CALM3

CALM3
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2VAY, 1Y6W, 4JPZ, 3UCY, 1WRZ, 4G28, 1ZOT, 1YRT, 1IQ5, 1CDL, 2LL6, 3HR4, 4BW7, 4BW8, 1YR5, 4J9Y, 4LZX, 1L7Z, 1ZUZ, 2BE6, 2V01, 1XFV, 2M55, 1CTR, 2I08, 2MG5, 2R28, 3O77, 4UPU, 2L7L, 2K0F, 2M0K, 4V0C, 1SW8, 2WEL, 3DVK, 2M0J, 3DVM, 2KUH, 1K90, 1K93, 4G27, 1CLL, 2KUG, 1XFX, 4DJC, 2LQC, 2LQP, 4L79, 2W73, 2LV6, 1NKF, 2JZI, 3UCT, 4GOW, 1J7O, 1PK0, 4Q5U, 2V02, 3BYA, 4Q57, 2KNE, 1YRU, 2Y4V, 2L53, 2F3Y, 3O78, 1LVC, 4M1L, 2K0E, 1S26, 4DCK, 1XFW, 3SUI, 2X0G, 3EWV, 1XFY, 2LL7, 4OVN, 3J41, 2BKI, 1SK6, 3DVJ, 3UCW, 2LGF, 4UMO, 3DVE, 4JQ0, 3OXQ, 2K61, 1XFU, 3SJQ, 2K0J, 4BYF, 1J7P, 3G43, 3EWT, 4J9Z, 1XFZ, 2F3Z, 1IWQ, 2N6A, 2HF5, 2N27, 4ZLK, 5COC,%%s2HF5
Identifiers
Aliases	CALM3, HEL-S-72, PHKD, PHKD3, calmodulin 3 (phosphorylase kinase, delta), CaM, CaMIII, calmodulin 3, CAM1, CAMB, CALM, CAM2, CPVT6, LQT16
External IDs	OMIM: 114183; HomoloGene: 134804; GeneCards: CALM3; OMA:CALM3 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.32 Start 46,601,074 bp End 46,610,782 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in prefrontal cortex right frontal lobe left testis right testis right hemisphere of cerebellum nucleus accumbens amygdala cingulate gyrus anterior cingulate cortex Brodmann area 9 n/a More reference expression data BioGPS n/a
Gene ontology Molecular function calcium ion binding protein binding calcium channel inhibitor activity protein kinase binding titin binding protein serine/threonine kinase activator activity transmembrane transporter binding metal ion binding protein phosphatase activator activity adenylate cyclase binding disordered domain specific binding inositol-1,4,5-trisphosphate 3-kinase activity ligand-gated ion channel activity adenylate cyclase activator activity protein domain specific binding nitric-oxide synthase regulator activity type 3 metabotropic glutamate receptor binding N-terminal myristoylation domain binding phosphatidylinositol 3-kinase binding protein N-terminus binding calcium-dependent protein binding nitric-oxide synthase binding kinase activity Cellular component cytoplasm cytosol calcium channel complex extracellular region spindle microtubule neuron projection cytoskeleton nucleus centrosome voltage-gated potassium channel complex extracellular exosome spindle pole growth cone plasma membrane spindle sarcomere nucleoplasm vesicle postsynaptic density catalytic complex microtubule organizing center synaptic vesicle membrane mitochondrial membranes protein-containing complex myelin sheath intracellular anatomical structure Biological process muscle contraction response to amphetamine positive regulation of protein serine/threonine kinase activity detection of calcium ion Fc-epsilon receptor signaling pathway positive regulation of phosphoprotein phosphatase activity G2/M transition of mitotic cell cycle regulation of high voltage-gated calcium channel activity positive regulation of DNA binding substantia nigra development positive regulation of protein dephosphorylation inositol phosphate metabolic process positive regulation of nitric-oxide synthase activity glycogen catabolic process positive regulation of cyclic-nucleotide phosphodiesterase activity G protein-coupled receptor signaling pathway regulation of cytokinesis regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion regulation of rhodopsin mediated signaling pathway response to corticosterone negative regulation of peptidyl-threonine phosphorylation activation of adenylate cyclase activity regulation of heart rate positive regulation of ryanodine-sensitive calcium-release channel activity response to calcium ion regulation of ryanodine-sensitive calcium-release channel activity regulation of nitric-oxide synthase activity platelet degranulation negative regulation of ryanodine-sensitive calcium-release channel activity MAPK cascade positive regulation of peptidyl-threonine phosphorylation positive regulation of protein autophosphorylation regulation of cardiac muscle contraction regulation of cell communication by electrical coupling involved in cardiac conduction regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum calcium-mediated signaling ion transmembrane transport Wnt signaling pathway, calcium modulating pathway positive regulation of GTPase activity protein methylation establishment of protein localization to membrane establishment of protein localization to mitochondrial membrane regulation of synaptic vesicle endocytosis regulation of synaptic vesicle exocytosis phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 808 n/a Ensembl ENSG00000160014 n/a UniProt P0DP23 Q96HY3 P0DP24 n/a RefSeq (mRNA) NM_001329921 NM_001329922 NM_001329923 NM_001329924 NM_001329925 NM_001329926 NM_005184 n/a RefSeq (protein) NP_001292553 NP_001292554 NP_001292555 NP_001734 NP_001316850 NP_001316851 NP_001316852 NP_001316853 NP_001316854 NP_001316855 NP_005175 NP_008819 NP_001292554.1 NP_001292555.1 NP_001350598 NP_001350599 NP_008819 NP_001292553 NP_001292554 NP_001292555 NP_001734 NP_001316850 NP_001316851 NP_001316852 NP_001316853 NP_001316854 NP_001316855 NP_005175 n/a Location (UCSC) Chr 19: 46.6 – 46.61 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

Calmodulin 3 is a protein that in humans is encoded by the CALM3 gene.

