Calmodulin 1

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]
End	90,408,268 bp[1]
RNA expression pattern
	Top expressed in
	internal globus pallidus; ; parietal lobe; ; postcentral gyrus; ; pons; ; frontal pole; ; orbitofrontal cortex; ; superior vestibular nucleus; ; external globus pallidus; ; entorhinal cortex; ; middle temporal gyrus;
	n/a
	More reference expression data
	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;
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 membrane; protein-containing complex; myelin sheath;
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;
	Sources:Amigo / QuickGO
Orthologs
	801
	n/a
	ENSG00000198668
	n/a
	P0DP23; P0DP24
	n/a
	NM_001166106; NM_006888; NM_001363669; NM_001363670
	n/a
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
	Wikidata
View/Edit Human

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

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 149 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:

References

GRCh38: Ensembl release 89: ENSG00000198668 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Wawrzynczak EJ, Perham RN (August 1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987.
"Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)".
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.
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. Bibcode:2004PNAS..101..464C. doi:10.1073/pnas.0307161101. PMC 327170. PMID 14695896.
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.
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.
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.
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. Bibcode:2003PNAS..100.8002N. doi:10.1073/pnas.1337252100. PMC 164702. PMID 12808128.

External links

UniProt.[1] Calm1 Human Gene

"CALM1 Gene", Definitions, Qeios, 2020-02-07, retrieved 2023-10-16

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000198668 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid6385987-3] 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)".

[pmid12221128-5] 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.

[pmid14695896-6] 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. Bibcode:2004PNAS..101..464C. doi:10.1073/pnas.0307161101. PMC 327170. PMID 14695896.

[pmid12446675-7] 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.

[pmid11734550-8] 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.

[pmid12051765-9] 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.

[pmid12808128-10] 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. Bibcode:2003PNAS..100.8002N. doi:10.1073/pnas.1337252100. PMC 164702. PMID 12808128.

[11] "CALM1 Gene", Definitions, Qeios, 2020-02-07, retrieved 2023-10-16

Calmodulin 1

Function

Interactions

References

Further reading

External links