1.
HS_CALM2.
ExpressionAtlasiP62158. baseline and differential.
GenevisibleiP62158. HS.

Organism-specific databases

HPAiCAB007790.
CAB018558.
HPA044999.

Interactioni

Subunit structurei

Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY. Interacts with USP6; the interaction is calcium dependent. Interacts with CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2. 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 similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9Z3052EBI-397435,EBI-9084208From a different organism.
ADORA2AP292743EBI-397435,EBI-2902702
ARRB1P494073EBI-397435,EBI-743313
ARRB2P321213EBI-397435,EBI-714559
C11orf65Q8NCR33EBI-397435,EBI-744790
CACNA1CQ1393612EBI-397435,EBI-1038838
CCP110O433039EBI-397435,EBI-1566217
cyaP401368EBI-397435,EBI-457011From a different organism.
DAPK1P533556EBI-397435,EBI-358616
EGFRP005334EBI-397435,EBI-297353
FASP254454EBI-397435,EBI-494743
KCNH1O952594EBI-397435,EBI-2909270
KCNH1O95259-28EBI-397435,EBI-9836801
KIAA1683A0JP073EBI-397435,EBI-10171456
KIAA1683Q9H0B34EBI-397435,EBI-745878
MarcksP266452EBI-397435,EBI-911805From a different organism.
MYO10Q9HD672EBI-397435,EBI-307061
RCHY1Q96PM52EBI-397435,EBI-947779
SCN5AQ145242EBI-397435,EBI-726858
TTNQ8WZ422EBI-397435,EBI-681210
YWHAZP631042EBI-397435,EBI-347088

Protein-protein interaction databases

BioGridi107252. 370 interactions.
107256. 30 interactions.
107259. 31 interactions.
DIPiDIP-31794N.
IntActiP62158. 201 interactions.
MINTiMINT-4999725.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi7 – 2014Combined sources
Beta strandi21 – 233Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 3910Combined sources
Helixi46 – 5611Combined sources
Helixi57 – 593Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 9328Combined sources
Beta strandi94 – 963Combined sources
Beta strandi97 – 1015Combined sources
Helixi103 – 11210Combined sources
Beta strandi113 – 1153Combined sources
Helixi119 – 12911Combined sources
Turni130 – 1323Combined sources
Beta strandi133 – 1386Combined sources
Helixi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJImodel-A5-148[»]
1CDLX-ray2.00A/B/C/D2-148[»]
1CLLX-ray1.70A2-149[»]
1CTRX-ray2.45A2-149[»]
1IWQX-ray2.00A2-149[»]
1J7ONMR-A2-77[»]
1J7PNMR-A83-149[»]
1K90X-ray2.75D/E/F2-149[»]
1K93X-ray2.95D/E/F6-149[»]
1L7ZX-ray2.30A2-149[»]
1LVCX-ray3.60D/E/F1-149[»]
1NKFNMR-A94-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1WRZX-ray2.00A1-149[»]
1XFUX-ray3.35O/P/Q/R/S/T1-149[»]
1XFVX-ray3.35O/P/Q/R/S/T1-149[»]
1XFWX-ray3.40O/P/Q/R/S/T1-149[»]
1XFXX-ray3.20O/P/Q/R/S/T1-149[»]
1XFYX-ray3.30O/P/Q/R/S/T1-149[»]
1XFZX-ray3.25O/P/Q/R/S/T1-149[»]
1Y6WX-ray2.40A2-149[»]
1YR5X-ray1.70A2-149[»]
1YRTX-ray2.10B76-149[»]
1YRUX-ray2.50B76-149[»]
1ZOTX-ray2.20B80-148[»]
1ZUZX-ray1.91A1-149[»]
2BE6X-ray2.00A/B/C1-149[»]
2F3YX-ray1.45A2-149[»]
2F3ZX-ray1.60A2-149[»]
2HF5NMR-A47-113[»]
2I08X-ray2.00A3-79[»]
2JZINMR-A2-149[»]
2K0ENMR-A2-149[»]
2K0FNMR-A2-149[»]
2K0JNMR-A3-149[»]
2K61NMR-A2-149[»]
2KNENMR-A2-149[»]
2KUGNMR-A2-77[»]
2KUHNMR-A83-149[»]
2L53NMR-A2-149[»]
2L7LNMR-A2-149[»]
2LGFNMR-A4-149[»]
2LL6NMR-A2-149[»]
2LL7NMR-A2-149[»]
2LQCNMR-A2-78[»]
2LQPNMR-A79-149[»]
2LV6Other-A2-149[»]
2M0JNMR-A2-149[»]
2M0KNMR-A2-149[»]
2M55NMR-A2-149[»]
2MG5NMR-A2-149[»]
2R28X-ray1.86A/B1-149[»]
2V01X-ray2.15A2-149[»]
2V02X-ray2.20A2-149[»]
2VAYX-ray1.94A4-149[»]
2W73X-ray1.45A/B/E/F1-149[»]
2WELX-ray1.90D1-149[»]
2X0GX-ray2.20B2-149[»]
2Y4VX-ray1.80A1-149[»]
3BYAX-ray1.85A2-149[»]
3DVEX-ray2.35A2-149[»]
3DVJX-ray2.80A2-149[»]
3DVKX-ray2.30A2-149[»]
3DVMX-ray2.60A2-149[»]
3EWTX-ray2.40A2-149[»]
3EWVX-ray2.60A2-149[»]
3G43X-ray2.10A/B/C/D2-149[»]
3HR4X-ray2.50B/D/F/H1-149[»]
3J41electron microscopy25.0E/F1-149[»]
3O77X-ray2.35A1-149[»]
3O78X-ray2.60A/B3-149[»]
3OXQX-ray2.55A/B/C/D1-149[»]
3SUIX-ray1.95A1-149[»]
3UCTX-ray1.90A/B2-80[»]
3UCWX-ray1.76A/B/C/D2-80[»]
3UCYX-ray1.80A2-80[»]
4BW7X-ray1.81A/C1-149[»]
4BW8X-ray1.80A/B1-149[»]
4BYFX-ray2.74B/D1-149[»]
4DCKX-ray2.20B1-149[»]
4DJCX-ray1.35A1-149[»]
4GOWX-ray2.60D4-147[»]
4JPZX-ray3.02C/I1-149[»]
4JQ0X-ray3.84C1-149[»]
4L79X-ray2.30B1-149[»]
4LZXX-ray1.50A2-149[»]
4M1LX-ray2.10A2-149[»]
4OVNX-ray2.80A/B/C/D/E1-149[»]
4Q57X-ray1.80A10-74[»]
4Q5UX-ray1.95A1-149[»]
4UMOX-ray3.00C/D1-149[»]
4UPUX-ray2.34A2-149[»]
4V0CX-ray2.86C/D1-149[»]
ProteinModelPortaliP62158.
SMRiP62158. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62158.