Further reading

• Reed GJ, Boczek NJ, Etheridge SP, Ackerman MJ (2015). "CALM3 mutation associated with long QT syndrome". Heart Rhythm. 12 (2): 419–22. doi:10.1016/j.hrthm.2014.10.035. PMC 4907373. PMID 25460178.
• Zhang M, Yuan T (1999). "Molecular mechanisms of calmodulin's functional versatility". Biochemistry and Cell Biology. 76 (2–3): 313–23. doi:10.1139/bcb-76-2-3-313. PMID 9923700.
• Gusev NB (2002). "Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation". Biokhimiya. 66 (10): 1112–21. doi:10.1023/A:1012480829618. PMID 11736632.
• Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications". European Journal of Biochemistry. 269 (15): 3619–31. doi:10.1046/j.1432-1033.2002.03038.x. hdl:10261/79981. PMID 12153558.
• Chattopadhyaya R, Meador WE, Means AR, Quiocho FA (1993). "Calmodulin structure refined at 1.7 A resolution". Journal of Molecular Biology. 228 (4): 1177–92. doi:10.1016/0022-2836(92)90324-D. PMID 1474585.
• Koller M, Schnyder B, Strehler EE (1990). "Structural organization of the human CaMIII calmodulin gene". Biochimica et Biophysica Acta. 1087 (2): 180–9. doi:10.1016/0167-4781(90)90203-e. PMID 2223880.
• Pegues JC, Friedberg F (1990). "Multiple mRNAs encoding human calmodulin". Biochemical and Biophysical Research Communications. 172 (3): 1145–9. doi:10.1016/0006-291X(90)91567-C. PMID 2244899.
• SenGupta B, Friedberg F, Detera-Wadleigh SD (1988). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". Journal of Biological Chemistry. 262 (34): 16663–70. PMID 2445749.
• Baudier J, Mochly-Rosen D, Newton A, et al. (1987). "Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C". Biochemistry. 26 (10): 2886–93. doi:10.1021/bi00384a033. PMID 3111527.
• Fischer R, Koller M, Flura M, et al. (1988). "Multiple divergent mRNAs code for a single human calmodulin". J. Biol. Chem. 263 (32): 17055–62. PMID 3182832.
• Wawrzynczak EJ, Perham RN (1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987.
• Sasagawa T, Ericsson LH, Walsh KA, et al. (1982). "Complete amino acid sequence of human brain calmodulin". Biochemistry. 21 (10): 2565–9. doi:10.1021/bi00539a041. PMID 7093203.
• Cook WJ, Walter LJ, Walter MR (1995). "Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex". Biochemistry. 33 (51): 15259–65. doi:10.1021/bi00255a006. PMID 7803388.
• Rhyner JA, Ottiger M, Wicki R, et al. (1994). "Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2". Eur. J. Biochem. 225 (1): 71–82. doi:10.1111/j.1432-1033.1994.00071.x. PMID 7925473.
• Srinivas SK, Srinivas RV, Anantharamaiah GM, et al. (1993). "Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins". J. Biol. Chem. 268 (30): 22895–9. PMID 8226798.
• Miller MA, Mietzner TA, Cloyd MW, et al. (1994). "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein". AIDS Research and Human Retroviruses. 9 (11): 1057–66. doi:10.1089/aid.1993.9.1057. PMID 8312049.
• Berchtold MW, Egli R, Rhyner JA, et al. (1993). "Localization of the human bona fide calmodulin genes CALM1, CALM2, and CALM3 to chromosomes 14q24-q31, 2p21.1-p21.3, and 19q13.2-q13.3". Genomics. 16 (2): 461–5. doi:10.1006/geno.1993.1211. PMID 8314583.
• Koller M, Strehler EE (1993). "Functional analysis of the promoters of the human CaMIII calmodulin gene and of the intronless gene coding for a calmodulin-like protein". Biochim. Biophys. Acta. 1163 (1): 1–9. doi:10.1016/0167-4838(93)90271-R. PMID 8476923.
• Radding W, Pan ZQ, Hunter E, et al. (1996). "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin". Biochem. Biophys. Res. Commun. 218 (1): 192–7. doi:10.1006/bbrc.1996.0034. PMID 8573130.
• Pan Z, Radding W, Zhou T, et al. (1996). "Role of calmodulin in HIV-potentiated Fas-mediated apoptosis". American Journal of Pathology. 149 (3): 903–10. PMC 1865159. PMID 8780394.
• Sasaki M, Uchiyama J, Ishikawa H, et al. (1996). "Induction of apoptosis by calmodulin-dependent intracellular Ca2+ elevation in CD4+ cells expressing gp 160 of HIV". Virology. 224 (1): 18–24. doi:10.1006/viro.1996.0502. PMID 8862395.

External links

• Human CALM3 genome location and CALM3 gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: P0DP23 (Calmodulin-1) at the PDBe-KB.
• Overview of all the structural information available in the PDB for UniProt: P0DP24 (Calmodulin-2) at the PDBe-KB.