Calmodulin 1

Calmodulin 1 is a protein that in humans is encoded by the CALM1 gene.[3]

CALM1
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
Identifiers
Aliases	CALM1, CALML2, CAMI, CPVT4, DD132, PHKD, caM, LQT14, Calmodulin 1, calmodulin 1 (phosphorylase kinase, delta), CAMC, CAMB, CAMIII, CAM3, CAM2
External IDs	OMIM: 114180 HomoloGene: 134804 GeneCards: CALM1
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q32.11 Start 90,396,502 bp[1] End 90,408,268 bp[1]
Gene ontology Molecular function • calcium ion binding • GO:0001948 protein binding • calcium channel inhibitor activity • protein kinase binding • titin binding • protein serine/threonine kinase activator activity • ion channel binding • metal ion binding • protein phosphatase activator activity • adenylate cyclase binding • disordered domain specific binding • Ras guanyl-nucleotide exchange factor activity • 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 Cellular component • cytoplasm • cytosol • calcium channel complex • extracellular region • spindle microtubule • neuron projection • cytoskeleton • cell nucleus • centrosome • voltage-gated potassium channel complex • extracellular exosome • spindle pole • growth cone • cell membrane • spindle • sarcomere • nucleoplasm • vesicle • GO:0097483, GO:0097481 postsynaptic density • catalytic complex • microtubule organizing center • synaptic vesicle membrane • mitochondrial membranes • macromolecular complex • myelin 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 • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 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 Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	801	n/a
Ensembl	ENSG00000198668	n/a
UniProt	P0DP23 P0DP24	n/a
RefSeq (mRNA)	NM_001166106 NM_006888 NM_001363669 NM_001363670	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_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 14: 90.4 – 90.41 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

Calmodulin 1 is the archetype of the family of calcium-modulated (calmodulin) proteins of which nearly 20 members have been found. They are identified by their occurrence in the cytosol or on membranes facing the cytosol and by a high affinity for calcium. Calmodulin contains 148 amino acids and has 4 calcium-binding EF hand motifs. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.[4]

Interactions

Calmodulin 1 has been shown to interact with:

• AKAP9,[5]
• Androgen receptor,[6]
• IQGAP1,[7][8]
• PPEF1,[9] and
• TRPV1.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000198668 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Wawrzynczak EJ, Perham RN (August 1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987.
4. "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)".
5. Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y (Sep 2002). "Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex". Mol. Biol. Cell. 13 (9): 3235–45. doi:10.1091/mbc.E02-02-0112. PMC 124155. PMID 12221128.
6. Cifuentes E, Mataraza JM, Yoshida BA, Menon M, Sacks DB, Barrack ER, Reddy GP (Jan 2004). "Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells". Proc. Natl. Acad. Sci. U.S.A. 101 (2): 464–9. doi:10.1073/pnas.0307161101. PMC 327170. PMID 14695896.
7. Li Z, Sacks DB (Feb 2003). "Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1". J. Biol. Chem. 278 (6): 4347–52. doi:10.1074/jbc.M208579200. PMID 12446675.
8. Briggs MW, Li Z, Sacks DB (Mar 2002). "IQGAP1-mediated stimulation of transcriptional co-activation by beta-catenin is modulated by calmodulin". J. Biol. Chem. 277 (9): 7453–65. doi:10.1074/jbc.M104315200. PMID 11734550.
9. Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N (May 2002). "Protein Ser/Thr phosphatases PPEF interact with calmodulin". Biochem. Biophys. Res. Commun. 293 (3): 1047–52. doi:10.1016/S0006-291X(02)00338-8. PMID 12051765.
10. Numazaki M, Tominaga T, Takeuchi K, Murayama N, Toyooka H, Tominaga M (Jun 2003). "Structural determinant of TRPV1 desensitization interacts with calmodulin". Proc. Natl. Acad. Sci. U.S.A. 100 (13): 8002–6. doi:10.1073/pnas.1337252100. PMC 164702. PMID 12808128.

Further reading

• Zhang M, Yuan T (1999). "Molecular mechanisms of calmodulin's functional versatility". Biochem. Cell Biol. 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". Biochemistry Mosc. 66 (10): 1112–21. doi:10.1023/A:1012480829618. PMID 11736632.
• Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications". Eur. J. Biochem. 269 (15): 3619–31. doi:10.1046/j.1432-1033.2002.03038.x. hdl:10261/79981. PMID 12153558.
• Trudeau MC, Zagotta WN (2003). "Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels". J. Biol. Chem. 278 (21): 18705–8. doi:10.1074/jbc.R300001200. PMID 12626507.

External links

• UniProt entry