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.
InParanoidiP62158.
KOiK02183.
OMAiKSHCRIL.
PhylomeDBiP62158.
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.

P62158-1 [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 cautioni

The sequence CAA36839.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241E → Q in AAH08437 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541N → I in CPVT4; the mutant has significantly reduced Ca(2+) affinity compared to wild-type. 1 Publication
VAR_069222
Natural varianti73 – 731M → T.
Corresponds to variant rs41389749 [ dbSNP | Ensembl ].
VAR_048585
Natural varianti90 – 901F → L in LQT14. 1 Publication
VAR_073275
Natural varianti96 – 961D → V in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073276
Natural varianti98 – 981N → I in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073277
Natural varianti98 – 981N → S in CPVT4 and LQT15; the mutant has significantly reduced Ca(2+) affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations. 2 Publications
VAR_069223
Natural varianti130 – 1301D → G in LQT14; reduction in Ca(2+) affinity. 1 Publication
VAR_073278
Natural varianti132 – 1321D → E in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073279
Natural varianti134 – 1341D → H in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073280
Natural varianti136 – 1361Q → P in LQT15; reduction in Ca(2+) affinity. 1 Publication
VAR_073281
Natural varianti142 – 1421F → L in LQT14; reduction in Ca(2+) affinity. 1 Publication
VAR_073282

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04046 mRNA. Translation: AAA51918.1.
M19311 mRNA. Translation: AAA35641.1.
M27319 mRNA. Translation: AAA35635.1.
X52606, X52607, X52608 Genomic DNA. Translation: CAA36839.1. Sequence problems.
U12022, U11886 Genomic DNA. Translation: AAB60644.1.
D45887 mRNA. Translation: BAA08302.1.
U94728, U94725, U94726 Genomic DNA. Translation: AAC83174.1.
BT006818 mRNA. Translation: AAP35464.1.
BT006855 mRNA. Translation: AAP35501.1.
BT009916 mRNA. Translation: AAP88918.1.
CR541990 mRNA. Translation: CAG46787.1.
CR542021 mRNA. Translation: CAG46818.1.
AC006536 Genomic DNA. Translation: AAD45181.1.
AC073283 Genomic DNA. Translation: AAY24085.1.
BC000454 mRNA. Translation: AAH00454.1.
BC003354 mRNA. Translation: AAH03354.1.
BC005137 mRNA. Translation: AAH05137.1.
BC006464 mRNA. Translation: AAH06464.1.
BC008437 mRNA. Translation: AAH08437.1.
BC008597 mRNA. Translation: AAH08597.1.
BC011834 mRNA. Translation: AAH11834.1.
BC017385 mRNA. Translation: AAH17385.1.
BC018677 mRNA. Translation: AAH18677.1.
BC026065 mRNA. Translation: AAH26065.1.
BC047523 mRNA. No translation available.
CCDSiCCDS1832.1.
CCDS33061.1.
CCDS9892.1.
PIRiS48728. MCHU.
RefSeqiNP_001734.1. NM_001743.5.
NP_005175.2. NM_005184.2.
NP_008819.1. NM_006888.4.
UniGeneiHs.282410.
Hs.468442.
Hs.515487.

Genome annotation databases

EnsembliENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.
GeneIDi801.
805.
808.
KEGGihsa:801.
hsa:805.
hsa:808.
UCSCiuc001xyl.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

A question of length - Issue 105 of May 2009

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04046 mRNA. Translation: AAA51918.1.
M19311 mRNA. Translation: AAA35641.1.
M27319 mRNA. Translation: AAA35635.1.
X52606, X52607, X52608 Genomic DNA. Translation: CAA36839.1. Sequence problems.
U12022, U11886 Genomic DNA. Translation: AAB60644.1.
D45887 mRNA. Translation: BAA08302.1.
U94728, U94725, U94726 Genomic DNA. Translation: AAC83174.1.
BT006818 mRNA. Translation: AAP35464.1.
BT006855 mRNA. Translation: AAP35501.1.
BT009916 mRNA. Translation: AAP88918.1.
CR541990 mRNA. Translation: CAG46787.1.
CR542021 mRNA. Translation: CAG46818.1.
AC006536 Genomic DNA. Translation: AAD45181.1.
AC073283 Genomic DNA. Translation: AAY24085.1.
BC000454 mRNA. Translation: AAH00454.1.
BC003354 mRNA. Translation: AAH03354.1.
BC005137 mRNA. Translation: AAH05137.1.
BC006464 mRNA. Translation: AAH06464.1.
BC008437 mRNA. Translation: AAH08437.1.
BC008597 mRNA. Translation: AAH08597.1.
BC011834 mRNA. Translation: AAH11834.1.
BC017385 mRNA. Translation: AAH17385.1.
BC018677 mRNA. Translation: AAH18677.1.
BC026065 mRNA. Translation: AAH26065.1.
BC047523 mRNA. No translation available.
CCDSiCCDS1832.1.
CCDS33061.1.
CCDS9892.1.
PIRiS48728. MCHU.
RefSeqiNP_001734.1. NM_001743.5.
NP_005175.2. NM_005184.2.
NP_008819.1. NM_006888.4.
UniGeneiHs.282410.
Hs.468442.
Hs.515487.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJImodel-A5-148[»]
1CDLX-ray2.00A/B/C/D2-148[»]
1CLLX-ray1.70A2-149[»]
1CTRX-ray2.45A2-149[»]
1IWQX-ray2.00A2-149[»]
1J7ONMR-A2-77[»]
1J7PNMR-A83-149[»]
1K90X-ray2.75D/E/F2-149[»]
1K93X-ray2.95D/E/F6-149[»]
1L7ZX-ray2.30A2-149[»]
1LVCX-ray3.60D/E/F1-149[»]
1NKFNMR-A94-105[»]
1PK0X-ray3.30D/E/F2-148[»]
1S26X-ray3.00D/E/F2-149[»]
1SK6X-ray3.20D/E/F2-149[»]
1SW8NMR-A2-80[»]
1WRZX-ray2.00A1-149[»]
1XFUX-ray3.35O/P/Q/R/S/T1-149[»]
1XFVX-ray3.35O/P/Q/R/S/T1-149[»]
1XFWX-ray3.40O/P/Q/R/S/T1-149[»]
1XFXX-ray3.20O/P/Q/R/S/T1-149[»]
1XFYX-ray3.30O/P/Q/R/S/T1-149[»]
1XFZX-ray3.25O/P/Q/R/S/T1-149[»]
1Y6WX-ray2.40A2-149[»]
1YR5X-ray1.70A2-149[»]
1YRTX-ray2.10B76-149[»]
1YRUX-ray2.50B76-149[»]
1ZOTX-ray2.20B80-148[»]
1ZUZX-ray1.91A1-149[»]
2BE6X-ray2.00A/B/C1-149[»]
2F3YX-ray1.45A2-149[»]
2F3ZX-ray1.60A2-149[»]
2HF5NMR-A47-113[»]
2I08X-ray2.00A3-79[»]
2JZINMR-A2-149[»]
2K0ENMR-A2-149[»]
2K0FNMR-A2-149[»]
2K0JNMR-A3-149[»]
2K61NMR-A2-149[»]
2KNENMR-A2-149[»]
2KUGNMR-A2-77[»]
2KUHNMR-A83-149[»]
2L53NMR-A2-149[»]
2L7LNMR-A2-149[»]
2LGFNMR-A4-149[»]
2LL6NMR-A2-149[»]
2LL7NMR-A2-149[»]
2LQCNMR-A2-78[»]
2LQPNMR-A79-149[»]
2LV6Other-A2-149[»]
2M0JNMR-A2-149[»]
2M0KNMR-A2-149[»]
2M55NMR-A2-149[»]
2MG5NMR-A2-149[»]
2R28X-ray1.86A/B1-149[»]
2V01X-ray2.15A2-149[»]
2V02X-ray2.20A2-149[»]
2VAYX-ray1.94A4-149[»]
2W73X-ray1.45A/B/E/F1-149[»]
2WELX-ray1.90D1-149[»]
2X0GX-ray2.20B2-149[»]
2Y4VX-ray1.80A1-149[»]
3BYAX-ray1.85A2-149[»]
3DVEX-ray2.35A2-149[»]
3DVJX-ray2.80A2-149[»]
3DVKX-ray2.30A2-149[»]
3DVMX-ray2.60A2-149[»]
3EWTX-ray2.40A2-149[»]
3EWVX-ray2.60A2-149[»]
3G43X-ray2.10A/B/C/D2-149[»]
3HR4X-ray2.50B/D/F/H1-149[»]
3J41electron microscopy25.0E/F1-149[»]
3O77X-ray2.35A1-149[»]
3O78X-ray2.60A/B3-149[»]
3OXQX-ray2.55A/B/C/D1-149[»]
3SUIX-ray1.95A1-149[»]
3UCTX-ray1.90A/B2-80[»]
3UCWX-ray1.76A/B/C/D2-80[»]
3UCYX-ray1.80A2-80[»]
4BW7X-ray1.81A/C1-149[»]
4BW8X-ray1.80A/B1-149[»]
4BYFX-ray2.74B/D1-149[»]
4DCKX-ray2.20B1-149[»]
4DJCX-ray1.35A1-149[»]
4GOWX-ray2.60D4-147[»]
4JPZX-ray3.02C/I1-149[»]
4JQ0X-ray3.84C1-149[»]
4L79X-ray2.30B1-149[»]
4LZXX-ray1.50A2-149[»]
4M1LX-ray2.10A2-149[»]
4OVNX-ray2.80A/B/C/D/E1-149[»]
4Q57X-ray1.80A10-74[»]
4Q5UX-ray1.95A1-149[»]
4UMOX-ray3.00C/D1-149[»]
4UPUX-ray2.34A2-149[»]
4V0CX-ray2.86C/D1-149[»]
ProteinModelPortaliP62158.
SMRiP62158. Positions 1-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107252. 370 interactions.
107256. 30 interactions.
107259. 31 interactions.
DIPiDIP-31794N.
IntActiP62158. 201 interactions.
MINTiMINT-4999725.

Chemistry

BindingDBiP62158.
ChEMBLiCHEMBL6093.
DrugBankiDB01429. Aprindine.
DB01244. Bepridil.
DB00477. Chlorpromazine.
DB00527. Cinchocaine.
DB01023. Felodipine.
DB04841. Flunarizine.
DB00623. Fluphenazine.
DB00753. Isoflurane.
DB00836. Loperamide.
DB01065. Melatonin.
DB00622. Nicardipine.
DB01115. Nifedipine.
DB00850. Perphenazine.
DB00925. Phenoxybenzamine.
DB01100. Pimozide.
DB01069. Promethazine.
DB00831. Trifluoperazine.

Protein family/group databases

TCDBi9.C.15.1.1. the animal calmodulin-dependent e.r. secretion pathway (csp) family.

PTM databases

PhosphoSiteiP62158.

Polymorphism and mutation databases

BioMutaiCALM1.
DMDMi49037474.

2D gel databases

DOSAC-COBS-2DPAGEP62158.
OGPiP02593.
SWISS-2DPAGEP62158.

Proteomic databases

MaxQBiP62158.
PaxDbiP62158.
PRIDEiP62158.

Protocols and materials databases

DNASUi801.
805.
808.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272298; ENSP00000272298; ENSG00000143933.
ENST00000291295; ENSP00000291295; ENSG00000160014.
ENST00000356978; ENSP00000349467; ENSG00000198668.
ENST00000596362; ENSP00000472141; ENSG00000160014.
GeneIDi801.
805.
808.
KEGGihsa:801.
hsa:805.
hsa:808.
UCSCiuc001xyl.2. human.

Organism-specific databases

CTDi801.
805.
808.
GeneCardsiGC02M047387.
GC14P090863.
GC19P047105.
GeneReviewsiCALM1.
HGNCiHGNC:1442. CALM1.
HGNC:1445. CALM2.
HGNC:1449. CALM3.
HPAiCAB007790.
CAB018558.
HPA044999.
MIMi114180. gene.
114182. gene.
114183. gene.
614916. phenotype.
616247. phenotype.
616249. phenotype.
neXtProtiNX_P62158.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
PharmGKBiPA26042.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOVERGENiHBG012180.
InParanoidiP62158.
KOiK02183.
OMAiKSHCRIL.
PhylomeDBiP62158.
TreeFamiTF300912.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000143933-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_12477. eNOS activation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_15334. DARPP-32 events.
REACT_15408. Cam-PDE 1 activation.
REACT_15502. CaMK IV-mediated phosphorylation of CREB.
REACT_163834. FCERI mediated Ca+2 mobilization.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_188329. CLEC7A (Dectin-1) induces NFAT activation.
REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
REACT_20558. Smooth Muscle Contraction.
REACT_20642. CREB phosphorylation through the activation of CaMKII.
REACT_20652. Activation of CaMK IV.
REACT_20661. CREB phosphorylation through the activation of CaMKK.
REACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_263982. Ca2+ pathway.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264273. VEGFR2 mediated cell proliferation.
REACT_318. Platelet degranulation.
REACT_355347. RHO GTPases activate PAKs.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_9000. Calmodulin induced events.
REACT_9053. CaM pathway.

Miscellaneous databases

ChiTaRSiCALM1. human.
CALM3. human.
EvolutionaryTraceiP62158.
GeneWikiiCALM2.
CALM3.
Calmodulin_1.
NextBioi3264.
PROiP62158.
SOURCEiSearch...

Gene expression databases

BgeeiP62158.
CleanExiHS_CALM1.
HS_CALM2.
ExpressionAtlasiP62158. baseline and differential.
GenevisibleiP62158. HS.

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. "Isolation and nucleotide sequence of a cDNA encoding human calmodulin."
    Wawrzynczak E.J., Perham R.N.
    Biochem. Int. 9:177-185(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species."
    Sengupta B., Friedberg F., Detera-Wadleigh S.D.
    J. Biol. Chem. 262:16663-16670(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Multiple divergent mRNAs code for a single human calmodulin."
    Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A., Krebs J., Penniston J.T., Carafoli E., Strehler E.E.
    J. Biol. Chem. 263:17055-17062(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Structural organization of the human CaMIII calmodulin gene."
    Koller M., Schnyder B., Strehler E.E.
    Biochim. Biophys. Acta 1087:180-189(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM3).
    Tissue: Blood.
  5. "Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2."
    Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.
    Eur. J. Biochem. 225:71-82(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM1).
    Tissue: Blood.
  6. "Human calmodulin cDNA."
    Kato S.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoma.
  7. "Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3."
    Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F., Tolon R., Strehler E.E.
    Cell Calcium 23:323-338(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM2).
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1; CALM2 AND CALM3).
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM2).
  10. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM1).
  11. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM2).
  12. "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] (CALM1; CALM2 AND CALM3).
    Tissue: Brain, Lung, Lymph, Placenta and Urinary bladder.
  13. Cited for: PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, METHYLATION AT LYS-116.
    Tissue: Brain.
  14. Bienvenut W.V., Bensaad K., Vousden K.H.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  15. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-31; 77-107 AND 128-149, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  16. "Structural basis for activation of the titin kinase domain during myofibrillogenesis."
    Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., Wilmanns M., Gautel M.
    Nature 395:863-869(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTN.
  17. "Recombinant expression, purification and characterisation of the HMG domain of human SRY."
    Kelly S., Yotis J., Macris M., Harley V.
    Protein Pept. Lett. 10:281-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  18. "Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6."
    Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.
    J. Biol. Chem. 280:35967-35973(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP6.
  19. "Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal."
    Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.
    Mol. Endocrinol. 19:1884-1892(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRY.
  20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
    Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
    Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCP110, SUBCELLULAR LOCATION.
  22. "Cep97 and CP110 suppress a cilia assembly program."
    Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.
    Cell 130:678-690(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEP97 AND CCP110.
  23. "S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
    Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
    J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RYR1 AND RYR2.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND TYR-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex."
    Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.
    J. Biol. Chem. 285:22658-22665(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK5RAP2.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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: INTERACTION WITH ORAI1.
  32. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  33. "Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
    Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
    Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCHO1.
  34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  35. Cited for: INVOLVEMENT IN LQT14, VARIANTS LQT14 GLY-130 AND LEU-142, CHARACTERIZATION OF VARIANTS LQT14 GLY-130 AND LEU-142, INVOLVEMENT IN LQT15, VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96.
  36. Cited for: INVOLVEMENT IN LQT15, VARIANTS LQT15 ILE-98; SER-98; GLU-132; HIS-134 AND PRO-136, CHARACTERIZATION OF VARIANTS LQT15 ILE-98; GLU-132; HIS-134 AND PRO-136.
  37. "A mutation in CALM1 encoding calmodulin in familial idiopathic ventricular fibrillation in childhood and adolescence."
    Marsman R.F., Barc J., Beekman L., Alders M., Dooijes D., van den Wijngaard A., Ratbi I., Sefiani A., Bhuiyan Z.A., Wilde A.A., Bezzina C.R.
    J. Am. Coll. Cardiol. 63:259-266(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LQT14, VARIANT LQT14 LEU-90.
  38. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  39. Cited for: STRUCTURE BY NMR OF 95-104.
  40. "Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains."
    Chou J.J., Li S., Klee C.B., Bax A.
    Nat. Struct. Biol. 8:990-997(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-77 AND 83-149.
  41. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  42. "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).
  43. "Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
    Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
    Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149.
  44. "Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins."
    Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A., Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.
    EMBO J. 21:6721-6732(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
  45. "Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin."
    Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.
    Nat. Struct. Biol. 10:226-231(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS.
  46. "Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex."
    Van Petegem F., Chatelain F.C., Minor D.L. Jr.
    Nat. Struct. Mol. Biol. 12:1108-1115(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C.
  47. "Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor."
    Shen Y., Zhukovskaya N.L., Guo Q., Florian J., Tang W.-J.
    EMBO J. 24:929-941(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
  48. "Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5."
    Chagot B., Chazin W.J.
    J. Mol. Biol. 406:106-119(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH SCN5A.
  49. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (25 ANGSTROMS) IN COMPLEX WITH MIP, FUNCTION, INTERACTION WITH MIP.
  50. Cited for: VARIANTS CPVT4 ILE-54 AND SER-98, CHARACTERIZATION OF VARIANTS CPVT4 ILE-54 AND SER-98.

Entry informationi

Entry nameiCALM_HUMAN
AccessioniPrimary (citable) accession number: P62158
Secondary accession number(s): P02593
, P70667, P99014, Q13942, Q53S29, Q61379, Q61380, Q96HK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein has four functional calcium-binding sites.

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  9. 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.